| Type |
Details |
Score |
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
5210
|
| Description: |
Disease resistance protein (TIR-NBS-LRR class) family; IPR000157 (Toll/interleukin-1 receptor homology (TIR) domain), IPR000767 (Disease resistance protein), IPR027417 (P-loop containing nucleoside triphosphate hydrolase); GO:0000166 (nucleotide binding), GO:0005515 (protein binding), GO:0006952 (defense response), GO:0007165 (signal transduction), GO:0017111 (nucleoside-triphosphatase activity), GO:0043531 (ADP binding) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
2274
|
| Description: |
phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN-like isoform X2 [Glycine max]; IPR000008 (C2 domain), IPR014019 (Phosphatase tensin type); GO:0004725 (protein tyrosine phosphatase activity), GO:0005515 (protein binding), GO:0006470 (protein dephosphorylation), GO:0008138 (protein tyrosine/serine/threonine phosphatase activity), GO:0016311 (dephosphorylation), GO:0016791 (phosphatase activity) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
7597
|
| Description: |
chromodomain-helicase-DNA-binding protein 1-like isoform X2 [Glycine max]; IPR001650 (Helicase, C-terminal), IPR013083 (Zinc finger, RING/FYVE/PHD-type), IPR016197 (Chromo domain-like), IPR027417 (P-loop containing nucleoside triphosphate hydrolase); GO:0003676 (nucleic acid binding), GO:0004386 (helicase activity), GO:0005515 (protein binding), GO:0005524 (ATP binding), GO:0008270 (zinc ion binding) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
1722
|
| Description: |
magnesium transporter 9; IPR002523 (Mg2+ transporter protein, CorA-like/Zinc transport protein ZntB), IPR026573 (Magnesium transporter MRS2/LPE10); GO:0015095 (magnesium ion transmembrane transporter activity), GO:0015693 (magnesium ion transport), GO:0016020 (membrane), GO:0030001 (metal ion transport), GO:0046873 (metal ion transmembrane transporter activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer echinospermum |
| Strain: |
S2Drd065 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
7111
|
| Description: |
ABC transporter family protein (ATP-binding component); IPR011527 (ABC transporter type 1, transmembrane domain), IPR027417 (P-loop containing nucleoside triphosphate hydrolase); GO:0000166 (nucleotide binding), GO:0005524 (ATP binding), GO:0006810 (transport), GO:0016021 (integral component of membrane), GO:0016887 (ATPase activity), GO:0017111 (nucleoside-triphosphatase activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer echinospermum |
| Strain: |
S2Drd065 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
414
|
| Description: |
Unknown protein; IPR001806 (Small GTPase superfamily), IPR005225 (Small GTP-binding protein domain), IPR027417 (P-loop containing nucleoside triphosphate hydrolase); GO:0005525 (GTP binding), GO:0005622 (intracellular), GO:0006184 (GTP catabolic process), GO:0007165 (signal transduction), GO:0007264 (small GTPase mediated signal transduction), GO:0015031 (protein transport), GO:0016020 (membrane) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
1233
|
| Description: |
uncharacterized protein LOC100815444 isoform X8 [Glycine max]; IPR001878 (Zinc finger, CCHC-type), IPR012923 (Replication fork protection component Swi3); GO:0003676 (nucleic acid binding), GO:0005634 (nucleus), GO:0006974 (cellular response to DNA damage stimulus), GO:0007049 (cell cycle), GO:0008270 (zinc ion binding), GO:0048478 (replication fork protection) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
3172
|
| Description: |
protein kinase family protein; IPR001611 (Leucine-rich repeat), IPR011009 (Protein kinase-like domain), IPR013210 (Leucine-rich repeat-containing N-terminal, type 2), IPR013320 (Concanavalin A-like lectin/glucanase, subgroup); GO:0004672 (protein kinase activity), GO:0004674 (protein serine/threonine kinase activity), GO:0005515 (protein binding), GO:0005524 (ATP binding), GO:0006468 (protein phosphorylation) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
4677
|
| Description: |
ABC transporter family protein (ATP-binding component); IPR011527 (ABC transporter type 1, transmembrane domain), IPR027417 (P-loop containing nucleoside triphosphate hydrolase); GO:0000166 (nucleotide binding), GO:0005524 (ATP binding), GO:0006810 (transport), GO:0016021 (integral component of membrane), GO:0016887 (ATPase activity), GO:0017111 (nucleoside-triphosphatase activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
3242
|
| Description: |
Disease resistance protein (TIR-NBS-LRR class) family; IPR000157 (Toll/interleukin-1 receptor homology (TIR) domain), IPR000767 (Disease resistance protein), IPR027417 (P-loop containing nucleoside triphosphate hydrolase); GO:0000166 (nucleotide binding), GO:0005515 (protein binding), GO:0006952 (defense response), GO:0007165 (signal transduction), GO:0017111 (nucleoside-triphosphatase activity), GO:0043531 (ADP binding) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
2495
|
| Description: |
receptor-like protein kinase 4; IPR001611 (Leucine-rich repeat), IPR003591 (Leucine-rich repeat, typical subtype), IPR011009 (Protein kinase-like domain), IPR013210 (Leucine-rich repeat-containing N-terminal, type 2), IPR013320 (Concanavalin A-like lectin/glucanase, subgroup); GO:0004672 (protein kinase activity), GO:0005515 (protein binding), GO:0005524 (ATP binding), GO:0006468 (protein phosphorylation) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
1655
|
| Description: |
magnesium transporter 3; IPR002523 (Mg2+ transporter protein, CorA-like/Zinc transport protein ZntB), IPR026573 (Magnesium transporter MRS2/LPE10); GO:0015095 (magnesium ion transmembrane transporter activity), GO:0015693 (magnesium ion transport), GO:0016020 (membrane), GO:0030001 (metal ion transport), GO:0046873 (metal ion transmembrane transporter activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
2414
|
| Description: |
asparagine-tRNA ligase; IPR009068 (S15/NS1, RNA-binding), IPR018150 (Aminoacyl-tRNA synthetase, class II (D/K/N)-like); GO:0000166 (nucleotide binding), GO:0003676 (nucleic acid binding), GO:0004812 (aminoacyl-tRNA ligase activity), GO:0004816 (asparagine-tRNA ligase activity), GO:0005524 (ATP binding), GO:0005737 (cytoplasm), GO:0006418 (tRNA aminoacylation for protein translation), GO:0006421 (asparaginyl-tRNA aminoacylation) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
1639
|
| Description: |
magnesium transporter 3; IPR002523 (Mg2+ transporter protein, CorA-like/Zinc transport protein ZntB), IPR026573 (Magnesium transporter MRS2/LPE10); GO:0015095 (magnesium ion transmembrane transporter activity), GO:0015693 (magnesium ion transport), GO:0016020 (membrane), GO:0030001 (metal ion transport), GO:0046873 (metal ion transmembrane transporter activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
3975
|
| Description: |
Disease resistance protein (TIR-NBS-LRR class) family; IPR000157 (Toll/interleukin-1 receptor homology (TIR) domain), IPR000767 (Disease resistance protein), IPR012417 (Calmodulin-binding domain, plant), IPR027417 (P-loop containing nucleoside triphosphate hydrolase); GO:0005515 (protein binding), GO:0005516 (calmodulin binding), GO:0006952 (defense response), GO:0007165 (signal transduction), GO:0043531 (ADP binding) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
6300
|
| Description: |
chromodomain-helicase-DNA-binding protein 1-like isoform X2 [Glycine max]; IPR000330 (SNF2-related), IPR001650 (Helicase, C-terminal), IPR016197 (Chromo domain-like), IPR025260 (Domain of unknown function DUF4208), IPR027417 (P-loop containing nucleoside triphosphate hydrolase); GO:0003676 (nucleic acid binding), GO:0003677 (DNA binding), GO:0004386 (helicase activity), GO:0005524 (ATP binding) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
1906
|
| Description: |
lupus La protein homolog A-like isoform X2 [Glycine max]; IPR002344 (Lupus La protein), IPR011991 (Winged helix-turn-helix DNA-binding domain), IPR012677 (Nucleotide-binding, alpha-beta plait); GO:0000166 (nucleotide binding), GO:0003676 (nucleic acid binding), GO:0003723 (RNA binding), GO:0005634 (nucleus), GO:0006396 (RNA processing), GO:0030529 (ribonucleoprotein complex) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
5675
|
| Description: |
ABC transporter family protein (ATP-binding component); IPR011527 (ABC transporter type 1, transmembrane domain), IPR027417 (P-loop containing nucleoside triphosphate hydrolase); GO:0000166 (nucleotide binding), GO:0005524 (ATP binding), GO:0006810 (transport), GO:0016021 (integral component of membrane), GO:0016887 (ATPase activity), GO:0017111 (nucleoside-triphosphatase activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
1197
|
| Description: |
uncharacterized protein LOC100815444 isoform X6 [Glycine max]; IPR001878 (Zinc finger, CCHC-type), IPR012923 (Replication fork protection component Swi3); GO:0003676 (nucleic acid binding), GO:0005634 (nucleus), GO:0006974 (cellular response to DNA damage stimulus), GO:0007049 (cell cycle), GO:0008270 (zinc ion binding), GO:0048478 (replication fork protection) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
1383
|
| Description: |
E3 ubiquitin-protein ligase SINAT3-like [Glycine max]; IPR004162 (E3 ubiquitin-protein ligase SINA like), IPR013083 (Zinc finger, RING/FYVE/PHD-type); GO:0004842 (ubiquitin-protein ligase activity), GO:0005515 (protein binding), GO:0005634 (nucleus), GO:0006511 (ubiquitin-dependent protein catabolic process), GO:0007275 (multicellular organismal development), GO:0008270 (zinc ion binding), GO:0016567 (protein ubiquitination) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
7990
|
| Description: |
ABC transporter family protein (ATP-binding component); IPR011527 (ABC transporter type 1, transmembrane domain), IPR027417 (P-loop containing nucleoside triphosphate hydrolase); GO:0000166 (nucleotide binding), GO:0005524 (ATP binding), GO:0006810 (transport), GO:0016021 (integral component of membrane), GO:0016887 (ATPase activity), GO:0017111 (nucleoside-triphosphatase activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
1972
|
| Description: |
lupus La protein homolog A-like isoform X2 [Glycine max]; IPR002344 (Lupus La protein), IPR011991 (Winged helix-turn-helix DNA-binding domain), IPR012677 (Nucleotide-binding, alpha-beta plait); GO:0000166 (nucleotide binding), GO:0003676 (nucleic acid binding), GO:0003723 (RNA binding), GO:0005634 (nucleus), GO:0006396 (RNA processing), GO:0030529 (ribonucleoprotein complex) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
6950
|
| Description: |
Disease resistance protein (TIR-NBS-LRR class) family; IPR000157 (Toll/interleukin-1 receptor homology (TIR) domain), IPR000767 (Disease resistance protein), IPR027417 (P-loop containing nucleoside triphosphate hydrolase); GO:0000166 (nucleotide binding), GO:0005515 (protein binding), GO:0006952 (defense response), GO:0007165 (signal transduction), GO:0017111 (nucleoside-triphosphatase activity), GO:0043531 (ADP binding) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
3723
|
| Description: |
disease resistance protein (TIR-NBS-LRR class), putative; IPR000157 (Toll/interleukin-1 receptor homology (TIR) domain), IPR000767 (Disease resistance protein), IPR027417 (P-loop containing nucleoside triphosphate hydrolase); GO:0000166 (nucleotide binding), GO:0005515 (protein binding), GO:0006952 (defense response), GO:0007165 (signal transduction), GO:0017111 (nucleoside-triphosphatase activity), GO:0043531 (ADP binding) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
2892
|
| Description: |
E3 ubiquitin-protein ligase SINAT3-like [Glycine max]; IPR004162 (E3 ubiquitin-protein ligase SINA like), IPR013083 (Zinc finger, RING/FYVE/PHD-type); GO:0004842 (ubiquitin-protein ligase activity), GO:0005515 (protein binding), GO:0005634 (nucleus), GO:0006511 (ubiquitin-dependent protein catabolic process), GO:0007275 (multicellular organismal development), GO:0008270 (zinc ion binding), GO:0016567 (protein ubiquitination) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
6120
|
| Description: |
dedicator of cytokinesis protein 7-like isoform X1 [Glycine max]; IPR010703 (Dedicator of cytokinesis C-terminal), IPR016024 (Armadillo-type fold), IPR026791 (Dedicator of cytokinesis), IPR027007 (DHR-1 domain), IPR027357 (DHR-2 domain); GO:0005085 (guanyl-nucleotide exchange factor activity), GO:0005488 (binding), GO:0007264 (small GTPase mediated signal transduction) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
414
|
| Description: |
Unknown protein; IPR001806 (Small GTPase superfamily), IPR005225 (Small GTP-binding protein domain), IPR027417 (P-loop containing nucleoside triphosphate hydrolase); GO:0005525 (GTP binding), GO:0005622 (intracellular), GO:0006184 (GTP catabolic process), GO:0007165 (signal transduction), GO:0007264 (small GTPase mediated signal transduction), GO:0015031 (protein transport), GO:0016020 (membrane) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
2607
|
| Description: |
ABC transporter family protein (ATP-binding component); IPR011527 (ABC transporter type 1, transmembrane domain), IPR027417 (P-loop containing nucleoside triphosphate hydrolase); GO:0000166 (nucleotide binding), GO:0005524 (ATP binding), GO:0006810 (transport), GO:0016021 (integral component of membrane), GO:0016887 (ATPase activity), GO:0017111 (nucleoside-triphosphatase activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
456
|
| Description: |
Unknown protein; IPR001806 (Small GTPase superfamily), IPR005225 (Small GTP-binding protein domain), IPR027417 (P-loop containing nucleoside triphosphate hydrolase); GO:0005525 (GTP binding), GO:0005622 (intracellular), GO:0006184 (GTP catabolic process), GO:0007165 (signal transduction), GO:0007264 (small GTPase mediated signal transduction), GO:0015031 (protein transport), GO:0016020 (membrane) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
3528
|
| Description: |
Disease resistance protein (TIR-NBS-LRR class) family; IPR000157 (Toll/interleukin-1 receptor homology (TIR) domain), IPR000767 (Disease resistance protein), IPR027417 (P-loop containing nucleoside triphosphate hydrolase); GO:0000166 (nucleotide binding), GO:0005515 (protein binding), GO:0006952 (defense response), GO:0007165 (signal transduction), GO:0017111 (nucleoside-triphosphatase activity), GO:0043531 (ADP binding) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
1850
|
| Description: |
magnesium transporter 9; IPR002523 (Mg2+ transporter protein, CorA-like/Zinc transport protein ZntB), IPR026573 (Magnesium transporter MRS2/LPE10); GO:0015095 (magnesium ion transmembrane transporter activity), GO:0015693 (magnesium ion transport), GO:0016020 (membrane), GO:0030001 (metal ion transport), GO:0046873 (metal ion transmembrane transporter activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
3413
|
| Description: |
kinesin-related protein 11-like isoform X2 [Glycine max]; IPR001752 (Kinesin, motor domain), IPR010994 (RuvA domain 2-like), IPR027417 (P-loop containing nucleoside triphosphate hydrolase), IPR027640 (Kinesin-like protein); GO:0003777 (microtubule motor activity), GO:0005524 (ATP binding), GO:0005871 (kinesin complex), GO:0007018 (microtubule-based movement), GO:0008017 (microtubule binding) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
1982
|
| Description: |
probable 26S proteasome non-ATPase regulatory subunit 3-like [Glycine max]; IPR000717 (Proteasome component (PCI) domain), IPR013143 (PCI/PINT associated module), IPR013586 (26S proteasome regulatory subunit, C-terminal); GO:0000502 (proteasome complex), GO:0005515 (protein binding), GO:0030234 (enzyme regulator activity), GO:0042176 (regulation of protein catabolic process) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
3040
|
| Description: |
ABC transporter family protein (ATP-binding component); IPR011527 (ABC transporter type 1, transmembrane domain), IPR027417 (P-loop containing nucleoside triphosphate hydrolase); GO:0000166 (nucleotide binding), GO:0005524 (ATP binding), GO:0006810 (transport), GO:0016021 (integral component of membrane), GO:0016887 (ATPase activity), GO:0017111 (nucleoside-triphosphatase activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
249
|
| Description: |
magnesium transporter 2; IPR002523 (Mg2+ transporter protein, CorA-like/Zinc transport protein ZntB), IPR026573 (Magnesium transporter MRS2/LPE10); GO:0015095 (magnesium ion transmembrane transporter activity), GO:0015693 (magnesium ion transport), GO:0016020 (membrane), GO:0030001 (metal ion transport), GO:0046873 (metal ion transmembrane transporter activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
2828
|
| Description: |
sec23/sec24 transport family protein; IPR002035 (von Willebrand factor, type A), IPR006895 (Zinc finger, Sec23/Sec24-type), IPR006896 (Sec23/Sec24, trunk domain), IPR006900 (Sec23/Sec24, helical domain); GO:0006886 (intracellular protein transport), GO:0006888 (ER to Golgi vesicle-mediated transport), GO:0008270 (zinc ion binding), GO:0030127 (COPII vesicle coat) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
1047
|
| Description: |
uncharacterized protein LOC100305864 isoform X2 [Glycine max]; IPR005227 (Resolvase, holliday junction-type, YqgF-like), IPR012337 (Ribonuclease H-like domain); GO:0003676 (nucleic acid binding), GO:0005737 (cytoplasm), GO:0006139 (nucleobase-containing compound metabolic process), GO:0006281 (DNA repair), GO:0006310 (DNA recombination), GO:0006974 (cellular response to DNA damage stimulus) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
3183
|
| Description: |
protein kinase family protein; IPR001611 (Leucine-rich repeat), IPR011009 (Protein kinase-like domain), IPR013210 (Leucine-rich repeat-containing N-terminal, type 2), IPR013320 (Concanavalin A-like lectin/glucanase, subgroup); GO:0004672 (protein kinase activity), GO:0004674 (protein serine/threonine kinase activity), GO:0005515 (protein binding), GO:0005524 (ATP binding), GO:0006468 (protein phosphorylation) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
1383
|
| Description: |
E3 ubiquitin-protein ligase SINAT3-like [Glycine max]; IPR004162 (E3 ubiquitin-protein ligase SINA like), IPR013083 (Zinc finger, RING/FYVE/PHD-type); GO:0004842 (ubiquitin-protein ligase activity), GO:0005515 (protein binding), GO:0005634 (nucleus), GO:0006511 (ubiquitin-dependent protein catabolic process), GO:0007275 (multicellular organismal development), GO:0008270 (zinc ion binding), GO:0016567 (protein ubiquitination) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
2442
|
| Description: |
signal recognition particle subunit SRP72-like [Glycine max]; IPR011990 (Tetratricopeptide-like helical), IPR013699 (Signal recognition particle, SRP72 subunit, RNA-binding), IPR026270 (Signal recognition particle, SRP72 subunit); GO:0005515 (protein binding), GO:0006614 (SRP-dependent cotranslational protein targeting to membrane), GO:0008312 (7S RNA binding), GO:0048500 (signal recognition particle) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
2833
|
| Description: |
Protein kinase superfamily protein; IPR001611 (Leucine-rich repeat), IPR011009 (Protein kinase-like domain), IPR013210 (Leucine-rich repeat-containing N-terminal, type 2), IPR013320 (Concanavalin A-like lectin/glucanase, subgroup), IPR025875 (Leucine rich repeat 4); GO:0004672 (protein kinase activity), GO:0005515 (protein binding), GO:0005524 (ATP binding), GO:0006468 (protein phosphorylation) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
8221
|
| Description: |
ABC transporter family protein (ATP-binding component); IPR011527 (ABC transporter type 1, transmembrane domain), IPR027417 (P-loop containing nucleoside triphosphate hydrolase); GO:0000166 (nucleotide binding), GO:0005524 (ATP binding), GO:0006810 (transport), GO:0016021 (integral component of membrane), GO:0016887 (ATPase activity), GO:0017111 (nucleoside-triphosphatase activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
1796
|
| Description: |
E3 ubiquitin-protein ligase SINAT3-like [Glycine max]; IPR004162 (E3 ubiquitin-protein ligase SINA like), IPR013083 (Zinc finger, RING/FYVE/PHD-type); GO:0004842 (ubiquitin-protein ligase activity), GO:0005515 (protein binding), GO:0005634 (nucleus), GO:0006511 (ubiquitin-dependent protein catabolic process), GO:0007275 (multicellular organismal development), GO:0008270 (zinc ion binding), GO:0016567 (protein ubiquitination) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
1297
|
| Description: |
calmodulin-binding transcription activator 5-like [Glycine max]; IPR002673 (Ribosomal protein L29e), IPR016156 (FAD/NAD-linked reductase, dimerisation domain); GO:0003735 (structural constituent of ribosome), GO:0005622 (intracellular), GO:0005840 (ribosome), GO:0006412 (translation), GO:0016491 (oxidoreductase activity), GO:0045454 (cell redox homeostasis), GO:0050660 (flavin adenine dinucleotide binding), GO:0055114 (oxidation-reduction process) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
5676
|
| Description: |
ABC transporter family protein (ATP-binding component); IPR011527 (ABC transporter type 1, transmembrane domain), IPR027417 (P-loop containing nucleoside triphosphate hydrolase); GO:0000166 (nucleotide binding), GO:0005524 (ATP binding), GO:0006810 (transport), GO:0016021 (integral component of membrane), GO:0016887 (ATPase activity), GO:0017111 (nucleoside-triphosphatase activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
414
|
| Description: |
Unknown protein; IPR001806 (Small GTPase superfamily), IPR005225 (Small GTP-binding protein domain), IPR027417 (P-loop containing nucleoside triphosphate hydrolase); GO:0005525 (GTP binding), GO:0005622 (intracellular), GO:0006184 (GTP catabolic process), GO:0007165 (signal transduction), GO:0007264 (small GTPase mediated signal transduction), GO:0015031 (protein transport), GO:0016020 (membrane) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
1936
|
| Description: |
magnesium transporter 9; IPR002523 (Mg2+ transporter protein, CorA-like/Zinc transport protein ZntB), IPR026573 (Magnesium transporter MRS2/LPE10); GO:0015095 (magnesium ion transmembrane transporter activity), GO:0015693 (magnesium ion transport), GO:0016020 (membrane), GO:0030001 (metal ion transport), GO:0046873 (metal ion transmembrane transporter activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
3027
|
| Description: |
ATP binding/protein serine/threonine kinase [Glycine max]; IPR001368 (TNFR/NGFR cysteine-rich region), IPR009091 (Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II), IPR011009 (Protein kinase-like domain); GO:0004672 (protein kinase activity), GO:0004674 (protein serine/threonine kinase activity), GO:0005515 (protein binding), GO:0005524 (ATP binding), GO:0006468 (protein phosphorylation) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
3121
|
| Description: |
protein kinase family protein; IPR001611 (Leucine-rich repeat), IPR011009 (Protein kinase-like domain), IPR013210 (Leucine-rich repeat-containing N-terminal, type 2), IPR013320 (Concanavalin A-like lectin/glucanase, subgroup); GO:0004672 (protein kinase activity), GO:0004674 (protein serine/threonine kinase activity), GO:0005515 (protein binding), GO:0005524 (ATP binding), GO:0006468 (protein phosphorylation) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
1597
|
| Description: |
E3 ubiquitin-protein ligase SINAT3-like [Glycine max]; IPR004162 (E3 ubiquitin-protein ligase SINA like), IPR013083 (Zinc finger, RING/FYVE/PHD-type); GO:0004842 (ubiquitin-protein ligase activity), GO:0005515 (protein binding), GO:0005634 (nucleus), GO:0006511 (ubiquitin-dependent protein catabolic process), GO:0007275 (multicellular organismal development), GO:0008270 (zinc ion binding), GO:0016567 (protein ubiquitination) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
2927
|
| Description: |
receptor-like protein kinase 4; IPR000858 (S-locus glycoprotein), IPR001480 (Bulb-type lectin domain), IPR003609 (Apple-like), IPR011009 (Protein kinase-like domain), IPR013320 (Concanavalin A-like lectin/glucanase, subgroup); GO:0004672 (protein kinase activity), GO:0004674 (protein serine/threonine kinase activity), GO:0005524 (ATP binding), GO:0006468 (protein phosphorylation), GO:0048544 (recognition of pollen) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
3943
|
| Description: |
putative transcription elongation factor SPT5 homolog 1-like isoform X2 [Glycine max]; IPR008991 (Translation protein SH3-like domain), IPR017071 (Transcription elongation factor Spt5); GO:0003735 (structural constituent of ribosome), GO:0005622 (intracellular), GO:0005840 (ribosome), GO:0006357 (regulation of transcription from RNA polymerase II promoter), GO:0006412 (translation) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
3368
|
| Description: |
Protein kinase superfamily protein; IPR001611 (Leucine-rich repeat), IPR011009 (Protein kinase-like domain), IPR013210 (Leucine-rich repeat-containing N-terminal, type 2), IPR013320 (Concanavalin A-like lectin/glucanase, subgroup); GO:0004672 (protein kinase activity), GO:0004674 (protein serine/threonine kinase activity), GO:0005515 (protein binding), GO:0005524 (ATP binding), GO:0006468 (protein phosphorylation) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
5031
|
| Description: |
ABC transporter family protein (ATP-binding component); IPR011527 (ABC transporter type 1, transmembrane domain), IPR027417 (P-loop containing nucleoside triphosphate hydrolase); GO:0000166 (nucleotide binding), GO:0005524 (ATP binding), GO:0006810 (transport), GO:0016021 (integral component of membrane), GO:0016887 (ATPase activity), GO:0017111 (nucleoside-triphosphatase activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
3156
|
| Description: |
magnesium transporter 9; IPR002523 (Mg2+ transporter protein, CorA-like/Zinc transport protein ZntB), IPR026573 (Magnesium transporter MRS2/LPE10); GO:0015095 (magnesium ion transmembrane transporter activity), GO:0015693 (magnesium ion transport), GO:0016020 (membrane), GO:0030001 (metal ion transport), GO:0046873 (metal ion transmembrane transporter activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
3396
|
| Description: |
kinesin-related protein 11-like isoform X1 [Glycine max]; IPR001752 (Kinesin, motor domain), IPR010994 (RuvA domain 2-like), IPR027417 (P-loop containing nucleoside triphosphate hydrolase), IPR027640 (Kinesin-like protein); GO:0003777 (microtubule motor activity), GO:0005524 (ATP binding), GO:0005871 (kinesin complex), GO:0007018 (microtubule-based movement), GO:0008017 (microtubule binding) |
| Organism: |
Cicer echinospermum |
| Strain: |
S2Drd065 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
3584
|
| Description: |
disease resistance protein (TIR-NBS-LRR class), putative; IPR000157 (Toll/interleukin-1 receptor homology (TIR) domain), IPR000767 (Disease resistance protein), IPR027417 (P-loop containing nucleoside triphosphate hydrolase); GO:0000166 (nucleotide binding), GO:0005515 (protein binding), GO:0006952 (defense response), GO:0007165 (signal transduction), GO:0017111 (nucleoside-triphosphatase activity), GO:0043531 (ADP binding) |
| Organism: |
Cicer echinospermum |
| Strain: |
S2Drd065 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
3261
|
| Description: |
protein kinase family protein; IPR001611 (Leucine-rich repeat), IPR011009 (Protein kinase-like domain), IPR013210 (Leucine-rich repeat-containing N-terminal, type 2), IPR013320 (Concanavalin A-like lectin/glucanase, subgroup); GO:0004672 (protein kinase activity), GO:0004674 (protein serine/threonine kinase activity), GO:0005515 (protein binding), GO:0005524 (ATP binding), GO:0006468 (protein phosphorylation) |
| Organism: |
Cicer echinospermum |
| Strain: |
S2Drd065 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
2204
|
| Description: |
GTP binding Elongation factor Tu family protein; IPR004541 (Translation elongation factor EFTu/EF1A, bacterial/organelle), IPR005225 (Small GTP-binding protein domain), IPR027417 (P-loop containing nucleoside triphosphate hydrolase); GO:0003746 (translation elongation factor activity), GO:0003924 (GTPase activity), GO:0005525 (GTP binding), GO:0005622 (intracellular), GO:0006414 (translational elongation) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
2770
|
| Description: |
magnesium (Mg) transporter 10; IPR002523 (Mg2+ transporter protein, CorA-like/Zinc transport protein ZntB), IPR026573 (Magnesium transporter MRS2/LPE10); GO:0015095 (magnesium ion transmembrane transporter activity), GO:0015693 (magnesium ion transport), GO:0016020 (membrane), GO:0030001 (metal ion transport), GO:0046873 (metal ion transmembrane transporter activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| Protein Domain |
| Name: |
Gamma-aminobutyric-acid A receptor, beta subunit |
| Type: |
Family |
| Description: |
Neurotransmitter ligand-gated ion channels are transmembrane receptor-ion channel complexes that open transiently upon binding of specific ligands, allowing rapid transmission of signals at chemical synapses [
,
]. Five of these ion channel receptor families have been shown to form a sequence-related superfamily:Nicotinic acetylcholine receptor (AchR), an excitatory cation channel in vertebrates and invertebrates; in vertebrate motor endplates it is composed of alpha, beta, gamma and delta/epsilon subunits; in neurons it is composed of alpha and non-alpha (or beta) subunits [
].Glycine receptor, an inhibitory chloride ion channel composed of alpha and beta subunits [
].Gamma-aminobutyric acid (GABA) receptor, an inhibitory chloride ion channel; at least four types of subunits (alpha, beta, gamma and delta) are known [
].Serotonin 5HT3 receptor, of which there are seven major types (5HT3-5HT7) [
].Glutamate receptor, an excitatory cation channel of which at least three types have been described (kainate, N-methyl-D-aspartate (NMDA) and quisqualate) [
].These receptors possess a pentameric structure (made up of varying subunits), surrounding a central pore. All known sequences of subunits from neurotransmitter-gated ion-channels are structurally related. They are composed of a large extracellular glycosylated N-terminal ligand-binding domain, followed by three hydrophobic transmembrane regions which form the ionic channel, followed by an intracellular region of variable length. A fourth hydrophobic region is found at the C-terminal of the sequence [
,
].Gamma-aminobutyric acid type A (GABAA) receptors are members of the neurotransmitter ligand-gated ion channels: they mediate neuronal inhibition on binding GABA. The effects of GABA on GABAA receptors are modulated by a range of therapeutically important drugs, including barbiturates, anaesthetics and benzodiazepines (BZs) [
]. The BZs are a diverse range of compounds, including widely prescribed drugs, such as librium and valium, and their interaction with GABAA receptors provides the most potent pharmacological means of distinguishing different GABAA receptor subtypes.GABAA receptors are pentameric membrane proteins that operate GABA-gated chloride channels [
]. Eight types of receptor subunit have been cloned, with multiple subtypes within some classes: alpha 1-6, beta 1-4, gamma 1-4, delta, epsilon, pi, rho 1-3 and theta [,
]. Subunits are typically 50-60kDa in size and comprise a long N-terminal extracellular domain, containing a putative signal peptide and a disulphide-bonded beta structural loop; 4 putative transmembrane (TM) domains; and a large cytoplasmic loop connecting the third and fourth TM domains. Amongst family members, the large cytoplasmic loop displays the most divergence in terms of primary structure, the TM domains showing the highest level of sequence conservation [].Most GABAA receptors contain one type of alpha and beta subunit, and a single gamma polypeptide in a ratio of 2:2:1 [
], though in some cases other subunits such as epsilon or delta may replace gamma. The BZ binding site is located at the interface of adjacent alpha and gamma subunits; therefore, the type of alpha and gamma subunits present is instrumental in determining BZ selectivity and sensitivity. Receptors can be categorised into 3 groups based on their alpha subunit content and, hence, sensitivity to BZs: alpha 1-containing receptors have greatest sensitivity towards BZs (type I); alpha 2, 3 and 5-containing receptors have similar but distinguishable properties (type II); and alpha 4- and 6-containing assemblies have very low BZ affinity [
]. A conserved histidine residue in the alpha subunit of type I and II receptors is believed to be responsible for BZ affinity []. A cDNA encoding the human GABAA receptor beta 2 subunit has been cloned and
sequenced []. Expression of recombinant human GABAA receptors containingdifferent beta subunits (beta 1, beta 2 or beta 3) in both transfected
cells and Xenopus laevis oocytes, has revealed the influence of the beta subunit onthe pharmacology of the receptor. For a number of benzodiazepine binding
site compounds, a barbiturate, and several neurosteroids, neither theaffinity nor the efficacy of the compounds is influenced by the type of
beta subunit present in the receptor molecule []. These observationssuggest that the beta subunit does not significantly influence the
benzodiazepine, barbiturate, or steroid site pharmacologies of human GABAAreceptor subtypes [
]. |
|
•
•
•
•
•
|
| Protein Domain |
| Name: |
Glucose transporter, type 4 (GLUT4) |
| Type: |
Family |
| Description: |
The ability to transport glucose across the plasma membrane is a feature common to nearly all cells, from simple bacteria through to highly specialised mammalian neurones. Facilitative sugar transport is mediated by members of the GLUT transporter family, which form an aqueous pore across the membrane through which sugars can move in a passive (i.e., energy-independent) manner; in consequence, they can only transport sugars down their concentration gradient. The GLUT family of glycosylated transmembrane proteins are predicted to span the membrane 12 times with both amino- and carboxyl-termini located in the cytosol. On the basis of sequence homology and structural similarity, three subclasses of sugar transporters have been defined: Class I (GLUTs 1-4) are glucose transporters; Class II (GLUTs 5, 7, 9 and 11) are fructose transporters; and Class III (GLUTs 6, 8, 10, 12 and HMIT1) are structurally atypical members of the GLUT family, which are poorly defined at present, indeed GLUT6 may only be a pseudo-gene [
,
,
,
,
].The confirmed isoforms are expressed in a tissue and cell-specific manner, and exhibit distinct kinetic and regulatory properties, presumably reflecting their specific functional roles. They belong to a much larger 'major facilitator superfamily' of 12 TM transporters that are involved in the transport of a variety of hexoses and other carbon compounds, and include: bacterial sugar-proton symporters (H
+/xylose and H
+/arabinose); bacterial transporters of carboxylic acids and antibiotics; and sugar transporters in various yeast, protozoa and higher plants. Nevertheless, amino acid identity within the superfamily may be as low as ~25% [
,
]. Besides the 12 presumed TM domains, the most characteristic structural feature of the superfamily is a five residue motif (RXGRR, where X is any amino acid). In the GLUT transporters, this motif is present in the presumed cytoplasmic loops connecting TM domains 2 with 3, and also 8 with 9. The 12 TM transporter superfamily appears to be structurally unrelated to the Na+-coupled, Na
+/glucose co-transporters (SGLT1-3) found in the intestine and kidney, which are able to transport glucose against its concentration gradient [
].Comparison of the hydropathy profiles for GLUT1-5 reveals that they are virtually superimposable, despite the fact that their primary structures may differ by up to 60%. Of the presumed TM domains, the fourth, fifth and sixth are the most highly conserved, and conserved residues are also found in the short exofacial loops joining the putative TM regions. The presumed cytoplasmic N- and C-termini, and the extracellular loop between the first and second TM domains, show the greatest divergence, both in terms of primary structure and size.GLUT4 is thought to be an insulin-responsive glucose transporter, expressed in the membranes of the cells and organelles of skeletal muscle, heart and fat. These tissues
are insulin-sensitive and respond to increased blood insulinlevels by a rapid and reversible 20-30 fold increase in glucose transport.
This is thought to be brought about (at least partially) by thetranslocation of a latent pool of glucose transporters from an intracellular
site to the plasma membrane. On entry into the endosomal system, GLUT4 isselectively retained at the expense of other recycling
transport that constitutively moves between the endosomes and the cell surface. This retention mechanism might predispose GLUT4 for sorting into transportvesicles that bud slowly from the endosome and that are targeted to the trans-Golgi network (TGN).
GLUT4 is sorted into a secretory pathway in the TGN. This probablyinvolves a specialised population of secretory vesicles that excludes other
secretory cargo, and that does not fuse constitutively with the plasma membrane.In the absence of insulin, GLUT4 storage vesicles might
slowly fuse with endosomes, thereby accounting for the presence of a significantbut small pool of GLUT4 in endosomes, even in the absence of insulin. Insulin
would then shift GLUT4 from this TGN-endosome cycle to a pathway that takesGLUT4 directly to the cell surface [
]. GLUT4 consists of 509 amino acids (human isoform) and shows ~60% amino acid
identity to the GLUT1-3 isoforms, being most similar to GLUT1. Both the N- and C-terminal portions of the molecule having been reported to beinvolved in the targeting. |
|
•
•
•
•
•
|
| Protein Domain |
| Name: |
Glycine receptor beta |
| Type: |
Family |
| Description: |
Neurotransmitter ligand-gated ion channels are transmembrane receptor-ion channel complexes that open transiently upon binding of specific ligands, allowing rapid transmission of signals at chemical synapses [
,
]. Five of these ion channel receptor families have been shown to form a sequence-related superfamily:Nicotinic acetylcholine receptor (AchR), an excitatory cation channel in vertebrates and invertebrates; in vertebrate motor endplates it is composed of alpha, beta, gamma and delta/epsilon subunits; in neurons it is composed of alpha and non-alpha (or beta) subunits [
].Glycine receptor, an inhibitory chloride ion channel composed of alpha and beta subunits [
].Gamma-aminobutyric acid (GABA) receptor, an inhibitory chloride ion channel; at least four types of subunits (alpha, beta, gamma and delta) are known [
].Serotonin 5HT3 receptor, of which there are seven major types (5HT3-5HT7) [
].Glutamate receptor, an excitatory cation channel of which at least three types have been described (kainate, N-methyl-D-aspartate (NMDA) and quisqualate) [
].These receptors possess a pentameric structure (made up of varying subunits), surrounding a central pore. All known sequences of subunits from neurotransmitter-gated ion-channels are structurally related. They are composed of a large extracellular glycosylated N-terminal ligand-binding domain, followed by three hydrophobic transmembrane regions which form the ionic channel, followed by an intracellular region of variable length. A fourth hydrophobic region is found at the C-terminal of the sequence [
,
].Glycine is a major inhibitory neurotransmitter (NT) in the adult vertebrate
central nervous system (CNS). Glycinergic synapses have a well-establishedrole in the processing of motor and sensory information that controls
movement, vision and audition []. This action of glycine is mediatedthrough its interaction with the glycine receptor (GlyR): an intrinsic
chloride channel is opened in response to agonist binding. The subsequentinflux of anions prevents membrane depolarisation and neuronal firing
induced by excitatory NTs. Strychnine acts as a competitive antagonist ofglycine binding, thereby reducing the activity of inhibitory neurones.
Poisoning with strychnine is characterised by over-excitation, muscle spasmsand convulsions. Whilst glycine is the principal physiological agonist at
GlyRs, taurine and beta-alanine also behave as agonists []. Compounds thatmodulate GlyR activity include zinc, some alcohols and anaesthetics,
picrotoxin, cocaine and some anticonvulsants. GlyRs were thought for sometime to be localised exclusively in the brain stem and spinal cord, but have
since been found to be expressed more widely, including the cochlear nuclei,cerebellar cortex and forebrain [
].GlyRs belong to the ligand-gated ion channel family, which also includes the
inhibitory gamma-aminobutyric acid type A (GABAA) and excitatory nicotinicacetylcholine (nACh) and serotonin type 3 (5-HT3) receptors [
].Affinity-purified GlyR was found to contain two glycosylated membrane
proteins of 48kDa and 56kDa, corresponding to alpha and beta subunits,respectively. Four genes encoding alpha subunits have been identified (GLRA1
to 4), together with a single beta polypeptide (GLRB). The heterogeneity ofalpha subunits is further increased by alternative exon splicing, yielding
two isoforms of GLRA1 to 3 []. The characteristics of different GlyRsubtypes, therefore, can be largely explained by their GLRA content.
GlyRs are generally believed to adopt a pentameric structure in vivo: five
subunits assemble to form a ring structure with a central pore. Typically, astoichiometry of 3:2 (alpha:beta) is observed [
]. GlyR subunits share ahigh overall level of sequence similarity both with themselves and with the
subunits of the GABAA and nACh receptors. Four highly conserved segmentshave been proposed to correspond to transmembrane (TM) α-helices (TM1-4),
the second of which is thought to contribute to the pore wall []. A long extracellular N-terminal segment precedes TM1 and a long cytoplasmic loop
links TM3 and 4. Short cytoplasmic and extracellular loops join TM1-2 andTM2-3, respectively, and a short C-terminal sequence follows TM4. Studies
using radiolabelled strychnine have shown the alpha subunit to beresponsible for ligand binding, the critical residues for this interaction
lying within the N-terminal domain. The beta subunit plays a structuralrole, contributing one of its TM domains to the pore wall as well as playing
a putative role in postsynaptic clustering of the receptor.In several mammalian species, defects in glycinergic transmission are
associated with complex motor disorders. Mutations in the gene encodingGLRA1 give rise to hyperplexia, or startle disease [
]. This ischaracterised by muscular spasms in response to unexpected light or noise
stimuli, similar to the symptoms of sublethal doses of strychnine. Themutations result in amino acid substitutions within the TM1-2 and TM3-4
loops, suggesting that these regions are involved in the transduction ofligand binding into channel activation.
|
|
•
•
•
•
•
|
| Protein Domain |
| Name: |
Gamma-aminobutyric acid receptor subunit gamma-1/4 |
| Type: |
Family |
| Description: |
Neurotransmitter ligand-gated ion channels are transmembrane receptor-ion channel complexes that open transiently upon binding of specific ligands, allowing rapid transmission of signals at chemical synapses [
,
]. Five of these ion channel receptor families have been shown to form a sequence-related superfamily:Nicotinic acetylcholine receptor (AchR), an excitatory cation channel in vertebrates and invertebrates; in vertebrate motor endplates it is composed of alpha, beta, gamma and delta/epsilon subunits; in neurons it is composed of alpha and non-alpha (or beta) subunits [
].Glycine receptor, an inhibitory chloride ion channel composed of alpha and beta subunits [
].Gamma-aminobutyric acid (GABA) receptor, an inhibitory chloride ion channel; at least four types of subunits (alpha, beta, gamma and delta) are known [
].Serotonin 5HT3 receptor, of which there are seven major types (5HT3-5HT7) [
].Glutamate receptor, an excitatory cation channel of which at least three types have been described (kainate, N-methyl-D-aspartate (NMDA) and quisqualate) [
].These receptors possess a pentameric structure (made up of varying subunits), surrounding a central pore. All known sequences of subunits from neurotransmitter-gated ion-channels are structurally related. They are composed of a large extracellular glycosylated N-terminal ligand-binding domain, followed by three hydrophobic transmembrane regions which form the ionic channel, followed by an intracellular region of variable length. A fourth hydrophobic region is found at the C-terminal of the sequence [
,
].Gamma-aminobutyric acid type A (GABAA) receptors are members of the neurotransmitter ligand-gated ion channels: they mediate neuronal inhibition on binding GABA. The effects of GABA on GABAA receptors are modulated by a range of therapeutically important drugs, including barbiturates, anaesthetics and benzodiazepines (BZs) [
]. The BZs are a diverse range of compounds, including widely prescribed drugs, such as librium and valium, and their interaction with GABAA receptors provides the most potent pharmacological means of distinguishing different GABAA receptor subtypes.GABAA receptors are pentameric membrane proteins that operate GABA-gated chloride channels [
]. Eight types of receptor subunit have been cloned, with multiple subtypes within some classes: alpha 1-6, beta 1-4, gamma 1-4, delta, epsilon, pi, rho 1-3 and theta [
,
]. Subunits are typically 50-60kDa in size and comprise a long N-terminal extracellular domain, containing a putative signal peptide and a disulphide-bonded beta structural loop; 4 putative transmembrane (TM) domains; and a large cytoplasmic loop connecting the third and fourth TM domains. Amongst family members, the large cytoplasmic loop displays the most divergence in terms of primary structure, the TM domains showing the highest level of sequence conservation [].Most GABAA receptors contain one type of alpha and beta subunit, and a single gamma polypeptide in a ratio of 2:2:1 [
], though in some cases other subunits such as epsilon or delta may replace gamma. The BZ binding site is located at the interface of adjacent alpha and gamma subunits; therefore, the type of alpha and gamma subunits present is instrumental in determining BZ selectivity and sensitivity. Receptors can be categorised into 3 groups based on their alpha subunit content and, hence, sensitivity to BZs: alpha 1-containing receptors have greatest sensitivity towards BZs (type I); alpha 2, 3 and 5-containing receptors have similar but distinguishable properties (type II); and alpha 4- and 6-containing assemblies have very low BZ affinity []. A conserved histidine residue in the alpha subunit of type I and II receptors is believed to be responsible for BZ affinity []. Three mammalian gamma subunits have been identified (gamma 1 to 3), each encoded by a separate gene, plus an avian gamma 4 subunit. The presence of a gamma 2 subunit, together with alpha 1, confers `classical' BZ-binding activity to GABAA receptors; substitution for gamma 1 or 3 leads to an altered binding profile for BZs [
]. The gamma 2 gene undergoes alternative exon splicing leading to the generation of two isoforms that differ by an additional 24-bp exon in the large putative cytoplasmic domain []. The isoforms are termed gamma 2L (long) and gamma 2S (short), and are ubiquitously expressed. The gamma 2L splice variant has been implicated in potentiation of GABAA receptors by ethanol.This entry represents Gamma-aminobutyric acid receptor subunit gamma-1/4 found in GABAA receptors, mainly found in Chordates. |
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•
•
•
•
•
|
| Protein Domain |
| Name: |
Gamma-aminobutyric-acid A receptor, gamma 1 subunit |
| Type: |
Family |
| Description: |
Neurotransmitter ligand-gated ion channels are transmembrane receptor-ion channel complexes that open transiently upon binding of specific ligands, allowing rapid transmission of signals at chemical synapses [
,
]. Five of these ion channel receptor families have been shown to form a sequence-related superfamily:Nicotinic acetylcholine receptor (AchR), an excitatory cation channel in vertebrates and invertebrates; in vertebrate motor endplates it is composed of alpha, beta, gamma and delta/epsilon subunits; in neurons it is composed of alpha and non-alpha (or beta) subunits [
].Glycine receptor, an inhibitory chloride ion channel composed of alpha and beta subunits [
].Gamma-aminobutyric acid (GABA) receptor, an inhibitory chloride ion channel; at least four types of subunits (alpha, beta, gamma and delta) are known [
].Serotonin 5HT3 receptor, of which there are seven major types (5HT3-5HT7) [
].Glutamate receptor, an excitatory cation channel of which at least three types have been described (kainate, N-methyl-D-aspartate (NMDA) and quisqualate) [
].These receptors possess a pentameric structure (made up of varying subunits), surrounding a central pore. All known sequences of subunits from neurotransmitter-gated ion-channels are structurally related. They are composed of a large extracellular glycosylated N-terminal ligand-binding domain, followed by three hydrophobic transmembrane regions which form the ionic channel, followed by an intracellular region of variable length. A fourth hydrophobic region is found at the C-terminal of the sequence [
,
].Gamma-aminobutyric acid type A (GABAA) receptors are members of the neurotransmitter ligand-gated ion channels: they mediate neuronal inhibition on binding GABA. The effects of GABA on GABAA receptors are modulated by a range of therapeutically important drugs, including barbiturates, anaesthetics and benzodiazepines (BZs) [
]. The BZs are a diverse range of compounds, including widely prescribed drugs, such as librium and valium, and their interaction with GABAA receptors provides the most potent pharmacological means of distinguishing different GABAA receptor subtypes.GABAA receptors are pentameric membrane proteins that operate GABA-gated chloride channels [
]. Eight types of receptor subunit have been cloned, with multiple subtypes within some classes: alpha 1-6, beta 1-4, gamma 1-4, delta, epsilon, pi, rho 1-3 and theta [,
]. Subunits are typically 50-60kDa in size and comprise a long N-terminal extracellular domain, containing a putative signal peptide and a disulphide-bonded beta structural loop; 4 putative transmembrane (TM) domains; and a large cytoplasmic loop connecting the third and fourth TM domains. Amongst family members, the large cytoplasmic loop displays the most divergence in terms of primary structure, the TM domains showing the highest level of sequence conservation [].Most GABAA receptors contain one type of alpha and beta subunit, and a single gamma polypeptide in a ratio of 2:2:1 [
], though in some cases other subunits such as epsilon or delta may replace gamma. The BZ binding site is located at the interface of adjacent alpha and gamma subunits; therefore, the type of alpha and gamma subunits present is instrumental in determining BZ selectivity and sensitivity. Receptors can be categorised into 3 groups based on their alpha subunit content and, hence, sensitivity to BZs: alpha 1-containing receptors have greatest sensitivity towards BZs (type I); alpha 2, 3 and 5-containing receptors have similar but distinguishable properties (type II); and alpha 4- and 6-containing assemblies have very low BZ affinity []. A conserved histidine residue in the alpha subunit of type I and II receptors is believed to be responsible for BZ affinity []. Three mammalian gamma subunits have been identified (gamma 1 to 3), each encoded by a separate gene, plus an avian gamma 4 subunit. The presence of a gamma 2 subunit, together with alpha 1, confers `classical' BZ-binding activity to GABAA receptors; substitution for gamma 1 or 3 leads to an altered binding profile for BZs [
]. The gamma 2 gene undergoes alternative exon splicing leading to the generation of two isoforms thatdiffer by an additional 24-bp exon in the large putative cytoplasmic domain [
]. The isoforms are termed gamma 2L (long) and gamma 2S (short), and are ubiquitously expressed. The gamma 2L splice variant has been implicated in potentiation of GABAA receptors by ethanol.This entry represents the gamma 1 subunit. |
|
•
•
•
•
•
|
| Protein Domain |
| Name: |
Gamma-aminobutyric-acid A receptor, gamma 2 subunit |
| Type: |
Family |
| Description: |
Neurotransmitter ligand-gated ion channels are transmembrane receptor-ion channel complexes that open transiently upon binding of specific ligands, allowing rapid transmission of signals at chemical synapses [
,
]. Five of these ion channel receptor families have been shown to form a sequence-related superfamily:Nicotinic acetylcholine receptor (AchR), an excitatory cation channel in vertebrates and invertebrates; in vertebrate motor endplates it is composed of alpha, beta, gamma and delta/epsilon subunits; in neurons it is composed of alpha and non-alpha (or beta) subunits [
].Glycine receptor, an inhibitory chloride ion channel composed of alpha and beta subunits [
].Gamma-aminobutyric acid (GABA) receptor, an inhibitory chloride ion channel; at least four types of subunits (alpha, beta, gamma and delta) are known [].Serotonin 5HT3 receptor, of which there are seven major types (5HT3-5HT7) [
].Glutamate receptor, an excitatory cation channel of which at least three types have been described (kainate, N-methyl-D-aspartate (NMDA) and quisqualate) [
].These receptors possess a pentameric structure (made up of varying subunits), surrounding a central pore. All known sequences of subunits from neurotransmitter-gated ion-channels are structurally related. They are composed of a large extracellular glycosylated N-terminal ligand-binding domain, followed by three hydrophobic transmembrane regions which form the ionic channel, followed by an intracellular region of variable length. A fourth hydrophobic region is found at the C-terminal of the sequence [
,
].Gamma-aminobutyric acid type A (GABAA) receptors are members of the neurotransmitter ligand-gated ion channels: they mediate neuronal inhibition on binding GABA. The effects of GABA on GABAA receptors are modulated by a range of therapeutically important drugs, including barbiturates, anaesthetics and benzodiazepines (BZs) [
]. The BZs are a diverse range of compounds, including widely prescribed drugs, such as librium and valium, and their interaction with GABAA receptors provides the most potent pharmacological means of distinguishing different GABAA receptor subtypes.GABAA receptors are pentameric membrane proteins that operate GABA-gated chloride channels [
]. Eight types of receptor subunit have been cloned, with multiple subtypes within some classes: alpha 1-6, beta 1-4, gamma 1-4, delta, epsilon, pi, rho 1-3 and theta [,
]. Subunits are typically 50-60kDa in size and comprise a long N-terminal extracellular domain, containing a putative signal peptide and a disulphide-bonded beta structural loop; 4 putative transmembrane (TM) domains; and a large cytoplasmic loop connecting the third and fourth TM domains. Amongst family members, the large cytoplasmic loop displays the most divergence in terms of primary structure, the TM domains showing the highest level of sequence conservation [].Most GABAA receptors contain one type of alpha and beta subunit, and a single gamma polypeptide in a ratio of 2:2:1 [
], though in some cases other subunits such as epsilon or delta may replace gamma. The BZ binding site is located at the interface of adjacent alpha and gamma subunits; therefore, the type of alpha and gamma subunits present is instrumental in determining BZ selectivity and sensitivity. Receptors can be categorised into 3 groups based on their alpha subunit content and, hence, sensitivity to BZs: alpha 1-containing receptors have greatest sensitivity towards BZs (type I); alpha 2, 3 and 5-containing receptors have similar but distinguishable properties (type II); and alpha 4- and 6-containing assemblies have very low BZ affinity []. A conserved histidine residue in the alpha subunit of type I and II receptors is believed to be responsible for BZ affinity []. Three mammalian gamma subunits have been identified (gamma 1 to 3), each encoded by a separate gene, plus an avian gamma 4 subunit. The presence of a gamma 2 subunit, together with alpha 1, confers `classical' BZ-binding activity to GABAA receptors; substitution for gamma 1 or 3 leads to an altered binding profile for BZs [
]. The gamma 2 gene undergoes alternative exon splicing leading to the generation of two isoforms that differ by an additional 24-bp exon in the large putative cytoplasmic domain []. The isoforms are termed gamma 2L (long) and gamma 2S (short), and are ubiquitously expressed. The gamma 2L splice variant has been implicated in potentiation of GABAA receptors by ethanol.This entry represents the gamma 2 subunit. |
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•
•
•
•
•
|
| Protein Domain |
| Name: |
Gamma-aminobutyric-acid A receptor, gamma 3 subunit |
| Type: |
Family |
| Description: |
Neurotransmitter ligand-gated ion channels are transmembrane receptor-ion channel complexes that open transiently upon binding of specific ligands, allowing rapid transmission of signals at chemical synapses [
,
]. Five of these ion channel receptor families have been shown to form a sequence-related superfamily:Nicotinic acetylcholine receptor (AchR), an excitatory cation channel in vertebrates and invertebrates; in vertebrate motor endplates it is composed of alpha, beta, gamma and delta/epsilon subunits; in neurons it is composed of alpha and non-alpha (or beta) subunits [
].Glycine receptor, an inhibitory chloride ion channel composed of alpha and beta subunits [
].Gamma-aminobutyric acid (GABA) receptor, an inhibitory chloride ion channel; at least four types of subunits (alpha, beta, gamma and delta) are known [
].Serotonin 5HT3 receptor, of which there are seven major types (5HT3-5HT7) [
].Glutamate receptor, an excitatory cation channel of which at least three types have been described (kainate, N-methyl-D-aspartate (NMDA) and quisqualate) [
].These receptors possess a pentameric structure (made up of varying subunits), surrounding a central pore. All known sequences of subunits from neurotransmitter-gated ion-channels are structurally related. They are composed of a large extracellular glycosylated N-terminal ligand-binding domain, followed by three hydrophobic transmembrane regions which form the ionic channel, followed by an intracellular region of variable length. A fourth hydrophobic region is found at the C-terminal of the sequence [
,
].Gamma-aminobutyric acid type A (GABAA) receptors are members of the neurotransmitter ligand-gated ion channels: they mediate neuronal inhibition on binding GABA. The effects of GABA on GABAA receptors are modulated by a range of therapeutically important drugs, including barbiturates, anaesthetics and benzodiazepines (BZs) [
]. The BZs are a diverse range of compounds, including widely prescribed drugs, such as librium and valium, and their interaction with GABAA receptors provides the most potent pharmacological means of distinguishing different GABAA receptor subtypes.GABAA receptors are pentameric membrane proteins that operate GABA-gated chloride channels [
]. Eight types of receptor subunit have been cloned, with multiple subtypes within some classes: alpha 1-6, beta 1-4, gamma 1-4, delta, epsilon, pi, rho 1-3 and theta [,
]. Subunits are typically 50-60kDa in size and comprise a long N-terminal extracellular domain, containing a putative signal peptide and a disulphide-bonded beta structural loop; 4 putative transmembrane (TM) domains; and a large cytoplasmic loop connecting the third and fourth TM domains. Amongst family members, the large cytoplasmic loop displays the most divergence in terms of primary structure, the TM domains showing the highest level of sequence conservation [].
Most GABAA receptors contain one type of alpha and beta subunit, and a single gamma polypeptide in a ratio of 2:2:1 [
], though in some cases other subunits such as epsilon or delta may replace gamma. The BZ binding site is located at the interface of adjacent alpha and gamma subunits; therefore, the type of alpha and gamma subunits present is instrumental in determining BZ selectivity and sensitivity. Receptors can be categorised into 3 groups based on their alpha subunit content and, hence, sensitivity to BZs: alpha 1-containing receptors have greatest sensitivity towards BZs (type I); alpha 2, 3 and 5-containing receptors have similar but distinguishable properties (type II); and alpha 4- and 6-containing assemblies have very low BZ affinity []. A conserved histidine residue in the alpha subunit of type I and II receptors is believed to be responsible for BZ affinity []. Three mammalian gamma subunits have been identified (gamma 1 to 3), each encoded by a separate gene, plus an avian gamma 4 subunit. The presence of a gamma 2 subunit, together with alpha 1, confers `classical' BZ-binding activity to GABAA receptors; substitution for gamma 1 or 3 leads to an altered binding profile for BZs [
]. The gamma 2 gene undergoes alternative exon splicing leading to the generation of two isoforms that differ by an additional 24-bp exon in the large putative cytoplasmic domain []. The isoforms are termed gamma 2L (long) and gamma 2S (short), and are ubiquitously expressed. The gamma 2L splice variant has been implicated in potentiation of GABAA receptors by ethanol.This entry represents the gamma 3 subunit. |
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•
•
•
•
|
| Protein Domain |
| Name: |
Glycine receptor alpha2 |
| Type: |
Family |
| Description: |
Neurotransmitter ligand-gated ion channels are transmembrane receptor-ion channel complexes that open transiently upon binding of specific ligands, allowing rapid transmission of signals at chemical synapses [
,
]. Five of these ion channel receptor families have been shown to form a sequence-related superfamily:Nicotinic acetylcholine receptor (AchR), an excitatory cation channel in vertebrates and invertebrates; in vertebrate motor endplates it is composed of alpha, beta, gamma and delta/epsilon subunits; in neurons it is composed of alpha and non-alpha (or beta) subunits [
].Glycine receptor, an inhibitory chloride ion channel composed of alpha and beta subunits [
].Gamma-aminobutyric acid (GABA) receptor, an inhibitory chloride ion channel; at least four types of subunits (alpha, beta, gamma and delta) are known [
].Serotonin 5HT3 receptor, of which there are seven major types (5HT3-5HT7) [
].Glutamate receptor, an excitatory cation channel of which at least three types have been described (kainate, N-methyl-D-aspartate (NMDA) and quisqualate) [
].These receptors possess a pentameric structure (made up of varying subunits), surrounding a central pore. All known sequences of subunits from neurotransmitter-gated ion-channels are structurally related. They are composed of a large extracellular glycosylated N-terminal ligand-binding domain, followed by three hydrophobic transmembrane regions which form the ionic channel, followed by an intracellular region of variable length. A fourth hydrophobic region is found at the C-terminal of the sequence [
,
].Glycine is a major inhibitory neurotransmitter (NT) in the adult vertebrate
central nervous system (CNS). Glycinergic synapses have a well-establishedrole in the processing of motor and sensory information that controls
movement, vision and audition []. This action of glycine is mediatedthrough its interaction with the glycine receptor (GlyR): an intrinsic
chloride channel is opened in response to agonist binding. The subsequentinflux of anions prevents membrane depolarisation and neuronal firing
induced by excitatory NTs. Strychnine acts as a competitive antagonist ofglycine binding, thereby reducing the activity of inhibitory neurones.
Poisoning with strychnine is characterised by over-excitation, muscle spasmsand convulsions. Whilst glycine is the principal physiological agonist at
GlyRs, taurine and beta-alanine also behave as agonists []. Compounds thatmodulate GlyR activity include zinc, some alcohols and anaesthetics,
picrotoxin, cocaine and some anticonvulsants. GlyRs were thought for sometime to be localised exclusively in the brain stem and spinal cord, but have
since been found to be expressed more widely, including the cochlear nuclei,cerebellar cortex and forebrain [
].GlyRs belong to the ligand-gated ion channel family, which also includes the
inhibitory gamma-aminobutyric acid type A (GABAA) and excitatory nicotinicacetylcholine (nACh) and serotonin type 3 (5-HT3) receptors [
].Affinity-purified GlyR was found to contain two glycosylated membrane
proteins of 48kDa and 56kDa, corresponding to alpha and beta subunits,respectively. Four genes encoding alpha subunits have been identified (GLRA1
to 4), together with a single beta polypeptide (GLRB). The heterogeneity ofalpha subunits is further increased by alternative exon splicing, yielding
two isoforms of GLRA1 to 3 []. The characteristics of different GlyRsubtypes, therefore, can be largely explained by their GLRA content.
GlyRs are generally believed to adopt a pentameric structure in vivo: five
subunits assemble to form a ring structure with a central pore. Typically, astoichiometry of 3:2 (alpha:beta) is observed [
]. GlyR subunits share ahigh overall level of sequence similarity both with themselves and with the
subunits of the GABAA and nACh receptors. Four highly conserved segmentshave been proposed to correspond to transmembrane (TM) α-helices (TM1-4),
the second of which is thought to contribute to the pore wall []. A long extracellular N-terminal segment precedes TM1 and a long cytoplasmic loop
links TM3 and 4. Short cytoplasmic and extracellular loops join TM1-2 andTM2-3, respectively, and a short C-terminal sequence follows TM4. Studies
using radiolabelled strychnine have shown the alpha subunit to be
responsible for ligand binding, the critical residues for this interaction lying within the N-terminal domain. The beta subunit plays a structural
role, contributing one of its TM domains to the pore wall as well as playinga putative role in postsynaptic clustering of the receptor.
In several mammalian species, defects in glycinergic transmission are
associated with complex motor disorders. Mutations in the gene encodingGLRA1 give rise to hyperplexia, or startle disease [
]. This ischaracterised by muscular spasms in response to unexpected light or noise
stimuli, similar to the symptoms of sublethal doses of strychnine. Themutations result in amino acid substitutions within the TM1-2 and TM3-4
loops, suggesting that these regions are involved in the transduction ofligand binding into channel activation.
In humans, the GLRA2 gene is located on chromosome Xp22.2-22.1 [
]. In situhybridisation studies have shown GLRA2 to be expressed in the hippocampus,
cerebral cortex and thalamus. GLRA2 trancripts predominate in the neonataland embyonic CNS, and are replaced postnatally by those of GLRA1 and, to a
lesser extent, GLRA3. |
|
•
•
•
•
•
|
| Protein Domain |
| Name: |
Glycine receptor alpha1 |
| Type: |
Family |
| Description: |
Neurotransmitter ligand-gated ion channels are transmembrane receptor-ion channel complexes that open transiently upon binding of specific ligands, allowing rapid transmission of signals at chemical synapses [
,
]. Five of these ion channel receptor families have been shown to form a sequence-related superfamily:Nicotinic acetylcholine receptor (AchR), an excitatory cation channel in vertebrates and invertebrates; in vertebrate motor endplates it is composed of alpha, beta, gamma and delta/epsilon subunits; in neurons it is composed of alpha and non-alpha (or beta) subunits [
].Glycine receptor, an inhibitory chloride ion channel composed of alpha and beta subunits [
].Gamma-aminobutyric acid (GABA) receptor, an inhibitory chloride ion channel; at least four types of subunits (alpha, beta, gamma and delta) are known [
].Serotonin 5HT3 receptor, of which there are seven major types (5HT3-5HT7) [
].Glutamate receptor, an excitatory cation channel of which at least three types have been described (kainate, N-methyl-D-aspartate (NMDA) and quisqualate) [
].These receptors possess a pentameric structure (made up of varying subunits), surrounding a central pore. All known sequences of subunits from neurotransmitter-gated ion-channels are structurally related. They are composed of a large extracellular glycosylated N-terminal ligand-binding domain, followed by three hydrophobic transmembrane regions which form the ionic channel, followed by an intracellular region of variable length. A fourth hydrophobic region is found at the C-terminal of the sequence [
,
].Glycine is a major inhibitory neurotransmitter (NT) in the adult vertebrate
central nervous system (CNS). Glycinergic synapses have a well-establishedrole in the processing of motor and sensory information that controls
movement, vision and audition []. This action of glycine is mediatedthrough its interaction with the glycine receptor (GlyR): an intrinsic
chloride channel is opened in response to agonist binding. The subsequentinflux of anions prevents membrane depolarisation and neuronal firing
induced by excitatory NTs. Strychnine acts as a competitive antagonist ofglycine binding, thereby reducing the activity of inhibitory neurones.
Poisoning with strychnine is characterised by over-excitation, muscle spasmsand convulsions. Whilst glycine is the principal physiological agonist at
GlyRs, taurine and beta-alanine also behave as agonists []. Compounds thatmodulate GlyR activity include zinc, some alcohols and anaesthetics,
picrotoxin, cocaine and some anticonvulsants. GlyRs were thought for sometime to be localised exclusively in the brain stem and spinal cord, but have
since been found to be expressed more widely, including the cochlear nuclei,cerebellar cortex and forebrain [
].GlyRs belong to the ligand-gated ion channel family, which also includes the
inhibitory gamma-aminobutyric acid type A (GABAA) and excitatory nicotinicacetylcholine (nACh) and serotonin type 3 (5-HT3) receptors [
].Affinity-purified GlyR was found to contain two glycosylated membrane
proteins of 48kDa and 56kDa, corresponding to alpha and beta subunits,respectively. Four genes encoding alpha subunits have been identified (GLRA1to 4), together with a single beta polypeptide (GLRB). The heterogeneity of
alpha subunits is further increased by alternative exon splicing, yieldingtwo isoforms of GLRA1 to 3 [
]. The characteristics of different GlyRsubtypes, therefore, can be largely explained by their GLRA content.
GlyRs are generally believed to adopt a pentameric structure in vivo: five
subunits assemble to form a ring structure with a central pore. Typically, astoichiometry of 3:2 (alpha:beta) is observed [
]. GlyR subunits share ahigh overall level of sequence similarity both with themselves and with the
subunits of the GABAA and nACh receptors. Four highly conserved segmentshave been proposed to correspond to transmembrane (TM) α-helices (TM1-4),
the second of which is thought to contribute to the pore wall []. A long extracellular N-terminal segment precedes TM1 and a long cytoplasmic loop
links TM3 and 4. Short cytoplasmic and extracellular loops join TM1-2 andTM2-3, respectively, and a short C-terminal sequence follows TM4. Studies
using radiolabelled strychnine have shown the alpha subunit to beresponsible for ligand binding, the critical residues for this interaction
lying within the N-terminal domain. The beta subunit plays a structuralrole, contributing one of its TM domains to the pore wall as well as playing
a putative role in postsynaptic clustering of the receptor.In several mammalian species, defects in glycinergic transmission are
associated with complex motor disorders. Mutations in the gene encodingGLRA1 give rise to hyperplexia, or startle disease [
]. This ischaracterised by muscular spasms in response to unexpected light or noise
stimuli, similar to the symptoms of sublethal doses of strychnine. Themutations result in amino acid substitutions within the TM1-2 and TM3-4
loops, suggesting that these regions are involved in the transduction ofligand binding into channel activation.
In humans, the alpha 1 gene is located on chromosome 5p32 [
]. In situhybridisation studies have shown GLRA1 to be expressed in the spinal cord,
brain stem and colliculi. GLRA1 trancripts, together with GLRA3, predominatein the postnatal CNS, replacing GLRA2, which is more abundant in embryonic
and neonatal neurones. |
|
•
•
•
•
•
|
| Protein Domain |
| Name: |
Glycine receptor alpha3 |
| Type: |
Family |
| Description: |
Neurotransmitter ligand-gated ion channels are transmembrane receptor-ion channel complexes that open transiently upon binding of specific ligands, allowing rapid transmission of signals at chemical synapses [
,
]. Five of these ion channel receptor families have been shown to form a sequence-related superfamily:Nicotinic acetylcholine receptor (AchR), an excitatory cation channel in vertebrates and invertebrates; in vertebrate motor endplates it is composed of alpha, beta, gamma and delta/epsilon subunits; in neurons it is composed of alpha and non-alpha (or beta) subunits [
].Glycine receptor, an inhibitory chloride ion channel composed of alpha and beta subunits [
].Gamma-aminobutyric acid (GABA) receptor, an inhibitory chloride ion channel; at least four types of subunits (alpha, beta, gamma and delta) are known [
].Serotonin 5HT3 receptor, of which there are seven major types (5HT3-5HT7) [
].Glutamate receptor, an excitatory cation channel of which at least three types have been described (kainate, N-methyl-D-aspartate (NMDA) and quisqualate) [
].These receptors possess a pentameric structure (made up of varying subunits), surrounding a central pore. All known sequences of subunits from neurotransmitter-gated ion-channels are structurally related. They are composed of a large extracellular glycosylated N-terminal ligand-binding domain, followed by three hydrophobic transmembrane regions which form the ionic channel, followed by an intracellular region of variable length. A fourth hydrophobic region is found at the C-terminal of the sequence [
,
].Glycine is a major inhibitory neurotransmitter (NT) in the adult vertebrate
central nervous system (CNS). Glycinergic synapses have a well-establishedrole in the processing of motor and sensory information that controls
movement, vision and audition []. This action of glycine is mediatedthrough its interaction with the glycine receptor (GlyR): an intrinsic
chloride channel is opened in response to agonist binding. The subsequentinflux of anions prevents membrane depolarisation and neuronal firing
induced by excitatory NTs. Strychnine acts as a competitive antagonist ofglycine binding, thereby reducing the activity of inhibitory neurones.
Poisoning with strychnine is characterised by over-excitation, muscle spasmsand convulsions. Whilst glycine is the principal physiological agonist at
GlyRs, taurine and beta-alanine also behave as agonists []. Compounds thatmodulate GlyR activity include zinc, some alcohols and anaesthetics,
picrotoxin, cocaine and some anticonvulsants. GlyRs were thought for sometime to be localised exclusively in the brain stem and spinal cord, but have
since been found to be expressed more widely, including the cochlear nuclei,cerebellar cortex and forebrain [
].GlyRs belong to the ligand-gated ion channel family, which also includes the
inhibitory gamma-aminobutyric acid type A (GABAA) and excitatory nicotinicacetylcholine (nACh) and serotonin type 3 (5-HT3) receptors [
].Affinity-purified GlyR was found to contain two glycosylated membrane
proteins of 48kDa and 56kDa, corresponding to alpha and beta subunits,respectively. Four genes encoding alpha subunits have been identified (GLRA1
to 4), together with a single beta polypeptide (GLRB). The heterogeneity ofalpha subunits is further increased by alternative exon splicing, yielding
two isoforms of GLRA1 to 3 []. The characteristics of different GlyRsubtypes, therefore, can be largely explained by their GLRA content.
GlyRs are generally believed to adopt a pentameric structure in vivo: five
subunits assemble to form a ring structure with a central pore. Typically, astoichiometry of 3:2 (alpha:beta) is observed [
]. GlyR subunits share ahigh overall level of sequence similarity both with themselves and with the
subunits of the GABAA and nACh receptors. Four highly conserved segmentshave been proposed to correspond to transmembrane (TM) α-helices (TM1-4),
the second of which is thought to contribute to the pore wall []. A long extracellular N-terminal segment precedes TM1 and a long cytoplasmic loop
links TM3 and 4. Short cytoplasmic and extracellular loops join TM1-2 andTM2-3, respectively, and a short C-terminal sequence follows TM4. Studies
using radiolabelled strychnine have shown the alpha subunit to beresponsible for ligand binding, the critical residues for this interaction
lying within the N-terminal domain. The beta subunit plays a structuralrole, contributing one of its TM domains to the pore wall as well as playing
a putative role in postsynaptic clustering of the receptor.In several mammalian species, defects in glycinergic transmission are
associated with complex motor disorders. Mutations in the gene encodingGLRA1 give rise to hyperplexia, or startle disease [
]. This ischaracterised by muscular spasms in response to unexpected light or noise
stimuli, similar to the symptoms of sublethal doses of strychnine. Themutations result in amino acid substitutions within the TM1-2 and TM3-4
loops, suggesting that these regions are involved in the transduction ofligand binding into channel activation.
GLRA3 is expressed in the
cerebellum, olfactory bulb and hippocampus. GLRA3 trancripts, together withGLRA1, predominate in the postnatal CNS, replacing GLRA2, which is more
abundant in embryonic and neonatal neurones. |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm1 |
| Annotation: |
ann1 |
| Length: |
4824
|
| Description: |
DNA-directed RNA polymerase subunit beta; IPR000454 (ATPase, F0 complex, subunit C), IPR000568 (ATPase, F0 complex, subunit A), IPR001865 (Ribosomal protein S2), IPR002379 (V-ATPase proteolipid subunit C-like domain), IPR006592 (RNA polymerase, N-terminal), IPR007080 (RNA polymerase Rpb1, domain 1), IPR012756 (DNA-directed RNA polymerase, subunit beta''), IPR023591 (Ribosomal protein S2, flavodoxin-like domain); GO:0003677 (DNA binding), GO:0003735 (structural constituent of ribosome), GO:0003899 (DNA-directed RNA polymerase activity), GO:0005622 (intracellular), GO:0005840 (ribosome), GO:0006412 (translation), GO:0015078 (hydrogen ion transmembrane transporter activity), GO:0015935 (small ribosomal subunit), GO:0015986 (ATP synthesis coupled proton transport), GO:0015991 (ATP hydrolysis coupled proton transport) |
| Organism: |
Cicer reticulatum |
| Strain: |
Besev079 |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
5214
|
| Description: |
kinesin-related protein 11-like isoform X2 [Glycine max]; IPR001752 (Kinesin, motor domain), IPR021881 (Protein of unknown function DUF3490), IPR027417 (P-loop containing nucleoside triphosphate hydrolase), IPR027640 (Kinesin-like protein); GO:0003777 (microtubule motor activity), GO:0005524 (ATP binding), GO:0005871 (kinesin complex), GO:0007018 (microtubule-based movement), GO:0008017 (microtubule binding) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
1866
|
| Description: |
probable protein phosphatase 2C 42-like [Glycine max]; IPR001932 (Protein phosphatase 2C (PP2C)-like domain), IPR012394 (Aldehyde dehydrogenase NAD(P)-dependent), IPR016161 (Aldehyde/histidinol dehydrogenase); GO:0003824 (catalytic activity), GO:0004030 (aldehyde dehydrogenase [NAD(P)+] activity), GO:0006081 (cellular aldehyde metabolic process), GO:0008152 (metabolic process), GO:0016491 (oxidoreductase activity), GO:0055114 (oxidation-reduction process) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
4211
|
| Description: |
kinesin-related protein 11-like isoform X1 [Glycine max]; IPR001752 (Kinesin, motor domain), IPR021881 (Protein of unknown function DUF3490), IPR027417 (P-loop containing nucleoside triphosphate hydrolase), IPR027640 (Kinesin-like protein); GO:0003777 (microtubule motor activity), GO:0005524 (ATP binding), GO:0005871 (kinesin complex), GO:0007018 (microtubule-based movement), GO:0008017 (microtubule binding) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
3460
|
| Description: |
Protein kinase superfamily protein; IPR006567 (PUG domain), IPR010513 (KEN domain), IPR011009 (Protein kinase-like domain), IPR027295 (Quinonprotein alcohol dehydrogenase-like domain); GO:0004540 (ribonuclease activity), GO:0004672 (protein kinase activity), GO:0004674 (protein serine/threonine kinase activity), GO:0005515 (protein binding), GO:0005524 (ATP binding), GO:0006397 (mRNA processing), GO:0006468 (protein phosphorylation) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
2420
|
| Description: |
sugar transport protein 11 [Glycine max]; IPR005828 (General substrate transporter), IPR016196 (Major facilitator superfamily domain, general substrate transporter); GO:0005215 (transporter activity), GO:0006810 (transport), GO:0016020 (membrane), GO:0016021 (integral component of membrane), GO:0022857 (transmembrane transporter activity), GO:0022891 (substrate-specific transmembrane transporter activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
2195
|
| Description: |
sugar transport protein 5-like [Glycine max]; IPR005828 (General substrate transporter), IPR016196 (Major facilitator superfamily domain, general substrate transporter); GO:0005215 (transporter activity), GO:0006810 (transport), GO:0016020 (membrane), GO:0016021 (integral component of membrane), GO:0022857 (transmembrane transporter activity), GO:0022891 (substrate-specific transmembrane transporter activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
2877
|
| Description: |
sugar transport protein 13 [Glycine max]; IPR005828 (General substrate transporter), IPR016196 (Major facilitator superfamily domain, general substrate transporter); GO:0005215 (transporter activity), GO:0006810 (transport), GO:0016020 (membrane), GO:0016021 (integral component of membrane), GO:0022857 (transmembrane transporter activity), GO:0022891 (substrate-specific transmembrane transporter activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
1719
|
| Description: |
sugar transport protein 13 [Glycine max]; IPR005828 (General substrate transporter), IPR016196 (Major facilitator superfamily domain, general substrate transporter); GO:0005215 (transporter activity), GO:0006810 (transport), GO:0016020 (membrane), GO:0016021 (integral component of membrane), GO:0022857 (transmembrane transporter activity), GO:0022891 (substrate-specific transmembrane transporter activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
2047
|
| Description: |
sugar transport protein 14-like [Glycine max]; IPR005828 (General substrate transporter), IPR016196 (Major facilitator superfamily domain, general substrate transporter); GO:0005215 (transporter activity), GO:0006810 (transport), GO:0016020 (membrane), GO:0016021 (integral component of membrane), GO:0022857 (transmembrane transporter activity), GO:0022891 (substrate-specific transmembrane transporter activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
1456
|
| Description: |
serine/threonine protein phosphatase 2A 57 kDa regulatory subunit B' beta isoform-like [Glycine max]; IPR002554 (Protein phosphatase 2A, regulatory B subunit, B56), IPR016024 (Armadillo-type fold); GO:0000159 (protein phosphatase type 2A complex), GO:0005488 (binding), GO:0007165 (signal transduction), GO:0008601 (protein phosphatase type 2A regulator activity) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
4776
|
| Description: |
sugar transport protein 13 [Glycine max]; IPR005828 (General substrate transporter), IPR016196 (Major facilitator superfamily domain, general substrate transporter); GO:0005215 (transporter activity), GO:0006810 (transport), GO:0016020 (membrane), GO:0016021 (integral component of membrane), GO:0022857 (transmembrane transporter activity), GO:0022891 (substrate-specific transmembrane transporter activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
3505
|
| Description: |
chaperone protein ClpB1-like [Glycine max]; IPR001270 (ClpA/B family), IPR004176 (Clp, N-terminal), IPR019489 (Clp ATPase, C-terminal), IPR023150 (Double Clp-N motif), IPR027417 (P-loop containing nucleoside triphosphate hydrolase), IPR028299 (ClpA/B, conserved site 2); GO:0000166 (nucleotide binding), GO:0005524 (ATP binding), GO:0017111 (nucleoside-triphosphatase activity), GO:0019538 (protein metabolic process) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
1877
|
| Description: |
sugar transport protein 5-like [Glycine max]; IPR005828 (General substrate transporter), IPR016196 (Major facilitator superfamily domain, general substrate transporter); GO:0005215 (transporter activity), GO:0006810 (transport), GO:0016020 (membrane), GO:0016021 (integral component of membrane), GO:0022857 (transmembrane transporter activity), GO:0022891 (substrate-specific transmembrane transporter activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
1818
|
| Description: |
sugar transport protein 14-like [Glycine max]; IPR005828 (General substrate transporter), IPR016196 (Major facilitator superfamily domain, general substrate transporter); GO:0005215 (transporter activity), GO:0006810 (transport), GO:0016020 (membrane), GO:0016021 (integral component of membrane), GO:0022857 (transmembrane transporter activity), GO:0022891 (substrate-specific transmembrane transporter activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
2675
|
| Description: |
threonyl-tRNA synthetase, putative / threonine--tRNA ligase, putative; IPR002320 (Threonine-tRNA ligase, class IIa), IPR012675 (Beta-grasp domain); GO:0000166 (nucleotide binding), GO:0004812 (aminoacyl-tRNA ligase activity), GO:0004829 (threonine-tRNA ligase activity), GO:0005524 (ATP binding), GO:0005737 (cytoplasm), GO:0006418 (tRNA aminoacylation for protein translation), GO:0006435 (threonyl-tRNA aminoacylation), GO:0043039 (tRNA aminoacylation) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
1934
|
| Description: |
sugar transport protein 14-like [Glycine max]; IPR005828 (General substrate transporter), IPR016196 (Major facilitator superfamily domain, general substrate transporter); GO:0005215 (transporter activity), GO:0006810 (transport), GO:0016020 (membrane), GO:0016021 (integral component of membrane), GO:0022857 (transmembrane transporter activity), GO:0022891 (substrate-specific transmembrane transporter activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
3767
|
| Description: |
kinesin-related protein 11-like isoform X2 [Glycine max]; IPR001752 (Kinesin, motor domain), IPR021881 (Protein of unknown function DUF3490), IPR027417 (P-loop containing nucleoside triphosphate hydrolase), IPR027640 (Kinesin-like protein); GO:0003777 (microtubule motor activity), GO:0005524 (ATP binding), GO:0005871 (kinesin complex), GO:0007018 (microtubule-based movement), GO:0008017 (microtubule binding) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
1703
|
| Description: |
sugar transport protein 14-like [Glycine max]; IPR005828 (General substrate transporter), IPR016196 (Major facilitator superfamily domain, general substrate transporter); GO:0005215 (transporter activity), GO:0006810 (transport), GO:0016020 (membrane), GO:0016021 (integral component of membrane), GO:0022857 (transmembrane transporter activity), GO:0022891 (substrate-specific transmembrane transporter activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
2315
|
| Description: |
probable protein phosphatase 2C 42-like [Glycine max]; IPR001932 (Protein phosphatase 2C (PP2C)-like domain), IPR012394 (Aldehyde dehydrogenase NAD(P)-dependent), IPR016161 (Aldehyde/histidinol dehydrogenase); GO:0003824 (catalytic activity), GO:0004030 (aldehyde dehydrogenase [NAD(P)+] activity), GO:0006081 (cellular aldehyde metabolic process), GO:0008152 (metabolic process), GO:0016491 (oxidoreductase activity), GO:0055114 (oxidation-reduction process) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
2082
|
| Description: |
E3 ubiquitin-protein ligase SINAT3-like isoform X2 [Glycine max]; IPR004162 (E3 ubiquitin-protein ligase SINA like), IPR013083 (Zinc finger, RING/FYVE/PHD-type); GO:0004842 (ubiquitin-protein ligase activity), GO:0005515 (protein binding), GO:0005634 (nucleus), GO:0006511 (ubiquitin-dependent protein catabolic process), GO:0007275 (multicellular organismal development), GO:0008270 (zinc ion binding), GO:0016567 (protein ubiquitination) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
3665
|
| Description: |
disease resistance protein (TIR-NBS-LRR class), putative; IPR000157 (Toll/interleukin-1 receptor homology (TIR) domain), IPR000767 (Disease resistance protein), IPR001611 (Leucine-rich repeat), IPR027417 (P-loop containing nucleoside triphosphate hydrolase); GO:0000166 (nucleotide binding), GO:0005515 (protein binding), GO:0006952 (defense response), GO:0007165 (signal transduction), GO:0017111 (nucleoside-triphosphatase activity), GO:0043531 (ADP binding) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
4297
|
| Description: |
zinc finger CCCH domain-containing protein 44-like [Glycine max]; IPR000571 (Zinc finger, CCCH-type), IPR003121 (SWIB/MDM2 domain), IPR003169 (GYF), IPR004343 (Plus-3), IPR013083 (Zinc finger, RING/FYVE/PHD-type); GO:0003677 (DNA binding), GO:0005515 (protein binding), GO:0005634 (nucleus), GO:0008270 (zinc ion binding), GO:0016570 (histone modification), GO:0046872 (metal ion binding) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
2193
|
| Description: |
probable glutamate--tRNA ligase, cytoplasmic-like [Glycine max]; IPR000924 (Glutamyl/glutaminyl-tRNA synthetase), IPR012336 (Thioredoxin-like fold); GO:0000166 (nucleotide binding), GO:0004812 (aminoacyl-tRNA ligase activity), GO:0004818 (glutamate-tRNA ligase activity), GO:0005524 (ATP binding), GO:0005737 (cytoplasm), GO:0006412 (translation), GO:0006418 (tRNA aminoacylation for protein translation), GO:0006424 (glutamyl-tRNA aminoacylation), GO:0043039 (tRNA aminoacylation) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
3072
|
| Description: |
Protein kinase superfamily protein; IPR000858 (S-locus glycoprotein), IPR001480 (Bulb-type lectin domain), IPR011009 (Protein kinase-like domain), IPR013320 (Concanavalin A-like lectin/glucanase, subgroup), IPR024171 (S-receptor-like serine/threonine-protein kinase); GO:0004672 (protein kinase activity), GO:0004674 (protein serine/threonine kinase activity), GO:0005524 (ATP binding), GO:0006468 (protein phosphorylation), GO:0048544 (recognition of pollen) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
1980
|
| Description: |
sugar transport protein 7-like [Glycine max]; IPR005828 (General substrate transporter), IPR016196 (Major facilitator superfamily domain, general substrate transporter); GO:0005215 (transporter activity), GO:0006810 (transport), GO:0016020 (membrane), GO:0016021 (integral component of membrane), GO:0022857 (transmembrane transporter activity), GO:0022891 (substrate-specific transmembrane transporter activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
1868
|
| Description: |
sugar transport protein 5-like [Glycine max]; IPR005828 (General substrate transporter), IPR016196 (Major facilitator superfamily domain, general substrate transporter); GO:0005215 (transporter activity), GO:0006810 (transport), GO:0016020 (membrane), GO:0016021 (integral component of membrane), GO:0022857 (transmembrane transporter activity), GO:0022891 (substrate-specific transmembrane transporter activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
861
|
| Description: |
RNA-binding protein 8A-like [Glycine max]; IPR017334 (Eukaryotic translation initiation factor 3 subunit G), IPR024675 (Eukaryotic translation initiation factor 3 subunit G, N-terminal); GO:0000166 (nucleotide binding), GO:0003676 (nucleic acid binding), GO:0003743 (translation initiation factor activity), GO:0005737 (cytoplasm), GO:0005852 (eukaryotic translation initiation factor 3 complex) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
2685
|
| Description: |
serine/threonine protein phosphatase 2A 57 kDa regulatory subunit B' iota isoform-like [Glycine max]; IPR002554 (Protein phosphatase 2A, regulatory B subunit, B56), IPR016024 (Armadillo-type fold); GO:0000159 (protein phosphatase type 2A complex), GO:0005488 (binding), GO:0007165 (signal transduction), GO:0008601 (protein phosphatase type 2A regulator activity) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
| mRNA |
| Assembly: |
gnm3 |
| Annotation: |
ann1 |
| Length: |
2268
|
| Description: |
sugar transport protein 11 [Glycine max]; IPR005828 (General substrate transporter), IPR016196 (Major facilitator superfamily domain, general substrate transporter); GO:0005215 (transporter activity), GO:0006810 (transport), GO:0016020 (membrane), GO:0016021 (integral component of membrane), GO:0022857 (transmembrane transporter activity), GO:0022891 (substrate-specific transmembrane transporter activity), GO:0055085 (transmembrane transport) |
| Organism: |
Cicer arietinum |
| Strain: |
CDCFrontier |
|
•
•
•
•
•
|
