LIS - Legume Information System
Information about legume traits for crop improvement
GlycineMine
v5.1.0.3
Glycine data from LIS
v5.1.0.3
Glycine data from LIS
| Type | Domain |
| Description | Bicarbonate (HCO 3-) transport mechanisms are the principal regulators of pH in animal cells. Such transport also plays a vital role in acid-base movements in the stomach, pancreas, intestine, kidney, reproductive organs and the central nervous system. Functional studies have suggested four different HCO 3-transport modes. Anion exchanger proteins exchange HCO 3-for Cl -in a reversible, electroneutral manner [ ]. Na+/HCO 3-co-transport proteins mediate the coupled movement of Na +and HCO 3-across plasma membranes, often in an electrogenic manner [ ]. Na+driven Cl -/HCO 3-exchange and K +/HCO 3-exchange activities have also been detected in certain cell types, although the molecular identities of the proteins responsible remain to be determined. Sequence analysis of the two families of HCO 3-transporters that have been cloned to date (the anion exchangers and Na +/HCO 3-co-transporters) reveals that they are homologous. This is not entirely unexpected, given that they both transport HCO 3-and are inhibited by a class of pharmacological agents called disulphonic stilbenes [ ]. They share around ~25-30% sequence identity, which is distributed along their entire sequence length, and have similar predicted membrane topologies, suggesting they have ~10 transmembrane (TM) domains.This entry represents transmembrane segments of bicarbonate transporters and related proteins.In animals, this domain is found at the C terminus of many bicarbonate and similar multifunctional transporters. The crystal structure of Band 3 anion transport protein, the founding member of the solute carrier 4 (SLC4) family of bicarbonate transporters, has been solved. This protein functions both as a transporter that mediates electroneutral anion exchange across the cell membrane and as a structural protein [ , , , ].Boron transporters from plants and yeast comprise only transmembrane segments, confirmed by the solved structures [ , , ]. In plants, boron is essential for maintaining the integrity of cell walls; this transporter mediates boron translocation from roots to shoots under boron limitation []. Boron transporter 1 from Saccharomyces cerevisiae protects yeast cells from boron toxicity and is involved in the trafficking of proteins to the vacuole. The mechanism of its activity seems to be consistent with this described for other members of the family [, ]. |
| Short Name | HCO3_transpt-like_TM_dom |
