Protein Domain : 11-S seed storage protein, conserved site IPR022379

Type  Conserved_site
Description  Plant seed storage proteins, whose principal function appears to be the major nitrogen source for the developing plant, can be classified, on the basis oftheir structure, into different families. 11-S are non-glycosylated proteins which form hexameric structures [, ]. Each of the subunits in the hexamer isitself composed of an acidic and a basic chain derived from a single precursor and linked by a disulphide bond. This structure is shown in the followingrepresentation. +-------------------------+ | |xxxxxxxxxxxCxxxxxxxxxxxxxxxxxxxxxxNGxCxxxxxxxxxxxxxxxxxxxxxxx |------Acidic-subunit-------------||-----Basic-subunit------||-----------------About-480-to-500-residues-----------------| 'C': conserved cysteine involved in a disulphide bond.Members of the 11-S family include pea and broad bean legumins, oil seed rapecruciferin, rice glutelins, cotton beta-globulins, soybean glycinins, pumpkin 11-S globulin, oat globulin, sunflower helianthinin G3, etc.This family represents the precursor protein which is cleaved into the two chains. These proteins contain two β-barrel domains.This family is a member of the 'cupin' superfamily on the basis of their conserved barrel domain ('cupa' is the Latin termfor a small barrel). The signature pattern for this family includes the conserved cleavage site between the acidic and basic subunits (Asn-Gly) and a proximal cysteine residue which is involved in the inter-chain disulphide bond.
Short Name  11S_seedstore_CS

0 Child Features

0 Gene Families

14 Genes

0 Ontology Annotations

0 Parent Features

3 Publications

USDA
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