spectrin

Function: - interaction of erythrocyte spectrin with other proteins through specific binding domains lead to the formation of an extensive subplasmalemmal meshwork which is thought to be responsible for the maintenance of the biconcave shape of human erythrocytes, for regulation of plasma membrane components & for maintenance of lipid asymmetry of the plasma membrane - spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane - associates with band 4.1 & actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane - F-actin pointed end capping protein - also F-actin bundling protein Structure: - composed of nonhomologous chains, spectrin-alpha & spectrin-beta, which aggregate side-to-side in an antiparallel fashion to form dimers, tetramers, & higher polymers Compartment: - complex is anchored to the cytoplasmic face of the plasma membrane via another protein, ankyrin, which binds to beta-spectrin & mediates the binding of the whole complex to a transmembrane protein band 3 Pathology: - spectrin deficiency associated with hereditary spherocytosis

General

blood protein calmodulin binding protein cytoskeletal protein membrane protein multisubunit protein PEST protein

Properties

COMPARTMENT: plasma membrane CELL: erythrocyte MOTIF: membrane region calmodulin binding site FOR-BINDING-OF: calmodulin PEST region SUBUNITS: spectrin alpha chain, erythrocyte MOTIF: spectrin repeat {19-51} spectrin repeat {53-156} spectrin repeat {158-262} spectrin repeat {264-368} spectrin repeat {370-474} spectrin repeat {476-580} spectrin repeat {582-685} spectrin repeat {687-791} spectrin repeat {793-897} spectrin repeat {899-975} src homology 3 [SH3] domain SITE: 977-1036 spectrin repeat {1057-1080} spectrin repeat {1082-1181} spectrin repeat {1183-1287} spectrin repeat {1289-1393} spectrin repeat {1395-1498} spectrin repeat {1500-1604} spectrin repeat {1606-1710} spectrin repeat {1712-1816} spectrin repeat {1818-1925} spectrin repeat {1927-2032} spectrin repeat {2042-2146} spectrin repeat {2156-2257} EF hand SITE: 2270-2305 MOTIF: Ca+2-binding site SITE: 2283-2294 EF hand SITE: 2313-2348 MOTIF: Ca+2-binding site SITE: 2326-2337 EF hand SITE: 2351-2385 beta-spectrin MOTIF: phosphorylation site src homology 3 [SH3] domain

Database Correlations

OMIM correlations MORBIDMAP 182870 UniProt P11277

References

- Cantley LC, Auger KR, Carpenter C, Duckworth B, Graziani A, Kapeller R, Soltoff S. Oncogenes and signal transduction. Cell. 1991 Jan 25;64(2):281-302. Review. Erratum in: Cell 1991 May 31;65(5):following 914. PMID: 1846320

Components

beta-spectrin spectrin alpha chain, erythrocyte; erythroid alpha-spectrin (SPTA1, SPTA)