Spectrin, alpha 1

Spectrin alpha chain, erythrocyte is a protein that in humans is encoded by the SPTA1 gene.[5]

SPTA1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1OWA, 3LBX
Identifiers
Aliases	SPTA1, EL2, HPP, HS3, SPH3, SPTA, Spectrin, alpha 1, spectrin alpha, erythrocytic 1
External IDs	OMIM: 182860 MGI: 98385 HomoloGene: 74460 GeneCards: SPTA1
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1q23.1 Start 158,610,704 bp[1] End 158,686,715 bp[1]
Gene location (Mouse) Chr. Chromosome 1 (mouse)[2] Band 1 H3|1 80.97 cM Start 174,172,776 bp[2] End 174,248,450 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • calcium ion binding • metal ion binding • actin filament binding • structural constituent of cytoskeleton • GO:0001948 protein binding • actin binding • Ras guanyl-nucleotide exchange factor activity • protein heterodimerization activity Cellular component • cytoplasm • cytosol • intrinsic component of the cytoplasmic side of the plasma membrane • cell cortex • actin cytoskeleton • cytoskeleton • spectrin • spectrin-associated cytoskeleton • cytoplasmic side of plasma membrane • membrane • axon • cortical cytoskeleton • cuticular plate Biological process • actin filament organization • MAPK cascade • axon guidance • ER to Golgi vesicle-mediated transport • actin filament capping • regulation of cell shape • lymphocyte homeostasis • porphyrin-containing compound biosynthetic process • plasma membrane organization • actin cytoskeleton organization • haematopoiesis • positive regulation of protein binding • positive regulation of T cell proliferation Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	6708	20739
Ensembl	ENSG00000163554	ENSMUSG00000026532
UniProt	P02549	P08032
RefSeq (mRNA)	NM_003126	NM_011465
RefSeq (protein)	NP_003117	NP_035595
Location (UCSC)	Chr 1: 158.61 – 158.69 Mb	Chr 1: 174.17 – 174.25 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is a tetramer made up of alpha-beta dimers linked in a head-to-head arrangement. This gene is one member of a family of alpha-spectrin genes. The encoded protein is primarily composed of 22 spectrin repeats which are involved in dimer formation. It forms weaker tetramer interactions than non-erythrocytic alpha spectrin, which may increase the plasma membrane elasticity and deformability of red blood cells. Mutations in this gene result in a variety of hereditary red blood cell disorders, including elliptocytosis type 2, pyropoikilocytosis, and spherocytic hemolytic anemia.[5]

Interactions

Spectrin, alpha 1 has been shown to interact with Abl gene.[6]

References

1. GRCh38: Ensembl release 89: ENSG00000163554 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000026532 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene: SPTA1 spectrin, alpha, erythrocytic 1 (elliptocytosis 2)".
6. Ziemnicka-Kotula, D; Xu J; Gu H; Potempska A; Kim K S; Jenkins E C; Trenkner E; Kotula L (May 1998). "Identification of a candidate human spectrin Src homology 3 domain-binding protein suggests a general mechanism of association of tyrosine kinases with the spectrin-based membrane skeleton". J. Biol. Chem. UNITED STATES. 273 (22): 13681–92. doi:10.1074/jbc.273.22.13681. ISSN 0021-9258. PMID 9593709.

Further reading

• Gallagher PG, Forget BG (1993). "Spectrin genes in health and disease". Semin. Hematol. 30 (1): 4–20. PMID 8094577.
• Delaunay J, Dhermy D (1993). "Mutations involving the spectrin heterodimer contact site: clinical expression and alterations in specific function". Semin. Hematol. 30 (1): 21–33. PMID 8434258.
• Snásel J, Pichová I (1997). "The cleavage of host cell proteins by HIV-1 protease". Folia Biol. (Praha). 42 (5): 227–30. doi:10.1007/BF02818986. PMID 8997639.
• Iolascon A, Miraglia del Giudice E, Perrotta S, et al. (1998). "Hereditary spherocytosis: from clinical to molecular defects". Haematologica. 83 (3): 240–57. PMID 9573679.
• De Matteis MA, Morrow JS (2000). "Spectrin tethers and mesh in the biosynthetic pathway". J. Cell Sci. 113 (13): 2331–43. PMID 10852813.
• Delaunay J (2003). "Molecular basis of red cell membrane disorders". Acta Haematol. 108 (4): 210–8. doi:10.1159/000065657. PMID 12432217.
• Dhermy D, Schrével J, Lecomte MC (2007). "Spectrin-based skeleton in red blood cells and malaria". Curr. Opin. Hematol. 14 (3): 198–202. doi:10.1097/MOH.0b013e3280d21afd. PMID 17414207.
• Hentati A, Hu P, Asgharzadeh S, Siddique T (1993). "Dinucleotide repeat polymorphism at the human erythroid alpha spectrin (SPTA1) locus". Hum. Mol. Genet. 1 (3): 218. doi:10.1093/hmg/1.3.218-a. PMID 1339473.
• Kanzaki A, Rabodonirina M, Yawata Y, et al. (1992). "A deletional frameshift mutation of the beta-spectrin gene associated with elliptocytosis in spectrin Tokyo (beta 220/216)". Blood. 80 (8): 2115–21. PMID 1391962.
• Gallagher PG, Tse WT, Coetzer T, et al. (1992). "A common type of the spectrin alpha I 46-50a-kD peptide abnormality in hereditary elliptocytosis and pyropoikilocytosis is associated with a mutation distant from the proteolytic cleavage site. Evidence for the functional importance of the triple helical model of spectrin". J. Clin. Invest. 89 (3): 892–8. doi:10.1172/JCI115669. PMC 442935. PMID 1541680.
• Speicher DW, Weglarz L, DeSilva TM (1992). "Properties of human red cell spectrin heterodimer (side-to-side) assembly and identification of an essential nucleation site". J. Biol. Chem. 267 (21): 14775–82. PMID 1634521.
• Alloisio N, Wilmotte R, Morlé L, et al. (1992). "Spectrin Jendouba: an alpha II/31 spectrin variant that is associated with elliptocytosis and carries a mutation distant from the dimer self-association site". Blood. 80 (3): 809–15. PMID 1638030.
• Kotula L, Laury-Kleintop LD, Showe L, et al. (1991). "The exon-intron organization of the human erythrocyte alpha-spectrin gene". Genomics. 9 (1): 131–40. doi:10.1016/0888-7543(91)90230-C. PMID 1672285.
• Coetzer TL, Sahr K, Prchal J, et al. (1991). "Four different mutations in codon 28 of alpha spectrin are associated with structurally and functionally abnormal spectrin alpha I/74 in hereditary elliptocytosis". J. Clin. Invest. 88 (3): 743–9. doi:10.1172/JCI115371. PMC 295451. PMID 1679439.
• Sahr KE, Laurila P, Kotula L, et al. (1990). "The complete cDNA and polypeptide sequences of human erythroid alpha-spectrin". J. Biol. Chem. 265 (8): 4434–43. PMID 1689726.
• Gallagher PG, Tse WT, Marchesi SL, et al. (1993). "A defect in alpha-spectrin mRNA accumulation in hereditary pyropoikilocytosis". Trans. Assoc. Am. Physicians. 104: 32–9. PMID 1845156.
• Floyd PB, Gallagher PG, Valentino LA, et al. (1991). "Heterogeneity of the molecular basis of hereditary pyropoikilocytosis and hereditary elliptocytosis associated with increased levels of the spectrin alpha I/74-kilodalton tryptic peptide". Blood. 78 (5): 1364–72. PMID 1878597.
• Shoeman RL, Kesselmier C, Mothes E, et al. (1991). "Non-viral cellular substrates for human immunodeficiency virus type 1 protease". FEBS Lett. 278 (2): 199–203. doi:10.1016/0014-5793(91)80116-K. PMID 1991513.
• Garbarz M, Tse WT, Gallagher PG, et al. (1991). "Spectrin Rouen (beta 220-218), a novel shortened beta-chain variant in a kindred with hereditary elliptocytosis. Characterization of the molecular defect as exon skipping due to a splice site mutation". J. Clin. Invest. 88 (1): 76–81. doi:10.1172/JCI115307. PMC 296005. PMID 2056132.
• Tse WT, Gallagher PG, Pothier B, et al. (1991). "An insertional frameshift mutation of the beta-spectrin gene associated with elliptocytosis in spectrin nice (beta 220/216)". Blood. 78 (2): 517–23. PMID 2070088.