SPTA1

From Wikipedia, the free encyclopedia

Spectrin, alpha, erythrocytic 1 (elliptocytosis 2)

PDB rendering based on 1owa.

Available structures: 1owa

Identifiers

Symbol(s)

SPTA1; EL2; SPTA

External IDs

OMIM: 182860 MGI: 98385 HomoloGene: 74460

Gene ontology
Molecular Function:	• structural constituent of cytoskeleton • calcium ion binding • protein binding • actin filament binding
Cellular Component:	• membrane fraction • cytoskeleton • spectrin • membrane
Biological Process:	• actin filament organization • regulation of cell shape • barbed-end actin filament capping

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_003126 (mRNA)
NP_003117 (protein)

NM_011465 (mRNA)
NP_035595 (protein)

Location

Chr 1: 156.85 - 156.92 Mb

Chr 1: 176.01 - 176.08 Mb

Pubmed search

[1]

[2]

Spectrin, alpha, erythrocytic 1 (elliptocytosis 2), also known as SPTA1, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: SPTA1 spectrin, alpha, erythrocytic 1 (elliptocytosis 2).

[edit] 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. 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 ( Pt 13): 2331–43. PMID 10852813.
Delaunay J (2003). "Molecular basis of red cell membrane disorders.". Acta Haematol. 108 (4): 210–8. 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. 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. 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. 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. 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. 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. 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.