ID SPTA1_HUMAN Reviewed; 2419 AA. AC P02549; Q15514; Q5VYL1; Q5VYL2; Q6LDY5; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 05-OCT-2010, sequence version 5. DT 01-MAY-2013, entry version 163. DE RecName: Full=Spectrin alpha chain, erythrocytic 1; DE AltName: Full=Erythroid alpha-spectrin; GN Name=SPTA1; Synonyms=SPTA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND VARIANTS RP ALA-1163 AND ARG-1568. RX PubMed=1689726; RA Sahr K.E., Laurila P., Kotula L., Scarpa A.L., Coupal E., Leto T.L., RA Linnenbach A.J., Winkelmann J.C., Speicher D.W., Marchesi V.T., RA Curtis P.J., Forget B.G.; RT "The complete cDNA and polypeptide sequences of human erythroid alpha- RT spectrin."; RL J. Biol. Chem. 265:4434-4443(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 7-533, AND VARIANTS EL2 PRO-260; RP PRO-261 AND PRO-471. RX PubMed=2794061; DOI=10.1172/JCI114291; RA Sahr K.E., Tobe T., Scarpa A., Laughinghouse K., Marchesi S.L., RA Agre P., Linnenbach A.J., Marchesi V.T., Forget B.G.; RT "Sequence and exon-intron organization of the DNA encoding the alpha I RT domain of human spectrin. Application to the study of mutations RT causing hereditary elliptocytosis."; RL J. Clin. Invest. 84:1243-1252(1989). RN [4] RP PROTEIN SEQUENCE OF 7-601. RX PubMed=6654896; RA Speicher D.W., Davis G., Marchesi V.T.; RT "Structure of human erythrocyte spectrin. II. The sequence of the RT alpha-I domain."; RL J. Biol. Chem. 258:14938-14947(1983). RN [5] RP PROTEIN SEQUENCE OF 7-125. RX PubMed=6654895; RA Speicher D.W., Davis G., Yurchenco P.D., Marchesi V.T.; RT "Structure of human erythrocyte spectrin. I. Isolation of the alpha-I RT domain and its cyanogen bromide peptides."; RL J. Biol. Chem. 258:14931-14937(1983). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 320-450. RX PubMed=3458204; DOI=10.1073/pnas.83.8.2397; RA Linnenbach A.J., Speicher D.W., Marchesi V.T., Forget B.G.; RT "Cloning of a portion of the chromosomal gene for human erythrocyte RT alpha-spectrin by using a synthetic gene fragment."; RL Proc. Natl. Acad. Sci. U.S.A. 83:2397-2401(1986). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1451-1688, AND VARIANT ARG-1568. RX PubMed=3000887; DOI=10.1016/0378-1119(85)90191-X; RA Curtis P.J., Palumbo A., Ming J., Fraser P.J., Cioe L., Meo P., RA Shane S., Rovera G.; RT "Sequence comparison of human and murine erythrocyte alpha-spectrin RT cDNA."; RL Gene 36:357-362(1985). RN [8] RP PARTIAL PROTEIN SEQUENCE. RX PubMed=6472478; DOI=10.1038/311177a0; RA Speicher D.W., Marchesi V.T.; RT "Erythrocyte spectrin is comprised of many homologous triple helical RT segments."; RL Nature 311:177-180(1984). RN [9] RP PROTEIN SEQUENCE OF 7-16; 46-55; 680-689; 1047-1056 AND 1922-1931. RX PubMed=1634521; RA Speicher D.W., Weglarz L., DeSilva T.M.; RT "Properties of human red cell spectrin heterodimer (side-to-side) RT assembly and identification of an essential nucleation site."; RL J. Biol. Chem. 267:14775-14782(1992). RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 19-28; 39-44 AND 50-59. RX PubMed=7929303; RA Lusitani D.M., Qtaishat N., LaBrake C.C., Yu R.N., Davis J., RA Kelley M.R., Fung L.W.-M.; RT "The first human alpha-spectrin structural domain begins with RT serine."; RL J. Biol. Chem. 269:25955-25958(1994). RN [11] RP IDENTIFICATION OF PROBABLE FRAMESHIFT IN 2408-2419. RA Gibson T.J.; RL Unpublished observations (MAR-1995). RN [12] RP INTERACTION WITH FASLG. RX PubMed=19807924; DOI=10.1186/1471-2172-10-53; RA Voss M., Lettau M., Janssen O.; RT "Identification of SH3 domain interaction partners of human FasL RT (CD178) by phage display screening."; RL BMC Immunol. 10:53-53(2009). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [14] RP STRUCTURE BY NMR OF 1-156, AND SUBUNIT. RX PubMed=12672815; DOI=10.1074/jbc.M300617200; RA Park S., Caffrey M.S., Johnson M.E., Fung L.W.-M.; RT "Solution structural studies on human erythrocyte alpha-spectrin RT tetramerization site."; RL J. Biol. Chem. 278:21837-21844(2003). RN [15] RP REVIEW ON VARIANTS. RX PubMed=8844207; RX DOI=10.1002/(SICI)1098-1004(1996)8:2<97::AID-HUMU1>3.3.CO;2-W; RA Maillet P., Alloisio N., Morle L., Delaunay J.; RT "Spectrin mutations in hereditary elliptocytosis and hereditary RT spherocytosis."; RL Hum. Mutat. 8:97-107(1996). RN [16] RP VARIANT EL2 SER-24. RX PubMed=8018926; RA Parquet N., Devaux I., Boulanger L., Galand C., Boivin P., RA Lecomte M.-C., Dhermy D., Garbarz M.; RT "Identification of three novel spectrin alpha I/74 mutations in RT hereditary elliptocytosis: further support for a triple-stranded RT folding unit model of the spectrin heterodimer contact site."; RL Blood 84:303-308(1994). RN [17] RP VARIANTS EL2 CYS-28; HIS-28; LEU-28 AND SER-28. RX PubMed=1679439; DOI=10.1172/JCI115371; RA Coetzer T.L., Sahr K., Prchal J., Blacklock H., Peterson L., Koler R., RA Doyle J., Manaster J., Palek J.; RT "Four different mutations in codon 28 of alpha spectrin are associated RT with structurally and functionally abnormal spectrin alpha I/74 in RT hereditary elliptocytosis."; RL J. Clin. Invest. 88:743-749(1991). RN [18] RP VARIANT EL2 SER-28, AND VARIANT HPP ARG-48. RX PubMed=1878597; RA Floyd P.B., Gallagher P.G., Valentino L.A., Davis M., Marchesi S.L., RA Forget B.G.; RT "Heterogeneity of the molecular basis of hereditary pyropoikilocytosis RT and hereditary elliptocytosis associated with increased levels of the RT spectrin alpha I/74-kilodalton tryptic peptide."; RL Blood 78:1364-1372(1991). RN [19] RP VARIANT EL2 SER-45. RX PubMed=2568862; RA Lecomte M.-C., Garbarz M., Grandchamp B., Feo C., Gautero H., RA Devaux I., Bournier O., Galand C., D'Auriol L., Galibert F., RA Sahr K.E., Forget B.G., Boivin P., Dhermy D.; RT "Sp alpha I/78: a mutation of the alpha I spectrin domain in a white RT kindred with HE and HPP phenotypes."; RL Blood 74:1126-1133(1989). RN [20] RP VARIANT EL2/HPP PRO-207. RX PubMed=1541680; DOI=10.1172/JCI115669; RA Gallagher P.G., Tse W.T., Coetzer T., Lecomte M.-C., Garbarz M., RA Zarkowsky H.S., Baruchel A., Ballas S.K., Dhermy D., Palek J., RA Forget B.G.; RT "A common type of the spectrin alpha I 46-50a-kD peptide abnormality RT in hereditary elliptocytosis and pyropoikilocytosis is associated with RT a mutation distant from the proteolytic cleavage site. Evidence for RT the functional importance of the triple helical model of spectrin."; RL J. Clin. Invest. 89:892-898(1992). RN [21] RP VARIANT VAL-1858. RX PubMed=8486776; DOI=10.1172/JCI116432; RA Wilmotte R., Marechal J., Morle L., Baklouti F., Philippe N., RA Kastally R., Kotula L., Delaunay J., Alloisio N.; RT "Low expression allele alpha LELY of red cell spectrin is associated RT with mutations in exon 40 (alpha V/41 polymorphism) and intron 45 and RT with partial skipping of exon 46."; RL J. Clin. Invest. 91:2091-2096(1993). RN [22] RP VARIANT EL2 BARCELONA PRO-469. RX PubMed=8364215; RA dalla Venezia N., Alloisio N., Forissier A., Denoroy L., Aymerich M., RA Vives-Corrons J.L., Besalduch J., Besson I., Delaunay J.; RT "Elliptopoikilocytosis associated with the alpha 469 His-->Pro RT mutation in spectrin Barcelona (alpha I/50-46b)."; RL Blood 82:1661-1665(1993). RN [23] RP VARIANT CAGLIARI GLY-2025. RX PubMed=8226774; RA Sahr K.E., Coetzer T.L., Moy L.S., Derick L.H., Chishti A.H., RA Jarolim P., Lorenzo F., del Giudice E.M., Iolascon A., Gallanello R., RA Cao A., Delaunay J., Liu S.-C., Palek J.; RT "Spectrin Cagliari: an Ala-->Gly substitution in helix 1 of beta RT spectrin repeat 17 that severely disrupts the structure and self- RT association of the erythrocyte spectrin heterodimer."; RL J. Biol. Chem. 268:22656-22662(1993). RN [24] RP VARIANT EL2 CULOZ VAL-46, AND VARIANT EL2 LYON PHE-49. RX PubMed=2384601; DOI=10.1172/JCI114743; RA Morle L., Roux A.-F., Alloisio N., Pothier B., Starck J., Denoroy J., RA Morle F., Rudigoz R.-C., Forget B.G., Delaunay J., Godet J.; RT "Two elliptocytogenic alpha I/74 variants of the spectrin alpha I RT domain. Spectrin Culoz (GGT-->GTT; alpha I 40 Gly-->Val) and spectrin RT Lyon (CTT-->TTT; alpha I 43 Leu-->Phe)."; RL J. Clin. Invest. 86:548-554(1990). RN [25] RP VARIANT EL2 JENDOUBA GLU-791. RX PubMed=1638030; RA Alloisio N., Wilmotte R., Morle L., Baklouti F., Marechal J., RA Ducluzeau M.-T., Denoroy L., Feo C., Forget B.G., Kastally R., RA Delaunay J.; RT "Spectrin Jendouba: an alpha II/31 spectrin variant that is associated RT with elliptocytosis and carries a mutation distant from the dimer RT self-association site."; RL Blood 80:809-815(1992). RN [26] RP VARIANT EL2 TUNIS TRP-41. RX PubMed=2568861; RA Morle L., Morle F., Roux A.-F., Godet J., Forget B.G., Denoroy L., RA Garbarz M., Dhermy D., Kastally R., Delaunay J.; RT "Spectrin Tunis (Sp alpha I/78), an elliptocytogenic variant, is due RT to the CGG-->TGG codon change (Arg-->Trp) at position 35 of the alpha RT I domain."; RL Blood 74:828-832(1989). RN [27] RP VARIANT EL2 GENOVA TRP-34. RX PubMed=8193371; RA Perrotta S., del Giudice E.M., Alloisio N., Sciarratta G., Pinto L., RA Delaunay J., Cutillo S., Lolascon A.; RT "Mild elliptocytosis associated with the alpha 34 Arg-->Trp mutation RT in spectrin Genova (alpha I/74)."; RL Blood 83:3346-3349(1994). RN [28] RP VARIANT EL2 ANASTASIA THR-45. RX PubMed=7772539; RA Perrotta S., Iolascon A., de Angelis F., Pagano L., Colonna G., RA Cutillo S., del Giudice E.M.; RT "Spectrin Anastasia (alpha I/78): a new spectrin variant (alpha 45 RT Arg-->Thr) with moderate elliptocytogenic potential."; RL Br. J. Haematol. 89:933-936(1995). CC -!- FUNCTION: Spectrin is the major constituent of the cytoskeletal CC network underlying the erythrocyte plasma membrane. It associates CC with band 4.1 and actin to form the cytoskeletal superstructure of CC the erythrocyte plasma membrane. CC -!- SUBUNIT: Composed of non-homologous chains, alpha and beta, which CC aggregate side-to-side in an antiparallel fashion to form dimers, CC tetramers, and higher polymers. Interacts with FASLG. CC -!- INTERACTION: CC Q8IZP0:ABI1; NbExp=2; IntAct=EBI-375617, EBI-375446; CC Q01082:SPTBN1; NbExp=3; IntAct=EBI-375617, EBI-351561; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cell CC cortex. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P02549-1; Sequence=Displayed; CC Name=2; CC IsoId=P02549-2; Sequence=VSP_037662; CC Note=Gene prediction based on EST data; CC -!- DISEASE: Elliptocytosis 2 (EL2) [MIM:130600]: A Rhesus-unlinked CC form of hereditary elliptocytosis, a genetically heterogeneous, CC autosomal dominant hematologic disorder. It is characterized by CC variable hemolytic anemia and elliptical or oval red cell shape. CC Note=The disease is caused by mutations affecting the gene CC represented in this entry. CC -!- DISEASE: Hereditary pyropoikilocytosis (HPP) [MIM:266140]: CC Autosomal recessive hematologic disorder characterized by CC hemolytic anemia, microspherocytosis, poikilocytosis, and an CC unusual thermal sensitivity of red cells. Note=The disease is CC caused by mutations affecting the gene represented in this entry. CC -!- DISEASE: Spherocytosis 3 (SPH3) [MIM:270970]: Spherocytosis is a CC hematologic disorder leading to chronic hemolytic anemia and CC characterized by numerous abnormally shaped erythrocytes which are CC generally spheroidal. SPH3 is characterized by severe hemolytic CC anemia. Inheritance is autosomal recessive. Note=The disease is CC caused by mutations affecting the gene represented in this entry. CC -!- MISCELLANEOUS: This complex is anchored to the cytoplasmic face of CC the plasma membrane via another protein, ankyrin, which binds to CC beta-spectrin and mediates the binding of the whole complex to a CC transmembrane protein band 3. The interaction of erythrocyte CC spectrin with other proteins through specific binding domains lead CC to the formation of an extensive subplasmalemmal meshwork which is CC thought to be responsible for the maintenance of the biconcave CC shape of human erythrocytes, for the regulation of plasma membrane CC components and for the maintenance of the lipid asymmetry of the CC plasma membrane. CC -!- SIMILARITY: Belongs to the spectrin family. CC -!- SIMILARITY: Contains 3 EF-hand domains. CC -!- SIMILARITY: Contains 1 SH3 domain. CC -!- SIMILARITY: Contains 21 spectrin repeats. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M61826; AAA60994.1; -; Genomic_DNA. DR EMBL; M61776; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61777; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61778; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61779; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61780; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61781; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61782; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61783; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61852; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61784; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61785; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61787; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61788; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61789; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61791; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61792; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61793; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61794; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61795; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61796; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61797; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61798; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61799; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61800; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61801; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61802; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61803; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61804; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61805; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61806; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61807; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61808; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61809; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61810; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61811; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61812; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61814; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61815; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61816; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61817; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61818; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61819; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61820; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61821; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61822; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61823; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61824; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61825; AAA60994.1; JOINED; Genomic_DNA. DR EMBL; M61877; AAA60577.1; -; mRNA. DR EMBL; AL353894; CAH73936.1; -; Genomic_DNA. DR EMBL; AL353894; CAH73937.1; -; Genomic_DNA. DR EMBL; M29994; AAA60575.1; -; Genomic_DNA. DR EMBL; M29983; AAA60575.1; JOINED; Genomic_DNA. DR EMBL; M29984; AAA60575.1; JOINED; Genomic_DNA. DR EMBL; M29985; AAA60575.1; JOINED; Genomic_DNA. DR EMBL; M29986; AAA60575.1; JOINED; Genomic_DNA. DR EMBL; M29987; AAA60575.1; JOINED; Genomic_DNA. DR EMBL; M29988; AAA60575.1; JOINED; Genomic_DNA. DR EMBL; M29989; AAA60575.1; JOINED; Genomic_DNA. DR EMBL; M29990; AAA60575.1; JOINED; Genomic_DNA. DR EMBL; M29991; AAA60575.1; JOINED; Genomic_DNA. DR EMBL; M29992; AAA60575.1; JOINED; Genomic_DNA. DR EMBL; M29993; AAA60575.1; JOINED; Genomic_DNA. DR EMBL; M13233; AAA53103.1; -; Genomic_DNA. DR EMBL; M11049; AAA60569.1; -; mRNA. DR IPI; IPI00220741; -. DR IPI; IPI00641363; -. DR PIR; A35716; SJHUA. DR RefSeq; NP_003117.2; NM_003126.2. DR UniGene; Hs.119825; -. DR PDB; 1OWA; NMR; -; A=1-156. DR PDB; 3LBX; X-ray; 2.80 A; A=1-158. DR PDBsum; 1OWA; -. DR PDBsum; 3LBX; -. DR ProteinModelPortal; P02549; -. DR SMR; P02549; 1-953, 993-1034, 1049-2264, 2275-2377. DR DIP; DIP-1020N; -. DR DIP; DIP-17031N; -. DR IntAct; P02549; 8. DR STRING; 9606.ENSP00000357130; -. DR PhosphoSite; P02549; -. DR DMDM; 308153675; -. DR PaxDb; P02549; -. DR PRIDE; P02549; -. DR DNASU; 6708; -. DR Ensembl; ENST00000368147; ENSP00000357129; ENSG00000163554. DR Ensembl; ENST00000368148; ENSP00000357130; ENSG00000163554. DR GeneID; 6708; -. DR KEGG; hsa:6708; -. DR UCSC; uc001fst.1; human. DR CTD; 6708; -. DR GeneCards; GC01M158580; -. DR H-InvDB; HIX0028529; -. DR HGNC; HGNC:11272; SPTA1. DR HPA; HPA028048; -. DR MIM; 130600; phenotype. DR MIM; 182860; gene. DR MIM; 266140; phenotype. DR MIM; 270970; phenotype. DR neXtProt; NX_P02549; -. DR Orphanet; 98864; Common hereditary elliptocytosis. DR Orphanet; 288; Hereditary elliptocytosis. DR Orphanet; 98867; Hereditary pyropoikilocytosis. DR Orphanet; 822; Hereditary spherocytosis. DR PharmGKB; PA36101; -. DR eggNOG; NOG237318; -. DR HOGENOM; HOG000246965; -. DR HOVERGEN; HBG059266; -. DR InParanoid; P02549; -. DR KO; K06114; -. DR OMA; EFWLSEA; -. DR OrthoDB; EOG4PC9R6; -. DR Reactome; REACT_111045; Developmental Biology. DR Reactome; REACT_127416; Developmental Biology. DR ChiTaRS; SPTA1; human. DR EvolutionaryTrace; P02549; -. DR GenomeRNAi; 6708; -. DR NextBio; 26158; -. DR ArrayExpress; P02549; -. DR Bgee; P02549; -. DR CleanEx; HS_SPTA1; -. DR Genevestigator; P02549; -. DR GermOnline; ENSG00000163554; Homo sapiens. DR GO; GO:0032437; C:cuticular plate; IEA:Compara. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0031235; C:intrinsic to internal side of plasma membrane; TAS:BHF-UCL. DR GO; GO:0008091; C:spectrin; TAS:ProtInc. DR GO; GO:0014731; C:spectrin-associated cytoskeleton; IDA:BHF-UCL. DR GO; GO:0051015; F:actin filament binding; TAS:ProtInc. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc. DR GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW. DR GO; GO:0007015; P:actin filament organization; TAS:ProtInc. DR GO; GO:0007411; P:axon guidance; TAS:Reactome. DR GO; GO:0030097; P:hemopoiesis; IEA:Compara. DR GO; GO:0002260; P:lymphocyte homeostasis; IEA:Compara. DR GO; GO:0007009; P:plasma membrane organization; IEA:Compara. DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:Compara. DR GO; GO:0032092; P:positive regulation of protein binding; IEA:Compara. DR GO; GO:0042102; P:positive regulation of T cell proliferation; IEA:Compara. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR Gene3D; 1.10.238.10; -; 2. DR InterPro; IPR011992; EF-hand-like_dom. DR InterPro; IPR014837; EF-hand_Ca_insen. DR InterPro; IPR002048; EF_hand_dom. DR InterPro; IPR001452; SH3_domain. DR InterPro; IPR018159; Spectrin/alpha-actinin. DR InterPro; IPR013315; Spectrin_alpha_SH3. DR InterPro; IPR002017; Spectrin_repeat. DR Pfam; PF08726; efhand_Ca_insen; 1. DR Pfam; PF00018; SH3_1; 1. DR Pfam; PF00435; Spectrin; 20. DR PRINTS; PR01887; SPECTRNALPHA. DR SMART; SM00054; EFh; 2. DR SMART; SM00326; SH3; 1. DR SMART; SM00150; SPEC; 20. DR SUPFAM; SSF50044; SH3; 1. DR PROSITE; PS50222; EF_HAND_2; 3. DR PROSITE; PS50002; SH3; 1. PE 1: Evidence at protein level; KW 3D-structure; Actin capping; Actin-binding; Alternative splicing; KW Calcium; Cell shape; Complete proteome; Cytoplasm; Cytoskeleton; KW Direct protein sequencing; Disease mutation; Elliptocytosis; KW Hereditary hemolytic anemia; Metal-binding; Polymorphism; KW Pyropoikilocytosis; Reference proteome; Repeat; SH3 domain. FT CHAIN 1 2419 Spectrin alpha chain, erythrocytic 1. FT /FTId=PRO_0000073452. FT REPEAT 19 51 Spectrin 1. FT REPEAT 53 156 Spectrin 2. FT REPEAT 158 262 Spectrin 3. FT REPEAT 264 368 Spectrin 4. FT REPEAT 370 474 Spectrin 5. FT REPEAT 476 580 Spectrin 6. FT REPEAT 582 685 Spectrin 7. FT REPEAT 687 791 Spectrin 8. FT REPEAT 793 897 Spectrin 9. FT REPEAT 899 968 Spectrin 10. FT DOMAIN 977 1036 SH3. FT REPEAT 1082 1181 Spectrin 11. FT REPEAT 1183 1287 Spectrin 12. FT REPEAT 1289 1393 Spectrin 13. FT REPEAT 1395 1498 Spectrin 14. FT REPEAT 1500 1605 Spectrin 15. FT REPEAT 1607 1711 Spectrin 16. FT REPEAT 1713 1817 Spectrin 17. FT REPEAT 1819 1926 Spectrin 18. FT REPEAT 1928 2033 Spectrin 19. FT REPEAT 2043 2147 Spectrin 20. FT REPEAT 2157 2258 Spectrin 21. FT DOMAIN 2271 2306 EF-hand 1. FT DOMAIN 2314 2349 EF-hand 2. FT DOMAIN 2352 2386 EF-hand 3. FT CA_BIND 2284 2295 1 (Potential). FT CA_BIND 2327 2338 2 (Potential). FT VAR_SEQ 1889 1891 Missing (in isoform 2). FT /FTId=VSP_037662. FT VARIANT 24 24 I -> S (in EL2; Lograno). FT /FTId=VAR_001324. FT VARIANT 28 28 R -> C (in EL2). FT /FTId=VAR_001328. FT VARIANT 28 28 R -> H (in EL2; Corbeil; FT dbSNP:rs28934004). FT /FTId=VAR_001325. FT VARIANT 28 28 R -> L (in EL2). FT /FTId=VAR_001326. FT VARIANT 28 28 R -> S (in EL2; dbSNP:rs28934005). FT /FTId=VAR_001327. FT VARIANT 31 31 V -> A (in EL2; Marseille). FT /FTId=VAR_001329. FT VARIANT 34 34 R -> W (in EL2; Genova). FT /FTId=VAR_001330. FT VARIANT 41 41 R -> W (in EL2; Tunis). FT /FTId=VAR_001331. FT VARIANT 45 45 R -> S (in EL2; Clichy). FT /FTId=VAR_001332. FT VARIANT 45 45 R -> T (in EL2; Anastasia). FT /FTId=VAR_001333. FT VARIANT 46 46 G -> V (in EL2; Culoz). FT /FTId=VAR_001334. FT VARIANT 48 48 K -> R (in HPP). FT /FTId=VAR_001335. FT VARIANT 49 49 L -> F (in EL2; Lyon). FT /FTId=VAR_001336. FT VARIANT 109 109 S -> F (in dbSNP:rs3737521). FT /FTId=VAR_038506. FT VARIANT 151 151 G -> D (in EL2; Ponte de Sor). FT /FTId=VAR_001337. FT VARIANT 152 152 D -> N (in dbSNP:rs16840544). FT /FTId=VAR_038507. FT VARIANT 154 154 L -> LL (in EL2). FT /FTId=VAR_001338. FT VARIANT 207 207 L -> P (in EL2 and HPP; Saint-Louis). FT /FTId=VAR_001339. FT VARIANT 260 260 L -> P (in EL2; Nigerian). FT /FTId=VAR_001340. FT VARIANT 261 261 S -> P (in EL2). FT /FTId=VAR_001341. FT VARIANT 469 469 H -> P (in EL2; Barcelona). FT /FTId=VAR_001342. FT VARIANT 469 469 Missing (in EL2; Alexandria). FT /FTId=VAR_001343. FT VARIANT 471 471 Q -> P (in EL2). FT /FTId=VAR_001344. FT VARIANT 701 701 R -> H (in dbSNP:rs12090314). FT /FTId=VAR_001345. FT VARIANT 766 766 A -> T (in dbSNP:rs11265047). FT /FTId=VAR_038508. FT VARIANT 791 791 D -> E (in EL2; Jendouba; FT dbSNP:rs7418956). FT /FTId=VAR_001346. FT VARIANT 809 809 I -> V (in dbSNP:rs7547313). FT /FTId=VAR_001347. FT VARIANT 853 853 T -> R (in dbSNP:rs35121052). FT /FTId=VAR_001348. FT VARIANT 957 957 A -> V (in dbSNP:rs34706737). FT /FTId=VAR_038509. FT VARIANT 970 970 A -> D (in dbSNP:rs35948326). FT /FTId=VAR_001349. FT VARIANT 1163 1163 S -> A (in dbSNP:rs2482965). FT /FTId=VAR_038510. FT VARIANT 1330 1330 R -> I (in dbSNP:rs34214405). FT /FTId=VAR_038511. FT VARIANT 1568 1568 C -> R (in dbSNP:rs863931). FT /FTId=VAR_038512. FT VARIANT 1693 1693 K -> Q (in dbSNP:rs857725). FT /FTId=VAR_059199. FT VARIANT 1836 1836 N -> S (in dbSNP:rs16830483). FT /FTId=VAR_059200. FT VARIANT 1858 1858 L -> V (in dbSNP:rs3737515). FT /FTId=VAR_001350. FT VARIANT 2025 2025 A -> G (in Cagliari). FT /FTId=VAR_001351. FT VARIANT 2265 2265 I -> T (in dbSNP:rs952094). FT /FTId=VAR_059201. FT CONFLICT 119 130 Missing (in Ref. 3; AAA60575). FT CONFLICT 395 395 A -> G (in Ref. 3; AAA60575). FT CONFLICT 1410 1410 W -> R (in Ref. 1; AAA60577/AAA60994). FT CONFLICT 1570 1570 Missing (in Ref. 1; AAA60577/AAA60994 and FT 7; AAA60569). FT CONFLICT 1891 1891 Q -> H (in Ref. 1; AAA60577/AAA60994). FT CONFLICT 2400 2419 GRSHLSGYDYVGFTNSYFGN -> VEAISLAMTTLASPIPT FT LATNKQLLVDRRKS (in Ref. 1; AAA60577/ FT AAA60994). FT STRAND 12 14 FT HELIX 24 26 FT HELIX 27 30 FT HELIX 31 33 FT HELIX 34 77 FT HELIX 87 118 FT HELIX 126 156 SQ SEQUENCE 2419 AA; 280014 MW; B60680145C58DF55 CRC64; MEQFPKETVV ESSGPKVLET AEEIQERRQE VLTRYQSFKE RVAERGQKLE DSYHLQVFKR DADDLGKWIM EKVNILTDKS YEDPTNIQGK YQKHQSLEAE VQTKSRLMSE LEKTREERFT MGHSAHEETK AHIEELRHLW DLLLELTLEK GDQLLRALKF QQYVQECADI LEWIGDKEAI ATSVELGEDW ERTEVLHKKF EDFQVELVAK EGRVVEVNQY ANECAEENHP DLPLIQSKQN EVNAAWERLR GLALQRQKAL SNAANLQRFK RDVTEAIQWI KEKEPVLTSE DYGKDLVASE GLFHSHKGLE RNLAVMSDKV KELCAKAEKL TLSHPSDAPQ IQEMKEDLVS SWEHIRALAT SRYEKLQATY WYHRFSSDFD ELSGWMNEKT AAINADELPT DVAGGEVLLD RHQQHKHEID SYDDRFQSAD ETGQDLVNAN HEASDEVREK MEILDNNWTA LLELWDERHR QYEQCLDFHL FYRDSEQVDS WMSRQEAFLE NEDLGNSLGS AEALLQKHED FEEAFTAQEE KIITVDKTAT KLIGDDHYDS ENIKAIRDGL LARRDALREK AATRRRLLKE SLLLQKLYED SDDLKNWINK KKKLADDEDY KDIQNLKSRV QKQQVFEKEL AVNKTQLENI QKTGQEMIEG GHYASDNVTT RLSEVASLWE ELLEATKQKG TQLHEANQQL QFENNAEDLQ RWLEDVEWQV TSEDYGKGLA EVQNRLRKHG LLESAVAARQ DQVDILTDLA AYFEEIGHPD SKDIRARQES LVCRFEALKE PLATRKKKLL DLLHLQLICR DTEDEEAWIQ ETEPSATSTY LGKDLIASKK LLNRHRVILE NIASHEPRIQ EITERGNKMV EEGHFAAEDV ASRVKSLNQN MESLRARAAR RQNDLEANVQ FQQYLADLHE AETWIREKEP IVDNTNYGAD EEAAGALLKK HEAFLLDLNS FGDSMKALRN QANACQQQQA APVEGVAGEQ RVMALYDFQA RSPREVTMKK GDVLTLLSSI NKDWWKVEAA DHQGIVPAVY VRRLAHDEFP MLPQRRREEP GNITQRQEQI ENQYRSLLDR AEERRRRLLQ RYNEFLLAYE AGDMLEWIQE KKAENTGVEL DDVWELQKKF DEFQKDLNTN EPRLRDINKV ADDLLFEGLL TPEGAQIRQE LNSRWGSLQR LADEQRQLLG SAHAVEVFHR EADDTKEQIE KKCQALSAAD PGSDLFSVQA LQRRHEGFER DLVPLGDKVT ILGETAERLS ESHPDATEDL QRQKMELNEA WEDLQGRTKD RKESLNEAQK FYLFLSKARD LQNWISSIGG MVSSQELAED LTGIEILLER HQEHRADMEA EAPTFQALED FSAELIDSGH HASPEIEKKL QAVKLERDDL EKAWEKRKKI LDQCLELQMF QGNCDQVESW MVARENSLRS DDKSSLDSLE ALMKKRDDLD KAITAQEGKI TDLEHFAESL IADEHYAKEE IATRLQRVLD RWKALKAQLI DERTKLGDYA NLKQFYRDLE ELEEWISEML PTACDESYKD ATNIQRKYLK HQTFAHEVDG RSEQVHGVIN LGNSLIECSA CDGNEEAMKE QLEQLKEHWD HLLERTNDKG KKLNEASRQQ RFNTSIRDFE FWLSEAETLL AMKDQARDLA SAGNLLKKHQ LLEREMLARE DALKDLNTLA EDLLSSGTFN VDQIVKKKDN VNKRFLNVQE LAAAHHEKLK EAYALFQFFQ DLDDEESWIE EKLIRVSSQD YGRDLQGVQN LLKKHKRLEG ELVAHEPAIQ NVLDMAEKLK DKAAVGQEEI QLRLAQFVEH WEKLKELAKA RGLKLEESLE YLQFMQNAEE EEAWINEKNA LAVRGDCGDT LAATQSLLMK HEALENDFAV HETRVQNVCA QGEDILNKVL QEESQNKEIS SKIEALNEKT PSLAKAIAAW KLQLEDDYAF QEFNWKADVV EAWIADKETS LKTNGNGADL GDFLTLLAKQ DTLDASLQSF QQERLPEITD LKDKLISAQH NQSKAIEERY AALLKRWEQL LEASAVHRQK LLEKQLPLQK AEDLFVEFAH KASALNNWCE KMEENLSEPV HCVSLNEIRQ LQKDHEDFLA SLARAQADFK CLLELDQQIK ALGVPSSPYT WLTVEVLERT WKHLSDIIEE REQELQKEEA RQVKNFEMCQ EFEQNASTFL QWILETRAYF LDGSLLKETG TLESQLEANK RKQKEIQAMK RQLTKIVDLG DNLEDALILD IKYSTIGLAQ QWDQLYQLGL RMQHNLEQQI QAKDIKGVSE ETLKEFSTIY KHFDENLTGR LTHKEFRSCL RGLNYYLPMV EEDEHEPKFE KFLDAVDPGR KGYVSLEDYT AFLIDKESEN IKSSDEIENA FQALAEGKSY ITKEDMKQAL TPEQVSFCAT HMQQYMDPRG RSHLSGYDYV GFTNSYFGN //