SPTA1_HUMAN
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 03-AUG-2022, entry version 242.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND VARIANTS ALA-1163
RP AND ARG-1568.
RX PubMed=1689726; DOI=10.1016/s0021-9258(19)39583-3;
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., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., 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., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., 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., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., 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., Agre P.,
RA 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 causing
RT hereditary elliptocytosis.";
RL J. Clin. Invest. 84:1243-1252(1989).
RN [4]
RP PROTEIN SEQUENCE OF 7-601.
RX PubMed=6654896; DOI=10.1016/s0021-9258(17)43754-9;
RA Speicher D.W., Davis G., Marchesi V.T.;
RT "Structure of human erythrocyte spectrin. II. The sequence of the alpha-I
RT domain.";
RL J. Biol. Chem. 258:14938-14947(1983).
RN [5]
RP PROTEIN SEQUENCE OF 7-125.
RX PubMed=6654895; DOI=10.1016/s0021-9258(17)43753-7;
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 alpha-
RT 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., Shane S.,
RA Rovera G.;
RT "Sequence comparison of human and murine erythrocyte alpha-spectrin 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; DOI=10.1016/s0021-9258(18)42107-2;
RA Speicher D.W., Weglarz L., DeSilva T.M.;
RT "Properties of human red cell spectrin heterodimer (side-to-side) assembly
RT 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; DOI=10.1016/s0021-9258(18)47141-4;
RA Lusitani D.M., Qtaishat N., LaBrake C.C., Yu R.N., Davis J., Kelley M.R.,
RA Fung L.W.-M.;
RT "The first human alpha-spectrin structural domain begins with 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 (CD178) by
RT 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., Buerckstuemmer T.,
RA 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-992 AND SER-1976, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
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 [17]
RP REVIEW ON VARIANTS.
RX PubMed=8844207;
RX DOI=10.1002/(sici)1098-1004(1996)8:2<97::aid-humu1>3.0.co;2-m;
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 [18]
RP VARIANT EL2 SER-24.
RX PubMed=8018926;
RA Parquet N., Devaux I., Boulanger L., Galand C., Boivin P., Lecomte M.-C.,
RA Dhermy D., Garbarz M.;
RT "Identification of three novel spectrin alpha I/74 mutations in hereditary
RT elliptocytosis: further support for a triple-stranded folding unit model of
RT the spectrin heterodimer contact site.";
RL Blood 84:303-308(1994).
RN [19]
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 with
RT structurally and functionally abnormal spectrin alpha I/74 in hereditary
RT elliptocytosis.";
RL J. Clin. Invest. 88:743-749(1991).
RN [20]
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 and
RT hereditary elliptocytosis associated with increased levels of the spectrin
RT alpha I/74-kilodalton tryptic peptide.";
RL Blood 78:1364-1372(1991).
RN [21]
RP VARIANT EL2 SER-45.
RX PubMed=2568862;
RA Lecomte M.-C., Garbarz M., Grandchamp B., Feo C., Gautero H., Devaux I.,
RA Bournier O., Galand C., D'Auriol L., Galibert F., Sahr K.E., Forget B.G.,
RA 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 [22]
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., Forget B.G.;
RT "A common type of the spectrin alpha I 46-50a-kD peptide abnormality in
RT hereditary elliptocytosis and pyropoikilocytosis is associated with a
RT mutation distant from the proteolytic cleavage site. Evidence for the
RT functional importance of the triple helical model of spectrin.";
RL J. Clin. Invest. 89:892-898(1992).
RN [23]
RP VARIANT VAL-1858.
RX PubMed=8486776; DOI=10.1172/jci116432;
RA Wilmotte R., Marechal J., Morle L., Baklouti F., Philippe N., Kastally R.,
RA Kotula L., Delaunay J., Alloisio N.;
RT "Low expression allele alpha LELY of red cell spectrin is associated with
RT mutations in exon 40 (alpha V/41 polymorphism) and intron 45 and with
RT partial skipping of exon 46.";
RL J. Clin. Invest. 91:2091-2096(1993).
RN [24]
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 mutation in
RT spectrin Barcelona (alpha I/50-46b).";
RL Blood 82:1661-1665(1993).
RN [25]
RP VARIANT CAGLIARI GLY-2025.
RX PubMed=8226774; DOI=10.1016/s0021-9258(18)41578-5;
RA Sahr K.E., Coetzer T.L., Moy L.S., Derick L.H., Chishti A.H., Jarolim P.,
RA Lorenzo F., del Giudice E.M., Iolascon A., Gallanello R., Cao A.,
RA Delaunay J., Liu S.-C., Palek J.;
RT "Spectrin Cagliari: an Ala-->Gly substitution in helix 1 of beta spectrin
RT repeat 17 that severely disrupts the structure and self-association of the
RT erythrocyte spectrin heterodimer.";
RL J. Biol. Chem. 268:22656-22662(1993).
RN [26]
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 domain.
RT Spectrin Culoz (GGT-->GTT; alpha I 40 Gly-->Val) and spectrin Lyon
RT (CTT-->TTT; alpha I 43 Leu-->Phe).";
RL J. Clin. Invest. 86:548-554(1990).
RN [27]
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., Delaunay J.;
RT "Spectrin Jendouba: an alpha II/31 spectrin variant that is associated with
RT elliptocytosis and carries a mutation distant from the dimer self-
RT association site.";
RL Blood 80:809-815(1992).
RN [28]
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 to the
RT CGG-->TGG codon change (Arg-->Trp) at position 35 of the alpha I domain.";
RL Blood 74:828-832(1989).
RN [29]
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 in
RT spectrin Genova (alpha I/74).";
RL Blood 83:3346-3349(1994).
RN [30]
RP VARIANT EL2 ANASTASIA THR-45.
RX PubMed=7772539;
RA Perrotta S., Iolascon A., de Angelis F., Pagano L., Colonna G., Cutillo S.,
RA 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 network
CC underlying the erythrocyte plasma membrane. It associates with band 4.1
CC and actin to form the cytoskeletal superstructure of the erythrocyte
CC 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 {ECO:0000269|PubMed:12672815, ECO:0000269|PubMed:19807924}.
CC -!- INTERACTION:
CC P02549; Q8IZP0: ABI1; NbExp=2; IntAct=EBI-375617, EBI-375446;
CC P02549; O14874: BCKDK; NbExp=3; IntAct=EBI-375617, EBI-1046765;
CC P02549; Q0VAL7: C21orf58; NbExp=3; IntAct=EBI-375617, EBI-10226774;
CC P02549; Q8N715: CCDC185; NbExp=3; IntAct=EBI-375617, EBI-740814;
CC P02549; Q9BY27: DGCR6L; NbExp=3; IntAct=EBI-375617, EBI-742953;
CC P02549; Q9NQT4: EXOSC5; NbExp=3; IntAct=EBI-375617, EBI-371876;
CC P02549; Q8TAE8: GADD45GIP1; NbExp=3; IntAct=EBI-375617, EBI-372506;
CC P02549; O95678: KRT75; NbExp=3; IntAct=EBI-375617, EBI-2949715;
CC P02549; A8MYP8: ODF3B; NbExp=3; IntAct=EBI-375617, EBI-12010090;
CC P02549; Q99959-2: PKP2; NbExp=3; IntAct=EBI-375617, EBI-10987518;
CC P02549; P11277: SPTB; NbExp=4; IntAct=EBI-375617, EBI-514908;
CC P02549; Q01082: SPTBN1; NbExp=3; IntAct=EBI-375617, EBI-351561;
CC P02549; Q9NRE2: TSHZ2; NbExp=3; IntAct=EBI-375617, EBI-10687282;
CC P02549; Q99757: TXN2; NbExp=3; IntAct=EBI-375617, EBI-2932492;
CC P02549; Q5BKZ1: ZNF326; NbExp=3; IntAct=EBI-375617, EBI-2560158;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cell 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 -!- DISEASE: Elliptocytosis 2 (EL2) [MIM:130600]: A Rhesus-unlinked form of
CC hereditary elliptocytosis, a genetically heterogeneous, autosomal
CC dominant hematologic disorder. It is characterized by variable
CC hemolytic anemia and elliptical or oval red cell shape.
CC {ECO:0000269|PubMed:1541680, ECO:0000269|PubMed:1638030,
CC ECO:0000269|PubMed:1679439, ECO:0000269|PubMed:1878597,
CC ECO:0000269|PubMed:2384601, ECO:0000269|PubMed:2568861,
CC ECO:0000269|PubMed:2568862, ECO:0000269|PubMed:2794061,
CC ECO:0000269|PubMed:7772539, ECO:0000269|PubMed:8018926,
CC ECO:0000269|PubMed:8193371, ECO:0000269|PubMed:8364215}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Hereditary pyropoikilocytosis (HPP) [MIM:266140]: Autosomal
CC recessive hematologic disorder characterized by hemolytic anemia,
CC microspherocytosis, poikilocytosis, and an unusual thermal sensitivity
CC of red cells. {ECO:0000269|PubMed:1878597}. Note=The disease is caused
CC by variants 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 anemia.
CC Inheritance is autosomal recessive. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: This complex is anchored to the cytoplasmic face of the
CC plasma membrane via another protein, ankyrin, which binds to beta-
CC spectrin and mediates the binding of the whole complex to a
CC transmembrane protein band 3. The interaction of erythrocyte spectrin
CC with other proteins through specific binding domains lead to the
CC formation of an extensive subplasmalemmal meshwork which is thought to
CC be responsible for the maintenance of the biconcave shape of human
CC erythrocytes, for the regulation of plasma membrane components and for
CC the maintenance of the lipid asymmetry of the plasma membrane.
CC -!- SIMILARITY: Belongs to the spectrin family. {ECO:0000305}.
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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; -; NOT_ANNOTATED_CDS; 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 CCDS; CCDS41423.1; -. [P02549-1]
DR PIR; A35716; SJHUA.
DR RefSeq; NP_003117.2; NM_003126.2. [P02549-1]
DR RefSeq; XP_011508218.1; XM_011509916.2. [P02549-1]
DR PDB; 1OWA; NMR; -; A=1-156.
DR PDB; 3LBX; X-ray; 2.80 A; A=1-158.
DR PDB; 5J4O; X-ray; 1.54 A; A=1599-1826.
DR PDBsum; 1OWA; -.
DR PDBsum; 3LBX; -.
DR PDBsum; 5J4O; -.
DR AlphaFoldDB; P02549; -.
DR SMR; P02549; -.
DR BioGRID; 112586; 83.
DR DIP; DIP-17031N; -.
DR IntAct; P02549; 28.
DR MINT; P02549; -.
DR STRING; 9606.ENSP00000357129; -.
DR GlyConnect; 2880; 1 O-Linked glycan (3 sites).
DR GlyGen; P02549; 4 sites, 1 O-linked glycan (4 sites).
DR iPTMnet; P02549; -.
DR PhosphoSitePlus; P02549; -.
DR BioMuta; SPTA1; -.
DR DMDM; 308153675; -.
DR EPD; P02549; -.
DR jPOST; P02549; -.
DR MassIVE; P02549; -.
DR MaxQB; P02549; -.
DR PaxDb; P02549; -.
DR PeptideAtlas; P02549; -.
DR PRIDE; P02549; -.
DR ProteomicsDB; 51533; -. [P02549-1]
DR ProteomicsDB; 51534; -. [P02549-2]
DR Antibodypedia; 10818; 177 antibodies from 28 providers.
DR DNASU; 6708; -.
DR Ensembl; ENST00000643759.2; ENSP00000495214.1; ENSG00000163554.15. [P02549-1]
DR GeneID; 6708; -.
DR KEGG; hsa:6708; -.
DR MANE-Select; ENST00000643759.2; ENSP00000495214.1; NM_003126.4; NP_003117.2.
DR UCSC; uc001fst.2; human. [P02549-1]
DR CTD; 6708; -.
DR DisGeNET; 6708; -.
DR GeneCards; SPTA1; -.
DR HGNC; HGNC:11272; SPTA1.
DR HPA; ENSG00000163554; Tissue enriched (bone).
DR MalaCards; SPTA1; -.
DR MIM; 130600; phenotype.
DR MIM; 182860; gene.
DR MIM; 266140; phenotype.
DR MIM; 270970; phenotype.
DR neXtProt; NX_P02549; -.
DR OpenTargets; ENSG00000163554; -.
DR Orphanet; 288; Hereditary elliptocytosis.
DR Orphanet; 822; Hereditary spherocytosis.
DR PharmGKB; PA36101; -.
DR VEuPathDB; HostDB:ENSG00000163554; -.
DR eggNOG; KOG0040; Eukaryota.
DR GeneTree; ENSGT00940000161240; -.
DR HOGENOM; CLU_000847_0_0_1; -.
DR InParanoid; P02549; -.
DR OMA; DYKDTQN; -.
DR OrthoDB; 1011028at2759; -.
DR PhylomeDB; P02549; -.
DR TreeFam; TF343803; -.
DR PathwayCommons; P02549; -.
DR Reactome; R-HSA-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-HSA-445095; Interaction between L1 and Ankyrins.
DR Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR SignaLink; P02549; -.
DR SIGNOR; P02549; -.
DR BioGRID-ORCS; 6708; 12 hits in 1074 CRISPR screens.
DR ChiTaRS; SPTA1; human.
DR EvolutionaryTrace; P02549; -.
DR GeneWiki; Spectrin,_alpha_1; -.
DR GenomeRNAi; 6708; -.
DR Pharos; P02549; Tbio.
DR PRO; PR:P02549; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P02549; protein.
DR Bgee; ENSG00000163554; Expressed in trabecular bone tissue and 108 other tissues.
DR Genevisible; P02549; HS.
DR GO; GO:0015629; C:actin cytoskeleton; TAS:BHF-UCL.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0032437; C:cuticular plate; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0031235; C:intrinsic component of the cytoplasmic side of the plasma membrane; TAS:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR GO; GO:0007015; P:actin filament organization; TAS:ProtInc.
DR GO; GO:0030097; P:hemopoiesis; IEA:Ensembl.
DR GO; GO:0002260; P:lymphocyte homeostasis; IEA:Ensembl.
DR GO; GO:0007009; P:plasma membrane organization; IEA:Ensembl.
DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:Ensembl.
DR GO; GO:0032092; P:positive regulation of protein binding; IEA:Ensembl.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IEA:Ensembl.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR CDD; cd00176; SPEC; 12.
DR DisProt; DP01700; -.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR014837; EF-hand_Ca_insen.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR Pfam; PF08726; EFhand_Ca_insen; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF00435; Spectrin; 20.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00150; SPEC; 20.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF50044; SSF50044; 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; Calcium;
KW Cell shape; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Disease variant; Elliptocytosis; Hereditary hemolytic anemia;
KW Metal-binding; Phosphoprotein; Pyropoikilocytosis; Reference proteome;
KW Repeat; SH3 domain.
FT CHAIN 1..2419
FT /note="Spectrin alpha chain, erythrocytic 1"
FT /id="PRO_0000073452"
FT REPEAT 53..155
FT /note="Spectrin 1"
FT /evidence="ECO:0000255"
FT REPEAT 159..261
FT /note="Spectrin 2"
FT /evidence="ECO:0000255"
FT REPEAT 265..367
FT /note="Spectrin 3"
FT /evidence="ECO:0000255"
FT REPEAT 371..474
FT /note="Spectrin 4"
FT /evidence="ECO:0000255"
FT REPEAT 477..580
FT /note="Spectrin 5"
FT /evidence="ECO:0000255"
FT REPEAT 583..685
FT /note="Spectrin 6"
FT /evidence="ECO:0000255"
FT REPEAT 688..790
FT /note="Spectrin 7"
FT /evidence="ECO:0000255"
FT REPEAT 794..896
FT /note="Spectrin 8"
FT /evidence="ECO:0000255"
FT REPEAT 900..969
FT /note="Spectrin 9"
FT /evidence="ECO:0000255"
FT DOMAIN 977..1036
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REPEAT 1087..1179
FT /note="Spectrin 10"
FT /evidence="ECO:0000255"
FT REPEAT 1185..1287
FT /note="Spectrin 11"
FT /evidence="ECO:0000255"
FT REPEAT 1290..1392
FT /note="Spectrin 12"
FT /evidence="ECO:0000255"
FT REPEAT 1396..1497
FT /note="Spectrin 13"
FT /evidence="ECO:0000255"
FT REPEAT 1501..1605
FT /note="Spectrin 14"
FT /evidence="ECO:0000255"
FT REPEAT 1608..1711
FT /note="Spectrin 15"
FT /evidence="ECO:0000255"
FT REPEAT 1714..1817
FT /note="Spectrin 16"
FT /evidence="ECO:0000255"
FT REPEAT 1820..1926
FT /note="Spectrin 17"
FT /evidence="ECO:0000255"
FT REPEAT 1929..2033
FT /note="Spectrin 18"
FT /evidence="ECO:0000255"
FT REPEAT 2044..2146
FT /note="Spectrin 19"
FT /evidence="ECO:0000255"
FT REPEAT 2158..2258
FT /note="Spectrin 20"
FT /evidence="ECO:0000255"
FT DOMAIN 2271..2306
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 2314..2349
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 2352..2386
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2284
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 2286
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 2288
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 2290
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 2295
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 2327
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 2333
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 2338
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT MOD_RES 992
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1976
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1889..1891
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_037662"
FT VARIANT 24
FT /note="I -> S (in EL2; Lograno)"
FT /evidence="ECO:0000269|PubMed:8018926"
FT /id="VAR_001324"
FT VARIANT 28
FT /note="R -> C (in EL2; dbSNP:rs121918642)"
FT /evidence="ECO:0000269|PubMed:1679439"
FT /id="VAR_001328"
FT VARIANT 28
FT /note="R -> H (in EL2; Corbeil; dbSNP:rs121918641)"
FT /evidence="ECO:0000269|PubMed:1679439"
FT /id="VAR_001325"
FT VARIANT 28
FT /note="R -> L (in EL2; dbSNP:rs121918641)"
FT /evidence="ECO:0000269|PubMed:1679439"
FT /id="VAR_001326"
FT VARIANT 28
FT /note="R -> S (in EL2; dbSNP:rs121918642)"
FT /evidence="ECO:0000269|PubMed:1679439,
FT ECO:0000269|PubMed:1878597"
FT /id="VAR_001327"
FT VARIANT 31
FT /note="V -> A (in EL2; Marseille; dbSNP:rs773826036)"
FT /id="VAR_001329"
FT VARIANT 34
FT /note="R -> W (in EL2; Genova; dbSNP:rs201568233)"
FT /evidence="ECO:0000269|PubMed:8193371"
FT /id="VAR_001330"
FT VARIANT 41
FT /note="R -> W (in EL2; Tunis; dbSNP:rs121918640)"
FT /evidence="ECO:0000269|PubMed:2568861"
FT /id="VAR_001331"
FT VARIANT 45
FT /note="R -> S (in EL2; Clichy; dbSNP:rs121918637)"
FT /evidence="ECO:0000269|PubMed:2568862"
FT /id="VAR_001332"
FT VARIANT 45
FT /note="R -> T (in EL2; Anastasia)"
FT /evidence="ECO:0000269|PubMed:7772539"
FT /id="VAR_001333"
FT VARIANT 46
FT /note="G -> V (in EL2; Culoz; dbSNP:rs121918638)"
FT /evidence="ECO:0000269|PubMed:2384601"
FT /id="VAR_001334"
FT VARIANT 48
FT /note="K -> R (in HPP; dbSNP:rs121918644)"
FT /evidence="ECO:0000269|PubMed:1878597"
FT /id="VAR_001335"
FT VARIANT 49
FT /note="L -> F (in EL2; Lyon; dbSNP:rs121918639)"
FT /evidence="ECO:0000269|PubMed:2384601"
FT /id="VAR_001336"
FT VARIANT 109
FT /note="S -> F (in dbSNP:rs3737521)"
FT /id="VAR_038506"
FT VARIANT 151
FT /note="G -> D (in EL2; Ponte de Sor; dbSNP:rs199725919)"
FT /id="VAR_001337"
FT VARIANT 152
FT /note="D -> N (in dbSNP:rs16840544)"
FT /id="VAR_038507"
FT VARIANT 154
FT /note="L -> LL (in EL2)"
FT /id="VAR_001338"
FT VARIANT 207
FT /note="L -> P (in EL2 and HPP; Saint-Louis;
FT dbSNP:rs121918643)"
FT /evidence="ECO:0000269|PubMed:1541680"
FT /id="VAR_001339"
FT VARIANT 260
FT /note="L -> P (in EL2; Nigerian; dbSNP:rs121918634)"
FT /evidence="ECO:0000269|PubMed:2794061"
FT /id="VAR_001340"
FT VARIANT 261
FT /note="S -> P (in EL2; dbSNP:rs121918636)"
FT /evidence="ECO:0000269|PubMed:2794061"
FT /id="VAR_001341"
FT VARIANT 469
FT /note="H -> P (in EL2; Barcelona)"
FT /evidence="ECO:0000269|PubMed:8364215"
FT /id="VAR_001342"
FT VARIANT 469
FT /note="Missing (in EL2; Alexandria)"
FT /id="VAR_001343"
FT VARIANT 471
FT /note="Q -> P (in EL2; dbSNP:rs121918635)"
FT /evidence="ECO:0000269|PubMed:2794061"
FT /id="VAR_001344"
FT VARIANT 701
FT /note="R -> H (in dbSNP:rs12090314)"
FT /id="VAR_001345"
FT VARIANT 766
FT /note="A -> T (in dbSNP:rs11265047)"
FT /id="VAR_038508"
FT VARIANT 791
FT /note="D -> E (in EL2; Jendouba; dbSNP:rs7418956)"
FT /evidence="ECO:0000269|PubMed:1638030"
FT /id="VAR_001346"
FT VARIANT 809
FT /note="I -> V (in dbSNP:rs7547313)"
FT /id="VAR_001347"
FT VARIANT 853
FT /note="T -> R (in dbSNP:rs35121052)"
FT /id="VAR_001348"
FT VARIANT 957
FT /note="A -> V (in dbSNP:rs34706737)"
FT /id="VAR_038509"
FT VARIANT 970
FT /note="A -> D (in dbSNP:rs35948326)"
FT /id="VAR_001349"
FT VARIANT 1163
FT /note="S -> A (in dbSNP:rs2482965)"
FT /evidence="ECO:0000269|PubMed:1689726"
FT /id="VAR_038510"
FT VARIANT 1330
FT /note="R -> I (in dbSNP:rs34214405)"
FT /id="VAR_038511"
FT VARIANT 1568
FT /note="C -> R (in dbSNP:rs863931)"
FT /evidence="ECO:0000269|PubMed:1689726,
FT ECO:0000269|PubMed:3000887"
FT /id="VAR_038512"
FT VARIANT 1693
FT /note="K -> Q (in dbSNP:rs857725)"
FT /id="VAR_059199"
FT VARIANT 1836
FT /note="N -> S (in dbSNP:rs16830483)"
FT /id="VAR_059200"
FT VARIANT 1858
FT /note="L -> V (in dbSNP:rs3737515)"
FT /evidence="ECO:0000269|PubMed:8486776"
FT /id="VAR_001350"
FT VARIANT 2025
FT /note="A -> G (in Cagliari)"
FT /evidence="ECO:0000269|PubMed:8226774"
FT /id="VAR_001351"
FT VARIANT 2265
FT /note="I -> T (in dbSNP:rs952094)"
FT /id="VAR_059201"
FT CONFLICT 119..130
FT /note="Missing (in Ref. 3; AAA60575)"
FT /evidence="ECO:0000305"
FT CONFLICT 395
FT /note="A -> G (in Ref. 3; AAA60575)"
FT /evidence="ECO:0000305"
FT CONFLICT 1410
FT /note="W -> R (in Ref. 1; AAA60577/AAA60994)"
FT /evidence="ECO:0000305"
FT CONFLICT 1570
FT /note="Missing (in Ref. 1; AAA60577/AAA60994 and 7;
FT AAA60569)"
FT /evidence="ECO:0000305"
FT CONFLICT 1891
FT /note="Q -> H (in Ref. 1; AAA60577/AAA60994)"
FT /evidence="ECO:0000305"
FT CONFLICT 2400..2419
FT /note="GRSHLSGYDYVGFTNSYFGN -> VEAISLAMTTLASPIPTLATNKQLLVDR
FT RKS (in Ref. 1; AAA60577/AAA60994)"
FT /evidence="ECO:0000305"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:1OWA"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:3LBX"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:3LBX"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:3LBX"
FT HELIX 34..77
FT /evidence="ECO:0007829|PDB:3LBX"
FT HELIX 87..118
FT /evidence="ECO:0007829|PDB:3LBX"
FT HELIX 126..156
FT /evidence="ECO:0007829|PDB:3LBX"
FT HELIX 1608..1631
FT /evidence="ECO:0007829|PDB:5J4O"
FT TURN 1632..1634
FT /evidence="ECO:0007829|PDB:5J4O"
FT HELIX 1639..1675
FT /evidence="ECO:0007829|PDB:5J4O"
FT HELIX 1681..1736
FT /evidence="ECO:0007829|PDB:5J4O"
FT HELIX 1745..1763
FT /evidence="ECO:0007829|PDB:5J4O"
FT HELIX 1766..1778
FT /evidence="ECO:0007829|PDB:5J4O"
FT STRAND 1780..1782
FT /evidence="ECO:0007829|PDB:5J4O"
FT HELIX 1783..1786
FT /evidence="ECO:0007829|PDB:5J4O"
FT HELIX 1788..1825
FT /evidence="ECO:0007829|PDB:5J4O"
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
