SFSWA_HUMAN
ID SFSWA_HUMAN Reviewed; 951 AA.
AC Q12872; B2RN45; B7ZM97; F5H6B8; Q6PJF7;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 3.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Splicing factor, suppressor of white-apricot homolog;
DE AltName: Full=Splicing factor, arginine/serine-rich 8;
DE AltName: Full=Suppressor of white apricot protein homolog;
GN Name=SFSWAP; Synonyms=SFRS8, SWAP;
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 [MRNA] (ISOFORM 1), AND VARIANTS GLN-52; PHE-136 AND
RP PRO-421.
RC TISSUE=Placenta;
RX PubMed=8206918; DOI=10.1016/s0021-9258(17)33989-3;
RA Denhez F., Lafyatis R.;
RT "Conservation of regulated alternative splicing and identification of
RT functional domains in vertebrate homologs to the Drosophila splicing
RT regulator, suppressor-of-white-apricot.";
RL J. Biol. Chem. 269:16170-16179(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PRO-421.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP PRO-421.
RC TISSUE=Brain, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION.
RX PubMed=8940107; DOI=10.1074/jbc.271.49.31106;
RA Sarkissian M., Winne A., Lafyatis R.;
RT "The mammalian homolog of suppressor-of-white-apricot regulates alternative
RT mRNA splicing of CD45 exon 4 and fibronectin IIICS.";
RL J. Biol. Chem. 271:31106-31114(1996).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-642, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283; SER-604 AND SER-909, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283 AND SER-909, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-315, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-604, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-604, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283; SER-832; SER-834 AND
RP SER-909, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-604, AND IDENTIFICATION BY
RP 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 189-282 AND 434-522.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the SURP1 and SURP2 domain in splicing factor,
RT arginine/serine-rich 8.";
RL Submitted (JUN-2007) to the PDB data bank.
CC -!- FUNCTION: Plays a role as an alternative splicing regulator. Regulate
CC its own expression at the level of RNA processing. Also regulates the
CC splicing of fibronectin and CD45 genes. May act, at least in part, by
CC interaction with other R/S-containing splicing factors. Represses the
CC splicing of MAPT/Tau exon 10. {ECO:0000269|PubMed:8940107}.
CC -!- INTERACTION:
CC Q12872; Q15637: SF1; NbExp=2; IntAct=EBI-1055938, EBI-744603;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q12872-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q12872-2; Sequence=VSP_044786;
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DR EMBL; U08377; AAA19604.1; -; mRNA.
DR EMBL; AC117500; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC131009; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW98526.1; -; Genomic_DNA.
DR EMBL; BC008707; AAH08707.1; -; mRNA.
DR EMBL; BC015953; AAH15953.1; -; mRNA.
DR EMBL; BC136678; AAI36679.1; -; mRNA.
DR EMBL; BC144364; AAI44365.1; -; mRNA.
DR CCDS; CCDS58290.1; -. [Q12872-2]
DR CCDS; CCDS9273.1; -. [Q12872-1]
DR PIR; A54037; A54037.
DR PIR; B54037; B54037.
DR PIR; C54037; C54037.
DR RefSeq; NP_001248340.1; NM_001261411.1. [Q12872-2]
DR RefSeq; NP_004583.2; NM_004592.3. [Q12872-1]
DR PDB; 2E5Z; NMR; -; A=440-522.
DR PDB; 2E60; NMR; -; A=189-282.
DR PDBsum; 2E5Z; -.
DR PDBsum; 2E60; -.
DR AlphaFoldDB; Q12872; -.
DR SMR; Q12872; -.
DR BioGRID; 112331; 78.
DR IntAct; Q12872; 18.
DR MINT; Q12872; -.
DR STRING; 9606.ENSP00000437738; -.
DR GlyGen; Q12872; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q12872; -.
DR PhosphoSitePlus; Q12872; -.
DR BioMuta; SFSWAP; -.
DR DMDM; 292495067; -.
DR EPD; Q12872; -.
DR jPOST; Q12872; -.
DR MassIVE; Q12872; -.
DR MaxQB; Q12872; -.
DR PaxDb; Q12872; -.
DR PeptideAtlas; Q12872; -.
DR PRIDE; Q12872; -.
DR ProteomicsDB; 27138; -.
DR ProteomicsDB; 58994; -. [Q12872-1]
DR Antibodypedia; 19429; 188 antibodies from 27 providers.
DR DNASU; 6433; -.
DR Ensembl; ENST00000261674.9; ENSP00000261674.4; ENSG00000061936.10. [Q12872-1]
DR Ensembl; ENST00000541286.5; ENSP00000437738.1; ENSG00000061936.10. [Q12872-2]
DR GeneID; 6433; -.
DR KEGG; hsa:6433; -.
DR MANE-Select; ENST00000261674.9; ENSP00000261674.4; NM_004592.4; NP_004583.2.
DR UCSC; uc001uja.3; human. [Q12872-1]
DR CTD; 6433; -.
DR DisGeNET; 6433; -.
DR GeneCards; SFSWAP; -.
DR HGNC; HGNC:10790; SFSWAP.
DR HPA; ENSG00000061936; Low tissue specificity.
DR MIM; 601945; gene.
DR neXtProt; NX_Q12872; -.
DR OpenTargets; ENSG00000061936; -.
DR PharmGKB; PA35706; -.
DR VEuPathDB; HostDB:ENSG00000061936; -.
DR eggNOG; KOG1847; Eukaryota.
DR GeneTree; ENSGT00940000153892; -.
DR HOGENOM; CLU_015459_0_0_1; -.
DR InParanoid; Q12872; -.
DR OMA; IAFNYDE; -.
DR OrthoDB; 1414730at2759; -.
DR PhylomeDB; Q12872; -.
DR TreeFam; TF106264; -.
DR PathwayCommons; Q12872; -.
DR SignaLink; Q12872; -.
DR BioGRID-ORCS; 6433; 577 hits in 1083 CRISPR screens.
DR ChiTaRS; SFSWAP; human.
DR EvolutionaryTrace; Q12872; -.
DR GenomeRNAi; 6433; -.
DR Pharos; Q12872; Tdark.
DR PRO; PR:Q12872; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q12872; protein.
DR Bgee; ENSG00000061936; Expressed in sural nerve and 205 other tissues.
DR ExpressionAtlas; Q12872; baseline and differential.
DR Genevisible; Q12872; HS.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IEA:Ensembl.
DR GO; GO:0000395; P:mRNA 5'-splice site recognition; IBA:GO_Central.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
DR Gene3D; 1.10.10.790; -; 2.
DR InterPro; IPR000061; Surp.
DR InterPro; IPR040397; SWAP.
DR InterPro; IPR035967; SWAP/Surp_sf.
DR InterPro; IPR019147; SWAP_N_domain.
DR PANTHER; PTHR13161; PTHR13161; 1.
DR Pfam; PF09750; DRY_EERY; 1.
DR Pfam; PF01805; Surp; 2.
DR SMART; SM01141; DRY_EERY; 1.
DR SMART; SM00648; SWAP; 2.
DR SUPFAM; SSF109905; SSF109905; 2.
DR PROSITE; PS50128; SURP; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; RNA-binding; Transcription; Transcription regulation.
FT CHAIN 1..951
FT /note="Splicing factor, suppressor of white-apricot
FT homolog"
FT /id="PRO_0000081934"
FT REPEAT 211..253
FT /note="SURP motif 1"
FT REPEAT 459..499
FT /note="SURP motif 2"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..423
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..684
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..755
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..814
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..862
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..904
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..927
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 315
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 642
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 832
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 834
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 905
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3USH5"
FT MOD_RES 909
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 801
FT /note="R -> RSRVTASPGTLRAEPCQSSASVTAAAEPGSYQAASTTTRFDSASSFE
FT GKPGKT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044786"
FT VARIANT 52
FT /note="L -> Q (in dbSNP:rs1051207)"
FT /evidence="ECO:0000269|PubMed:8206918"
FT /id="VAR_046442"
FT VARIANT 122
FT /note="L -> F (in dbSNP:rs1051314)"
FT /id="VAR_046443"
FT VARIANT 136
FT /note="L -> F (in dbSNP:rs1131564)"
FT /evidence="ECO:0000269|PubMed:8206918"
FT /id="VAR_046444"
FT VARIANT 421
FT /note="L -> P (in dbSNP:rs1982528)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:8206918, ECO:0000269|Ref.3"
FT /id="VAR_021789"
FT VARIANT 512
FT /note="G -> S (in dbSNP:rs34541796)"
FT /id="VAR_057248"
FT VARIANT 538
FT /note="E -> G (in dbSNP:rs34744641)"
FT /id="VAR_057249"
FT VARIANT 887
FT /note="A -> E (in dbSNP:rs34729193)"
FT /id="VAR_057250"
FT CONFLICT 236
FT /note="R -> P (in Ref. 1; AAA19604)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="H -> Y (in Ref. 1; AAA19604)"
FT /evidence="ECO:0000305"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:2E60"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:2E60"
FT HELIX 206..221
FT /evidence="ECO:0007829|PDB:2E60"
FT HELIX 224..233
FT /evidence="ECO:0007829|PDB:2E60"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:2E60"
FT HELIX 249..262
FT /evidence="ECO:0007829|PDB:2E60"
FT TURN 454..456
FT /evidence="ECO:0007829|PDB:2E5Z"
FT HELIX 457..469
FT /evidence="ECO:0007829|PDB:2E5Z"
FT HELIX 472..481
FT /evidence="ECO:0007829|PDB:2E5Z"
FT HELIX 484..486
FT /evidence="ECO:0007829|PDB:2E5Z"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:2E5Z"
FT HELIX 496..509
FT /evidence="ECO:0007829|PDB:2E5Z"
SQ SEQUENCE 951 AA; 104822 MW; A942D589F4B6BF47 CRC64;
MYGASGGRAK PERKSGAKEE AGPGGAGGGG SRVELLVFGY ACKLFRDDER ALAQEQGQHL
IPWMGDHKIL IDRYDGRGHL HDLSEYDAEY STWNRDYQLS EEEARIEALC DEERYLALHT
DLLEEEARQE EEYKRLSEAL AEDGSYNAVG FTYGSDYYDP SEPTEEEEPS KQREKNEAEN
LEENEEPFVA PLGLSVPSDV ELPPTAKMHA IIERTASFVC RQGAQFEIML KAKQARNSQF
DFLRFDHYLN PYYKFIQKAM KEGRYTVLAE NKSDEKKKSG VSSDNEDDDD EEDGNYLHPS
LFASKKCNRL EELMKPLKVV DPDHPLAALV RKAQADSSTP TPHNADGAPV QPSQVEYTAD
STVAAMYYSY YMLPDGTYCL APPPPGIDVT TYYSTLPAGV TVSNSPGVTT TAPPPPGTTP
LPPPTTAETS SGATSTTTTT SALAPVAAII PPPPDVQPVI DKLAEYVARN GLKFETSVRA
KNDQRFEFLQ PWHQYNAYYE FKKQFFLQKE GGDSMQAVSA PEEAPTDSAP EKPSDAGEDG
APEDAAEVGA RAGSGGKKEA SSSKTVPDGK LVKASFAPIS FAIKAKENDL LPLEKNRVKL
DDDSDDDEES KEGQESSSSA ANTNPAVAPP CVVVEEKKPQ LTQEELEAKQ AKQKLEDRLA
AAAREKLAQA SKESKEKQLQ AERKRKAALF LQTLKNPLPE AEAGKIEESP FSVEESSTTP
CPLLTGGRPL PTLEVKPPDR PSSKSKDPPR EEEKEKKKKK HKKRSRTRSR SPKYHSSSKS
RSRSHSKAKH SLPSAYRTVR RSRSRSRSPR RRAHSPERRR EERSVPTAYR VSRSPGASRK
RTRSRSPHEK KKKRRSRSRT KSKARSQSVS PSKQAAPRPA APAAHSAHSA SVSPVESRGS
SQERSRGVSQ EKEAQISSAI VSSVQSKITQ DLMAKVRAML AASKNLQTSA S
