GCFC2_HUMAN
ID GCFC2_HUMAN Reviewed; 781 AA.
AC P16383; A4UHQ8; A4UHQ9; O95032; Q53TY0; Q6P2F2;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Intron Large complex component GCFC2 {ECO:0000305};
DE AltName: Full=GC-rich sequence DNA-binding factor;
DE AltName: Full=GC-rich sequence DNA-binding factor 2;
DE AltName: Full=Transcription factor 9;
DE Short=TCF-9;
GN Name=GCFC2; Synonyms=C2orf3, GCF, TCF9;
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 2).
RX PubMed=2556218; DOI=10.1016/0092-8674(89)90605-3;
RA Kageyama R., Pastan I.;
RT "Molecular cloning and characterization of a human DNA binding factor that
RT represses transcription.";
RL Cell 59:815-825(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-249.
RX PubMed=10500253; DOI=10.1016/s0167-4781(99)00127-x;
RA Takimoto M., Mao P., Wei G., Yamazaki H., Miura T., Johnson A.C.,
RA Kuzumaki N.;
RT "Molecular analysis of the GCF gene identifies revisions to the cDNA and
RT amino acid sequences.";
RL Biochim. Biophys. Acta 1447:125-131(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
RX PubMed=17309879; DOI=10.1093/hmg/ddm009;
RA Anthoni H., Zucchelli M., Matsson H., Muller-Myhsok B., Fransson I.,
RA Schumacher J., Massinen S., Onkamo P., Warnke A., Griesemann H.,
RA Hoffmann P., Nopola-Hemmi J., Lyytinen H., Schulte-Korne G., Kere J.,
RA Nothen M.M., Peyrard-Janvid M.;
RT "A locus on 2p12 containing the co-regulated MRPL19 and C2ORF3 genes is
RT associated to dyslexia.";
RL Hum. Mol. Genet. 16:667-677(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-32.
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-17; SER-19; THR-213;
RP SER-214 AND SER-217, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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-16; SER-17; SER-19; THR-213;
RP SER-214 AND SER-217, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 AND THR-97, AND
RP IDENTIFICATION BY 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 [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-17; SER-19; SER-96
RP AND THR-97, AND IDENTIFICATION BY 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-19; SER-40; SER-96; THR-97;
RP SER-174 AND SER-180, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 FUNCTION, IDENTIFICATION IN THE INTRON LARGE COMPLEX, SUBCELLULAR LOCATION,
RP INTERACTION WITH TFIP11 AND DHX15, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=24304693; DOI=10.1111/gtc.12114;
RA Yoshimoto R., Okawa K., Yoshida M., Ohno M., Kataoka N.;
RT "Identification of a novel component C2ORF3 in the lariat-intron complex:
RT lack of C2ORF3 interferes with pre-mRNA splicing via intron turnover
RT pathway.";
RL Genes Cells 19:78-87(2014).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-17 AND SER-19, AND
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).
CC -!- FUNCTION: Involved in pre-mRNA splicing through regulating spliceosome
CC C complex formation (PubMed:24304693). May play a role during late-
CC stage splicing events and turnover of excised introns
CC (PubMed:24304693). {ECO:0000269|PubMed:24304693}.
CC -!- SUBUNIT: Found in the Intron Large (IL) complex, a post-mRNA release
CC spliceosomal complex containing the excised intron, U2, U5 and U6
CC snRNPs, and splicing factors (PubMed:24304693). Interacts with TFIP11
CC and DHX15 (PubMed:24304693). {ECO:0000269|PubMed:24304693}.
CC -!- INTERACTION:
CC P16383; Q9UBB9: TFIP11; NbExp=5; IntAct=EBI-954074, EBI-1105213;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:24304693}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:24304693}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P16383-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P16383-2; Sequence=VSP_021798;
CC Name=3;
CC IsoId=P16383-3; Sequence=VSP_054362, VSP_054363;
CC Name=4;
CC IsoId=P16383-4; Sequence=VSP_057398, VSP_057399;
CC -!- TISSUE SPECIFICITY: Widely expressed in tissues and cell lines.
CC -!- SIMILARITY: Belongs to the GCF family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a DNA-binding transcriptional
CC repressor. However, later work showed that the original sequence was a
CC chimera and that the DNA-binding activity was derived from the
CC incorrect N-terminal sequence. {ECO:0000305|PubMed:10500253,
CC ECO:0000305|PubMed:2556218}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA35598.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA35598.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. The N-terminus matches the 2q37.3 region.; Evidence={ECO:0000305};
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DR EMBL; M29204; AAA35598.1; ALT_SEQ; mRNA.
DR EMBL; AB026911; BAA85386.1; -; mRNA.
DR EMBL; EF158467; ABO84856.1; -; mRNA.
DR EMBL; EF158468; ABO84857.1; -; mRNA.
DR EMBL; AC005034; AAY14973.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99586.1; -; Genomic_DNA.
DR EMBL; BC064559; AAH64559.1; -; mRNA.
DR CCDS; CCDS1961.1; -. [P16383-1]
DR CCDS; CCDS62943.1; -. [P16383-3]
DR PIR; A33633; A33633.
DR RefSeq; NP_001188263.1; NM_001201334.1.
DR RefSeq; NP_001188264.1; NM_001201335.1. [P16383-3]
DR RefSeq; NP_003194.3; NM_003203.4. [P16383-1]
DR AlphaFoldDB; P16383; -.
DR SMR; P16383; -.
DR BioGRID; 112797; 53.
DR CORUM; P16383; -.
DR IntAct; P16383; 27.
DR MINT; P16383; -.
DR STRING; 9606.ENSP00000318690; -.
DR GlyGen; P16383; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P16383; -.
DR PhosphoSitePlus; P16383; -.
DR BioMuta; GCFC2; -.
DR DMDM; 118572650; -.
DR EPD; P16383; -.
DR jPOST; P16383; -.
DR MassIVE; P16383; -.
DR MaxQB; P16383; -.
DR PaxDb; P16383; -.
DR PeptideAtlas; P16383; -.
DR PRIDE; P16383; -.
DR ProteomicsDB; 53347; -. [P16383-1]
DR ProteomicsDB; 53348; -. [P16383-2]
DR ProteomicsDB; 704; -.
DR Antibodypedia; 31654; 175 antibodies from 27 providers.
DR DNASU; 6936; -.
DR Ensembl; ENST00000321027.8; ENSP00000318690.3; ENSG00000005436.14. [P16383-1]
DR Ensembl; ENST00000409857.7; ENSP00000386552.3; ENSG00000005436.14. [P16383-2]
DR Ensembl; ENST00000470503.1; ENSP00000474481.1; ENSG00000005436.14. [P16383-3]
DR Ensembl; ENST00000541687.5; ENSP00000437767.1; ENSG00000005436.14. [P16383-4]
DR GeneID; 6936; -.
DR KEGG; hsa:6936; -.
DR MANE-Select; ENST00000321027.8; ENSP00000318690.3; NM_003203.5; NP_003194.3.
DR UCSC; uc002sno.4; human. [P16383-1]
DR UCSC; uc061lbc.1; human.
DR CTD; 6936; -.
DR DisGeNET; 6936; -.
DR GeneCards; GCFC2; -.
DR HGNC; HGNC:1317; GCFC2.
DR HPA; ENSG00000005436; Low tissue specificity.
DR MIM; 189901; gene.
DR neXtProt; NX_P16383; -.
DR OpenTargets; ENSG00000005436; -.
DR PharmGKB; PA25892; -.
DR VEuPathDB; HostDB:ENSG00000005436; -.
DR eggNOG; KOG2136; Eukaryota.
DR GeneTree; ENSGT00390000000455; -.
DR HOGENOM; CLU_1144868_0_0_1; -.
DR InParanoid; P16383; -.
DR OMA; MKMYVEN; -.
DR OrthoDB; 1217358at2759; -.
DR PhylomeDB; P16383; -.
DR TreeFam; TF315109; -.
DR PathwayCommons; P16383; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; P16383; -.
DR BioGRID-ORCS; 6936; 14 hits in 1085 CRISPR screens.
DR ChiTaRS; GCFC2; human.
DR GeneWiki; C2orf3; -.
DR GenomeRNAi; 6936; -.
DR Pharos; P16383; Tbio.
DR PRO; PR:P16383; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P16383; protein.
DR Bgee; ENSG00000005436; Expressed in ventricular zone and 182 other tissues.
DR ExpressionAtlas; P16383; baseline and differential.
DR Genevisible; P16383; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0071008; C:U2-type post-mRNA release spliceosomal complex; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0000245; P:spliceosomal complex assembly; IMP:UniProtKB.
DR InterPro; IPR012890; GCFC2-like.
DR InterPro; IPR022783; GCFC_dom.
DR PANTHER; PTHR12214; PTHR12214; 1.
DR Pfam; PF07842; GCFC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..781
FT /note="Intron Large complex component GCFC2"
FT /id="PRO_0000087441"
FT REGION 1..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 267..312
FT /evidence="ECO:0000255"
FT COMPBIAS 79..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 97
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BKT3"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 213
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT VAR_SEQ 169..207
FT /note="GMKRESEDDPESEPDDHEKRIPFTLRPQTLRQRMAEESI -> V (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:2556218"
FT /id="VSP_021798"
FT VAR_SEQ 207..213
FT /note="ISRNEET -> SMDLPIY (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17309879"
FT /id="VSP_054362"
FT VAR_SEQ 214..779
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17309879"
FT /id="VSP_054363"
FT VAR_SEQ 240..254
FT /note="ERDIDLSCGNGSSKV -> INITTGNSPLTPEGV (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17309879"
FT /id="VSP_057398"
FT VAR_SEQ 255..781
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17309879"
FT /id="VSP_057399"
FT VARIANT 32
FT /note="P -> A (in dbSNP:rs7559767)"
FT /evidence="ECO:0000269|PubMed:15815621"
FT /id="VAR_051005"
FT VARIANT 249
FT /note="N -> S (in dbSNP:rs7560262)"
FT /id="VAR_051006"
FT VARIANT 316
FT /note="Q -> E (in dbSNP:rs6742946)"
FT /id="VAR_051007"
FT VARIANT 594
FT /note="T -> A (in dbSNP:rs6722682)"
FT /id="VAR_051008"
FT VARIANT 724
FT /note="E -> D (in dbSNP:rs17690300)"
FT /id="VAR_051009"
SQ SEQUENCE 781 AA; 89385 MW; 38D34EE4442EB3DF CRC64;
MAHRPKRTFR QRAADSSDSD GAEESPAEPG APRELPVPGS AEEEPPSGGG RAQVAGLPHR
VRGPRGRGRV WASSRRATKA APRADEGSES RTLDVSTDEE DKIHHSSESK DDQGLSSDSS
SSLGEKELSS TVKIPDAAFI QAARRKRELA RAQDDYISLD VQHTSSISGM KRESEDDPES
EPDDHEKRIP FTLRPQTLRQ RMAEESISRN EETSEESQED EKQDTWEQQQ MRKAVKIIEE
RDIDLSCGNG SSKVKKFDTS ISFPPVNLEI IKKQLNTRLT LLQETHRSHL REYEKYVQDV
KSSKSTIQNL ESSSNQALNC KFYKSMKIYV ENLIDCLNEK IINIQEIESS MHALLLKQAM
TFMKRRQDEL KHESTYLQQL SRKDETSTSG NFSVDEKTQW ILEEIESRRT KRRQARVLSG
NCNHQEGTSS DDELPSAEMI DFQKSQGDIL QKQKKVFEEV QDDFCNIQNI LLKFQQWREK
FPDSYYEAFI SLCIPKLLNP LIRVQLIDWN PLKLESTGLK EMPWFKSVEE FMDSSVEDSK
KESSSDKKVL SAIINKTIIP RLTDFVEFLW DPLSTSQTTS LITHCRVILE EHSTCENEVS
KSRQDLLKSI VSRMKKAVED DVFIPLYPKS AVENKTSPHS KFQERQFWSG LKLFRNILLW
NGLLTDDTLQ ELGLGKLLNR YLIIALLNAT PGPDVVKKCN QVAACLPEKW FENSAMRTSI
PQLENFIQFL LQSAHKLSRS EFRDEVEEII LILVKIKALN QAESFIGEHH LDHLKSLIKE
D
