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SEM6D_HUMAN
ID   SEM6D_HUMAN             Reviewed;        1073 AA.
AC   Q8NFY4; A6NF10; A6NM95; A6NNK1; A7E2A0; Q8NFY3; Q8NFY5; Q8NFY6; Q8NFY7;
AC   Q9P249;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 157.
DE   RecName: Full=Semaphorin-6D;
DE   Flags: Precursor;
GN   Name=SEMA6D; Synonyms=KIAA1479;
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] (ISOFORMS 1; 2; 3; 4 AND 7), SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=12110693; DOI=10.1074/jbc.m206451200;
RA   Qu X., Wei H., Zhai Y., Que H., Chen Q., Tang F., Wu Y., Xing G., Zhu Y.,
RA   Liu S., Fan M., He F.;
RT   "Identification, characterization, and functional study of the two novel
RT   human members of the semaphorin gene family.";
RL   J. Biol. Chem. 277:35574-35585(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA   Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XVII. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 7:143-150(2000).
RN   [3]
RP   SEQUENCE REVISION.
RX   PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA   Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT   "Construction of expression-ready cDNA clones for KIAA genes: manual
RT   curation of 330 KIAA cDNA clones.";
RL   DNA Res. 9:99-106(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16572171; DOI=10.1038/nature04601;
RA   Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA   Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA   FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA   Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA   Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA   DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA   Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA   Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA   Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA   O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA   Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA   Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT   "Analysis of the DNA sequence and duplication history of human chromosome
RT   15.";
RL   Nature 440:671-675(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-723; SER-744; THR-773;
RP   SER-931; SER-957 AND SER-983, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
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).
CC   -!- FUNCTION: Shows growth cone collapsing activity on dorsal root ganglion
CC       (DRG) neurons in vitro. May be a stop signal for the DRG neurons in
CC       their target areas, and possibly also for other neurons. May also be
CC       involved in the maintenance and remodeling of neuronal connections.
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I
CC       membrane protein.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane; Single-pass type I
CC       membrane protein.
CC   -!- SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane; Single-pass type I
CC       membrane protein.
CC   -!- SUBCELLULAR LOCATION: [Isoform 4]: Cell membrane; Single-pass type I
CC       membrane protein.
CC   -!- SUBCELLULAR LOCATION: [Isoform 5]: Cell membrane; Single-pass type I
CC       membrane protein.
CC   -!- SUBCELLULAR LOCATION: [Isoform 7]: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=8;
CC       Name=4; Synonyms=SEMA6D.4;
CC         IsoId=Q8NFY4-1; Sequence=Displayed;
CC       Name=1; Synonyms=SEMA6D.1;
CC         IsoId=Q8NFY4-2; Sequence=VSP_016565, VSP_016566;
CC       Name=2; Synonyms=SEMA6D.2;
CC         IsoId=Q8NFY4-3; Sequence=VSP_016566;
CC       Name=3; Synonyms=SEMA6D.3;
CC         IsoId=Q8NFY4-4; Sequence=VSP_016567;
CC       Name=5;
CC         IsoId=Q8NFY4-5; Sequence=VSP_016565, VSP_016567;
CC       Name=6;
CC         IsoId=Q8NFY4-6; Sequence=VSP_016572;
CC       Name=7; Synonyms=SEMA6Ds, Short;
CC         IsoId=Q8NFY4-7; Sequence=VSP_016564;
CC       Name=8;
CC         IsoId=Q8NFY4-8; Sequence=VSP_016572, VSP_054084;
CC   -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA96003.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF389426; AAM69449.1; -; mRNA.
DR   EMBL; AF389427; AAM69450.1; -; mRNA.
DR   EMBL; AF389428; AAM69451.1; -; mRNA.
DR   EMBL; AF389429; AAM69452.1; -; mRNA.
DR   EMBL; AF389430; AAM69453.1; -; mRNA.
DR   EMBL; AB040912; BAA96003.2; ALT_INIT; mRNA.
DR   EMBL; AC018900; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC044787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC009558; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC012050; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC023905; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC066615; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC084882; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC150253; AAI50254.1; -; mRNA.
DR   CCDS; CCDS32224.1; -. [Q8NFY4-2]
DR   CCDS; CCDS32225.1; -. [Q8NFY4-1]
DR   CCDS; CCDS32226.1; -. [Q8NFY4-4]
DR   CCDS; CCDS32227.1; -. [Q8NFY4-3]
DR   CCDS; CCDS32228.1; -. [Q8NFY4-8]
DR   CCDS; CCDS32229.1; -. [Q8NFY4-7]
DR   RefSeq; NP_001185928.1; NM_001198999.1. [Q8NFY4-2]
DR   RefSeq; NP_065909.1; NM_020858.1. [Q8NFY4-2]
DR   RefSeq; NP_079242.2; NM_024966.2. [Q8NFY4-7]
DR   RefSeq; NP_705869.1; NM_153616.1. [Q8NFY4-3]
DR   RefSeq; NP_705870.1; NM_153617.1. [Q8NFY4-4]
DR   RefSeq; NP_705871.1; NM_153618.1. [Q8NFY4-1]
DR   RefSeq; NP_705872.1; NM_153619.1. [Q8NFY4-8]
DR   RefSeq; XP_005254744.1; XM_005254687.2.
DR   RefSeq; XP_005254746.1; XM_005254689.3. [Q8NFY4-6]
DR   RefSeq; XP_011520379.1; XM_011522077.2. [Q8NFY4-6]
DR   RefSeq; XP_011520380.1; XM_011522078.2. [Q8NFY4-5]
DR   RefSeq; XP_011520381.1; XM_011522079.2. [Q8NFY4-4]
DR   RefSeq; XP_011520382.1; XM_011522080.2. [Q8NFY4-2]
DR   RefSeq; XP_011520383.1; XM_011522081.2. [Q8NFY4-3]
DR   RefSeq; XP_016878108.1; XM_017022619.1. [Q8NFY4-5]
DR   RefSeq; XP_016878109.1; XM_017022620.1. [Q8NFY4-4]
DR   RefSeq; XP_016878110.1; XM_017022621.1. [Q8NFY4-3]
DR   AlphaFoldDB; Q8NFY4; -.
DR   SMR; Q8NFY4; -.
DR   BioGRID; 123081; 11.
DR   CORUM; Q8NFY4; -.
DR   IntAct; Q8NFY4; 1.
DR   STRING; 9606.ENSP00000324857; -.
DR   CarbonylDB; Q8NFY4; -.
DR   GlyGen; Q8NFY4; 5 sites.
DR   iPTMnet; Q8NFY4; -.
DR   PhosphoSitePlus; Q8NFY4; -.
DR   BioMuta; SEMA6D; -.
DR   DMDM; 74715611; -.
DR   jPOST; Q8NFY4; -.
DR   MassIVE; Q8NFY4; -.
DR   MaxQB; Q8NFY4; -.
DR   PaxDb; Q8NFY4; -.
DR   PeptideAtlas; Q8NFY4; -.
DR   PRIDE; Q8NFY4; -.
DR   ProteomicsDB; 1522; -.
DR   ProteomicsDB; 73385; -. [Q8NFY4-1]
DR   ProteomicsDB; 73386; -. [Q8NFY4-2]
DR   ProteomicsDB; 73387; -. [Q8NFY4-3]
DR   ProteomicsDB; 73388; -. [Q8NFY4-4]
DR   ProteomicsDB; 73389; -. [Q8NFY4-5]
DR   ProteomicsDB; 73390; -. [Q8NFY4-6]
DR   ProteomicsDB; 73391; -. [Q8NFY4-7]
DR   Antibodypedia; 24461; 186 antibodies from 27 providers.
DR   DNASU; 80031; -.
DR   Ensembl; ENST00000316364.9; ENSP00000324857.5; ENSG00000137872.17. [Q8NFY4-1]
DR   Ensembl; ENST00000354744.8; ENSP00000346786.4; ENSG00000137872.17. [Q8NFY4-4]
DR   Ensembl; ENST00000355997.7; ENSP00000348276.3; ENSG00000137872.17. [Q8NFY4-8]
DR   Ensembl; ENST00000358066.8; ENSP00000350770.4; ENSG00000137872.17. [Q8NFY4-2]
DR   Ensembl; ENST00000389425.7; ENSP00000374076.3; ENSG00000137872.17. [Q8NFY4-7]
DR   Ensembl; ENST00000389428.7; ENSP00000374079.3; ENSG00000137872.17. [Q8NFY4-3]
DR   Ensembl; ENST00000536845.7; ENSP00000446152.3; ENSG00000137872.17. [Q8NFY4-1]
DR   Ensembl; ENST00000558014.5; ENSP00000452815.1; ENSG00000137872.17. [Q8NFY4-2]
DR   Ensembl; ENST00000558816.5; ENSP00000453661.1; ENSG00000137872.17. [Q8NFY4-8]
DR   GeneID; 80031; -.
DR   KEGG; hsa:80031; -.
DR   MANE-Select; ENST00000536845.7; ENSP00000446152.3; NM_001358351.3; NP_001345280.1.
DR   UCSC; uc001zvw.4; human. [Q8NFY4-1]
DR   CTD; 80031; -.
DR   DisGeNET; 80031; -.
DR   GeneCards; SEMA6D; -.
DR   HGNC; HGNC:16770; SEMA6D.
DR   HPA; ENSG00000137872; Tissue enhanced (intestine, placenta).
DR   MIM; 609295; gene.
DR   neXtProt; NX_Q8NFY4; -.
DR   OpenTargets; ENSG00000137872; -.
DR   PharmGKB; PA134951035; -.
DR   VEuPathDB; HostDB:ENSG00000137872; -.
DR   eggNOG; KOG3611; Eukaryota.
DR   GeneTree; ENSGT00940000159303; -.
DR   HOGENOM; CLU_009051_2_1_1; -.
DR   InParanoid; Q8NFY4; -.
DR   OMA; IAEEPWF; -.
DR   PhylomeDB; Q8NFY4; -.
DR   TreeFam; TF316102; -.
DR   PathwayCommons; Q8NFY4; -.
DR   Reactome; R-HSA-416700; Other semaphorin interactions.
DR   SignaLink; Q8NFY4; -.
DR   BioGRID-ORCS; 80031; 12 hits in 1062 CRISPR screens.
DR   ChiTaRS; SEMA6D; human.
DR   GenomeRNAi; 80031; -.
DR   Pharos; Q8NFY4; Tbio.
DR   PRO; PR:Q8NFY4; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; Q8NFY4; protein.
DR   Bgee; ENSG00000137872; Expressed in jejunal mucosa and 179 other tissues.
DR   ExpressionAtlas; Q8NFY4; baseline and differential.
DR   Genevisible; Q8NFY4; HS.
DR   GO; GO:0009986; C:cell surface; IMP:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IMP:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0045499; F:chemorepellent activity; IBA:GO_Central.
DR   GO; GO:0030215; F:semaphorin receptor binding; IBA:GO_Central.
DR   GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR   GO; GO:0050919; P:negative chemotaxis; IBA:GO_Central.
DR   GO; GO:0030517; P:negative regulation of axon extension; IDA:UniProtKB.
DR   GO; GO:0048843; P:negative regulation of axon extension involved in axon guidance; IBA:GO_Central.
DR   GO; GO:0014912; P:negative regulation of smooth muscle cell migration; IEA:Ensembl.
DR   GO; GO:0001755; P:neural crest cell migration; IBA:GO_Central.
DR   GO; GO:0030335; P:positive regulation of cell migration; IBA:GO_Central.
DR   GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IEA:Ensembl.
DR   GO; GO:0071526; P:semaphorin-plexin signaling pathway; IBA:GO_Central.
DR   GO; GO:0014909; P:smooth muscle cell migration; IEA:Ensembl.
DR   GO; GO:0021591; P:ventricular system development; IEA:Ensembl.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR002165; Plexin_repeat.
DR   InterPro; IPR016201; PSI.
DR   InterPro; IPR001627; Semap_dom.
DR   InterPro; IPR036352; Semap_dom_sf.
DR   InterPro; IPR027231; Semaphorin.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PANTHER; PTHR11036; PTHR11036; 1.
DR   Pfam; PF01437; PSI; 1.
DR   Pfam; PF01403; Sema; 1.
DR   SMART; SM00423; PSI; 1.
DR   SMART; SM00630; Sema; 1.
DR   SUPFAM; SSF101912; SSF101912; 1.
DR   PROSITE; PS51004; SEMA; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Cytoplasm; Developmental protein;
KW   Differentiation; Disulfide bond; Glycoprotein; Membrane; Neurogenesis;
KW   Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..1073
FT                   /note="Semaphorin-6D"
FT                   /id="PRO_0000044615"
FT   TOPO_DOM        21..662
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        663..683
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        684..1073
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          27..512
FT                   /note="Sema"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DOMAIN          514..569
FT                   /note="PSI"
FT   REGION          744..775
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          787..825
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          839..874
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          914..1005
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1021..1073
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        787..801
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        850..874
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        928..946
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        968..999
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1021..1041
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         723
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         734
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q76KF0"
FT   MOD_RES         744
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         773
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         931
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         957
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         983
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   CARBOHYD        51
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        283
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        435
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        461
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        631
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        108..118
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DISULFID        136..145
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DISULFID        259..370
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DISULFID        284..329
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DISULFID        477..506
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DISULFID        515..533
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DISULFID        521..568
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DISULFID        525..541
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   VAR_SEQ         477..1073
FT                   /note="Missing (in isoform 7)"
FT                   /evidence="ECO:0000303|PubMed:12110693"
FT                   /id="VSP_016564"
FT   VAR_SEQ         549
FT                   /note="L -> LLLTEDFFAFHNHS (in isoform 1 and isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:10819331,
FT                   ECO:0000303|PubMed:12110693, ECO:0000303|PubMed:15489334"
FT                   /id="VSP_016565"
FT   VAR_SEQ         570..644
FT                   /note="Missing (in isoform 1 and isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10819331,
FT                   ECO:0000303|PubMed:12110693, ECO:0000303|PubMed:15489334"
FT                   /id="VSP_016566"
FT   VAR_SEQ         570..588
FT                   /note="Missing (in isoform 6 and isoform 8)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_016572"
FT   VAR_SEQ         589..644
FT                   /note="Missing (in isoform 3 and isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:12110693"
FT                   /id="VSP_016567"
FT   VAR_SEQ         601..1073
FT                   /note="ASIPEITPKVIDTWRPKLTSSRKFVVQDDPNTSDFTDPLSGIPKGVRWEVQS
FT                   GESNQMVHMNVLITCVFAAFVLGAFIAGVAVYCYRDMFVRKNRKIHKDAESAQSCTDSS
FT                   GSFAKLNGLFDSPVKEYQQNIDSPKLYSNLLTSRKELPPNGDTKSMVMDHRGQPPELAA
FT                   LPTPESTPVLHQKTLQAMKSHSEKAHGHGASRKETPQFFPSSPPPHSPLSHGHIPSAIV
FT                   LPNATHDYNTSFSNSNAHKAEKKLQNIDHPLTKSSSKRDHRRSVDSRNTLNDLLKHLND
FT                   PNSNPKAIMGDIQMAHQNLMLDPMGSMSEVPPKVPNREASLYSPPSTLPRNSPTKRVDV
FT                   PTTPGVPMTSLERQRGYHKNSSQRHSISAMPKNLNSPNGVLLSRQPSMNRGGYMPTPTG
FT                   AKVDYIQGTPVSVHLQPSLSRQSSYTSNGTLPRTGLKRTPSLKPDVPPKPSFVPQTPSV
FT                   RPLNKYTY -> VYDGKSSLESPTRWST (in isoform 8)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_054084"
FT   VARIANT         307
FT                   /note="N -> S (in dbSNP:rs3743279)"
FT                   /id="VAR_051931"
FT   VARIANT         478
FT                   /note="S -> N (in dbSNP:rs532598)"
FT                   /id="VAR_051932"
FT   VARIANT         969
FT                   /note="S -> T (in dbSNP:rs16960074)"
FT                   /id="VAR_051933"
SQ   SEQUENCE   1073 AA;  119872 MW;  7DCE4DFC5BF70F9E CRC64;
     MRVFLLCAYI LLLMVSQLRA VSFPEDDEPL NTVDYHYSRQ YPVFRGRPSG NESQHRLDFQ
     LMLKIRDTLY IAGRDQVYTV NLNEMPKTEV IPNKKLTWRS RQQDRENCAM KGKHKDECHN
     FIKVFVPRND EMVFVCGTNA FNPMCRYYRL STLEYDGEEI SGLARCPFDA RQTNVALFAD
     GKLYSATVAD FLASDAVIYR SMGDGSALRT IKYDSKWIKE PHFLHAIEYG NYVYFFFREI
     AVEHNNLGKA VYSRVARICK NDMGGSQRVL EKHWTSFLKA RLNCSVPGDS FFYFDVLQSI
     TDIIQINGIP TVVGVFTTQL NSIPGSAVCA FSMDDIEKVF KGRFKEQKTP DSVWTAVPED
     KVPKPRPGCC AKHGLAEAYK TSIDFPDETL SFIKSHPLMD SAVPPIADEP WFTKTRVRYR
     LTAISVDHSA GPYQNYTVIF VGSEAGMVLK VLAKTSPFSL NDSVLLEEIE AYNHAKCSAE
     NEEDKKVISL QLDKDHHALY VAFSSCIIRI PLSRCERYGS CKKSCIASRD PYCGWLSQGS
     CGRVTPGMLA EGYEQDTEFG NTAHLGDCHE ILPTSTTPDY KIFGGPTSDM EVSSSSVTTM
     ASIPEITPKV IDTWRPKLTS SRKFVVQDDP NTSDFTDPLS GIPKGVRWEV QSGESNQMVH
     MNVLITCVFA AFVLGAFIAG VAVYCYRDMF VRKNRKIHKD AESAQSCTDS SGSFAKLNGL
     FDSPVKEYQQ NIDSPKLYSN LLTSRKELPP NGDTKSMVMD HRGQPPELAA LPTPESTPVL
     HQKTLQAMKS HSEKAHGHGA SRKETPQFFP SSPPPHSPLS HGHIPSAIVL PNATHDYNTS
     FSNSNAHKAE KKLQNIDHPL TKSSSKRDHR RSVDSRNTLN DLLKHLNDPN SNPKAIMGDI
     QMAHQNLMLD PMGSMSEVPP KVPNREASLY SPPSTLPRNS PTKRVDVPTT PGVPMTSLER
     QRGYHKNSSQ RHSISAMPKN LNSPNGVLLS RQPSMNRGGY MPTPTGAKVD YIQGTPVSVH
     LQPSLSRQSS YTSNGTLPRT GLKRTPSLKP DVPPKPSFVP QTPSVRPLNK YTY
 
 
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