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