SLIT3_HUMAN
ID SLIT3_HUMAN Reviewed; 1523 AA.
AC O75094; A6H8U9; J3KNP3; O95804; Q9UFH5;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Slit homolog 3 protein;
DE Short=Slit-3;
DE AltName: Full=Multiple epidermal growth factor-like domains protein 5;
DE Short=Multiple EGF-like domains protein 5;
DE Flags: Precursor;
GN Name=SLIT3; Synonyms=KIAA0814, MEGF5, SLIL2; ORFNames=UNQ691/PRO1336;
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 AND 3), TISSUE SPECIFICITY, AND
RP VARIANT ALA-371.
RX PubMed=9813312; DOI=10.1016/s0169-328x(98)00224-1;
RA Itoh A., Miyabayashi T., Ohno M., Sakano S.;
RT "Cloning and expressions of three mammalian homologues of Drosophila slit
RT suggest possible roles for Slit in the formation and maintenance of the
RT nervous system.";
RL Brain Res. Mol. Brain Res. 62:175-186(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-371.
RC TISSUE=Brain;
RX PubMed=9693030; DOI=10.1006/geno.1998.5341;
RA Nakayama M., Nakajima D., Nagase T., Nomura N., Seki N., Ohara O.;
RT "Identification of high-molecular-weight proteins with multiple EGF-like
RT motifs by motif-trap screening.";
RL Genomics 51:27-34(1998).
RN [3]
RP SEQUENCE REVISION.
RA Nakayama M., Nakajima D., Nagase T., Nomura N., Seki N., Ohara O.;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ALA-371
RP AND SER-618.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-371.
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 337-657, AND VARIANT ALA-371.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 574-1523 (ISOFORM 2).
RX PubMed=10349621; DOI=10.1016/s0925-4773(98)00174-9;
RA Holmes G.P., Negus K., Burridge L., Raman S., Algar E., Yamada T.,
RA Little M.H.;
RT "Distinct but overlapping expression patterns of two vertebrate slit
RT homologs implies functional roles in CNS development and organogenesis.";
RL Mech. Dev. 79:57-72(1998).
CC -!- FUNCTION: May act as molecular guidance cue in cellular migration, and
CC function may be mediated by interaction with roundabout homolog
CC receptors.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O75094-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75094-2; Sequence=VSP_009714;
CC Name=3;
CC IsoId=O75094-3; Sequence=VSP_009715;
CC Name=4;
CC IsoId=O75094-4; Sequence=VSP_054798;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in thyroid.
CC {ECO:0000269|PubMed:9813312}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA32466.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB59249.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/SLIT3ID50515ch5q34.html";
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DR EMBL; AB017169; BAA35186.1; -; mRNA.
DR EMBL; AB011538; BAA32466.2; ALT_INIT; mRNA.
DR EMBL; AY358884; AAQ89243.1; -; mRNA.
DR EMBL; AC008409; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC008479; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011365; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011389; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC027311; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC094081; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC112165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC146759; AAI46760.1; -; mRNA.
DR EMBL; AL122074; CAB59249.1; ALT_SEQ; mRNA.
DR EMBL; AF075240; AAD19336.1; -; mRNA.
DR CCDS; CCDS4369.1; -. [O75094-1]
DR CCDS; CCDS64311.1; -. [O75094-4]
DR PIR; T34555; T34555.
DR RefSeq; NP_001258875.1; NM_001271946.1. [O75094-4]
DR RefSeq; NP_003053.1; NM_003062.3. [O75094-1]
DR AlphaFoldDB; O75094; -.
DR SMR; O75094; -.
DR BioGRID; 112473; 4.
DR IntAct; O75094; 7.
DR MINT; O75094; -.
DR STRING; 9606.ENSP00000332164; -.
DR GlyConnect; 1750; 1 N-Linked glycan (1 site).
DR GlyGen; O75094; 14 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; O75094; -.
DR PhosphoSitePlus; O75094; -.
DR BioMuta; SLIT3; -.
DR jPOST; O75094; -.
DR MassIVE; O75094; -.
DR MaxQB; O75094; -.
DR PaxDb; O75094; -.
DR PeptideAtlas; O75094; -.
DR PRIDE; O75094; -.
DR ProteomicsDB; 49755; -. [O75094-1]
DR ProteomicsDB; 49756; -. [O75094-2]
DR ProteomicsDB; 49757; -. [O75094-3]
DR Antibodypedia; 16807; 245 antibodies from 31 providers.
DR DNASU; 6586; -.
DR Ensembl; ENST00000332966.8; ENSP00000332164.8; ENSG00000184347.15. [O75094-4]
DR Ensembl; ENST00000519560.6; ENSP00000430333.2; ENSG00000184347.15. [O75094-1]
DR GeneID; 6586; -.
DR KEGG; hsa:6586; -.
DR MANE-Select; ENST00000519560.6; ENSP00000430333.2; NM_003062.4; NP_003053.2.
DR UCSC; uc003mab.5; human. [O75094-1]
DR CTD; 6586; -.
DR DisGeNET; 6586; -.
DR GeneCards; SLIT3; -.
DR HGNC; HGNC:11087; SLIT3.
DR HPA; ENSG00000184347; Low tissue specificity.
DR MIM; 603745; gene.
DR neXtProt; NX_O75094; -.
DR OpenTargets; ENSG00000184347; -.
DR PharmGKB; PA35940; -.
DR VEuPathDB; HostDB:ENSG00000184347; -.
DR eggNOG; KOG4237; Eukaryota.
DR GeneTree; ENSGT00940000159322; -.
DR InParanoid; O75094; -.
DR OMA; PACNANS; -.
DR OrthoDB; 28488at2759; -.
DR PhylomeDB; O75094; -.
DR TreeFam; TF332887; -.
DR PathwayCommons; O75094; -.
DR Reactome; R-HSA-373752; Netrin-1 signaling.
DR Reactome; R-HSA-376176; Signaling by ROBO receptors.
DR Reactome; R-HSA-428542; Regulation of commissural axon pathfinding by SLIT and ROBO.
DR SignaLink; O75094; -.
DR BioGRID-ORCS; 6586; 4 hits in 1065 CRISPR screens.
DR ChiTaRS; SLIT3; human.
DR GeneWiki; SLIT3; -.
DR GenomeRNAi; 6586; -.
DR Pharos; O75094; Tbio.
DR PRO; PR:O75094; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; O75094; protein.
DR Bgee; ENSG00000184347; Expressed in right coronary artery and 187 other tissues.
DR ExpressionAtlas; O75094; baseline and differential.
DR Genevisible; O75094; HS.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; NAS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB.
DR GO; GO:0008201; F:heparin binding; IBA:GO_Central.
DR GO; GO:0048495; F:Roundabout binding; IPI:UniProtKB.
DR GO; GO:0003180; P:aortic valve morphogenesis; ISS:BHF-UCL.
DR GO; GO:0061364; P:apoptotic process involved in luteolysis; IEP:UniProtKB.
DR GO; GO:0003181; P:atrioventricular valve morphogenesis; ISS:BHF-UCL.
DR GO; GO:0048846; P:axon extension involved in axon guidance; IDA:UniProtKB.
DR GO; GO:0007411; P:axon guidance; IDA:UniProtKB.
DR GO; GO:0032870; P:cellular response to hormone stimulus; IEP:UniProtKB.
DR GO; GO:0050919; P:negative chemotaxis; IDA:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; IMP:BHF-UCL.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0070100; P:negative regulation of chemokine-mediated signaling pathway; IMP:BHF-UCL.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0051414; P:response to cortisol; IEP:UniProtKB.
DR GO; GO:0035385; P:Roundabout signaling pathway; IMP:BHF-UCL.
DR GO; GO:0060412; P:ventricular septum morphogenesis; ISS:BHF-UCL.
DR CDD; cd00110; LamG; 1.
DR Gene3D; 3.80.10.10; -; 5.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR006207; Cys_knot_C.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR Pfam; PF00008; EGF; 6.
DR Pfam; PF12661; hEGF; 1.
DR Pfam; PF02210; Laminin_G_2; 1.
DR Pfam; PF13855; LRR_8; 5.
DR Pfam; PF01463; LRRCT; 4.
DR Pfam; PF01462; LRRNT; 3.
DR SMART; SM00041; CT; 1.
DR SMART; SM00181; EGF; 9.
DR SMART; SM00179; EGF_CA; 9.
DR SMART; SM00282; LamG; 1.
DR SMART; SM00369; LRR_TYP; 18.
DR SMART; SM00082; LRRCT; 4.
DR SMART; SM00013; LRRNT; 4.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS01185; CTCK_1; 1.
DR PROSITE; PS01225; CTCK_2; 1.
DR PROSITE; PS00022; EGF_1; 9.
DR PROSITE; PS01186; EGF_2; 7.
DR PROSITE; PS50026; EGF_3; 9.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
DR PROSITE; PS51450; LRR; 20.
PE 2: Evidence at transcript level;
KW Alternative splicing; Developmental protein; Differentiation;
KW Disulfide bond; EGF-like domain; Glycoprotein; Leucine-rich repeat;
KW Neurogenesis; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..1523
FT /note="Slit homolog 3 protein"
FT /id="PRO_0000007732"
FT DOMAIN 34..61
FT /note="LRRNT"
FT REPEAT 62..83
FT /note="LRR 1"
FT REPEAT 86..107
FT /note="LRR 2"
FT REPEAT 110..131
FT /note="LRR 3"
FT REPEAT 134..155
FT /note="LRR 4"
FT REPEAT 158..179
FT /note="LRR 5"
FT REPEAT 182..203
FT /note="LRR 6"
FT DOMAIN 215..265
FT /note="LRRCT 1"
FT DOMAIN 271..307
FT /note="LRRNT 2"
FT REPEAT 308..329
FT /note="LRR 7"
FT REPEAT 332..353
FT /note="LRR 8"
FT REPEAT 356..377
FT /note="LRR 9"
FT REPEAT 380..401
FT /note="LRR 10"
FT REPEAT 404..425
FT /note="LRR 11"
FT DOMAIN 437..487
FT /note="LRRCT 2"
FT DOMAIN 496..532
FT /note="LRRNT 3"
FT REPEAT 533..554
FT /note="LRR 12"
FT REPEAT 558..579
FT /note="LRR 13"
FT REPEAT 582..603
FT /note="LRR 14"
FT REPEAT 606..627
FT /note="LRR 15"
FT REPEAT 630..651
FT /note="LRR 16"
FT DOMAIN 663..713
FT /note="LRRCT 3"
FT DOMAIN 716..752
FT /note="LRRNT 4"
FT REPEAT 753..775
FT /note="LRR 17"
FT REPEAT 776..797
FT /note="LRR 18"
FT REPEAT 800..821
FT /note="LRR 19"
FT REPEAT 824..845
FT /note="LRR 20"
FT DOMAIN 857..907
FT /note="LRRCT 4"
FT DOMAIN 918..953
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 955..994
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 996..1032
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1034..1072
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1074..1110
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1119..1155
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1158..1332
FT /note="Laminin G-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1340..1365
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1368..1403
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1408..1444
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1449..1523
FT /note="CTCK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 563
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 622
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 784
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 792
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 797
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 928
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1008
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1025
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 284..293
FT /evidence="ECO:0000250"
FT DISULFID 441..464
FT /evidence="ECO:0000250"
FT DISULFID 443..485
FT /evidence="ECO:0000250"
FT DISULFID 505..511
FT /evidence="ECO:0000250"
FT DISULFID 509..518
FT /evidence="ECO:0000250"
FT DISULFID 667..690
FT /evidence="ECO:0000250"
FT DISULFID 669..711
FT /evidence="ECO:0000250"
FT DISULFID 920..931
FT /evidence="ECO:0000250"
FT DISULFID 925..941
FT /evidence="ECO:0000250"
FT DISULFID 943..952
FT /evidence="ECO:0000250"
FT DISULFID 959..970
FT /evidence="ECO:0000250"
FT DISULFID 964..982
FT /evidence="ECO:0000250"
FT DISULFID 984..993
FT /evidence="ECO:0000250"
FT DISULFID 1000..1011
FT /evidence="ECO:0000250"
FT DISULFID 1005..1020
FT /evidence="ECO:0000250"
FT DISULFID 1022..1031
FT /evidence="ECO:0000250"
FT DISULFID 1038..1051
FT /evidence="ECO:0000250"
FT DISULFID 1045..1060
FT /evidence="ECO:0000250"
FT DISULFID 1062..1071
FT /evidence="ECO:0000250"
FT DISULFID 1078..1089
FT /evidence="ECO:0000250"
FT DISULFID 1083..1098
FT /evidence="ECO:0000250"
FT DISULFID 1100..1109
FT /evidence="ECO:0000250"
FT DISULFID 1123..1134
FT /evidence="ECO:0000250"
FT DISULFID 1128..1143
FT /evidence="ECO:0000250"
FT DISULFID 1145..1154
FT /evidence="ECO:0000250"
FT DISULFID 1305..1332
FT /evidence="ECO:0000250"
FT DISULFID 1355..1364
FT /evidence="ECO:0000250"
FT DISULFID 1372..1382
FT /evidence="ECO:0000250"
FT DISULFID 1377..1391
FT /evidence="ECO:0000250"
FT DISULFID 1393..1402
FT /evidence="ECO:0000250"
FT DISULFID 1412..1422
FT /evidence="ECO:0000250"
FT DISULFID 1417..1432
FT /evidence="ECO:0000250"
FT DISULFID 1434..1443
FT /evidence="ECO:0000250"
FT DISULFID 1449..1487
FT /evidence="ECO:0000250"
FT DISULFID 1467..1501
FT /evidence="ECO:0000250"
FT DISULFID 1478..1517
FT /evidence="ECO:0000250"
FT DISULFID 1482..1519
FT /evidence="ECO:0000250"
FT VAR_SEQ 906
FT /note="K -> KVLWFCCP (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_054798"
FT VAR_SEQ 1117..1216
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10349621,
FT ECO:0000303|PubMed:9813312"
FT /id="VSP_009714"
FT VAR_SEQ 1446..1523
FT /note="ENPCLGQVVREVIRRQKGYASCATASKVPIMECRGGCGPQCCQPTRSKRRKY
FT VFQCTDGSSFVEEVERHLECGCLACS -> VFRAQVFQSSLPGNCSWSCWPPRPPMP
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9813312"
FT /id="VSP_009715"
FT VARIANT 371
FT /note="V -> A (in dbSNP:rs891921)"
FT /evidence="ECO:0000269|PubMed:12975309,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005,
FT ECO:0000269|PubMed:9693030, ECO:0000269|PubMed:9813312"
FT /id="VAR_049004"
FT VARIANT 395
FT /note="R -> Q (in dbSNP:rs2288792)"
FT /id="VAR_021905"
FT VARIANT 618
FT /note="G -> S (in dbSNP:rs10036727)"
FT /evidence="ECO:0000269|PubMed:12975309"
FT /id="VAR_024265"
FT VARIANT 810
FT /note="R -> Q (in dbSNP:rs36052924)"
FT /id="VAR_049005"
FT VARIANT 994
FT /note="E -> G (in dbSNP:rs2305993)"
FT /id="VAR_020168"
FT VARIANT 1064
FT /note="P -> A (in dbSNP:rs10072243)"
FT /id="VAR_049006"
SQ SEQUENCE 1523 AA; 167713 MW; CEB00887F6908554 CRC64;
MAPGWAGVGA AVRARLALAL ALASVLSGPP AVACPTKCTC SAASVDCHGL GLRAVPRGIP
RNAERLDLDR NNITRITKMD FAGLKNLRVL HLEDNQVSVI ERGAFQDLKQ LERLRLNKNK
LQVLPELLFQ STPKLTRLDL SENQIQGIPR KAFRGITDVK NLQLDNNHIS CIEDGAFRAL
RDLEILTLNN NNISRILVTS FNHMPKIRTL RLHSNHLYCD CHLAWLSDWL RQRRTVGQFT
LCMAPVHLRG FNVADVQKKE YVCPAPHSEP PSCNANSISC PSPCTCSNNI VDCRGKGLME
IPANLPEGIV EIRLEQNSIK AIPAGAFTQY KKLKRIDISK NQISDIAPDA FQGLKSLTSL
VLYGNKITEI VKGLFDGLVS LQLLLLNANK INCLRVNTFQ DLQNLNLLSL YDNKLQTISK
GLFAPLQSIQ TLHLAQNPFV CDCHLKWLAD YLQDNPIETS GARCSSPRRL ANKRISQIKS
KKFRCSGSED YRSRFSSECF MDLVCPEKCR CEGTIVDCSN QKLVRIPSHL PEYVTDLRLN
DNEVSVLEAT GIFKKLPNLR KINLSNNKIK EVREGAFDGA ASVQELMLTG NQLETVHGRV
FRGLSGLKTL MLRSNLIGCV SNDTFAGLSS VRLLSLYDNR ITTITPGAFT TLVSLSTINL
LSNPFNCNCH LAWLGKWLRK RRIVSGNPRC QKPFFLKEIP IQDVAIQDFT CDGNEESSCQ
LSPRCPEQCT CMETVVRCSN KGLRALPRGM PKDVTELYLE GNHLTAVPRE LSALRHLTLI
DLSNNSISML TNYTFSNMSH LSTLILSYNR LRCIPVHAFN GLRSLRVLTL HGNDISSVPE
GSFNDLTSLS HLALGTNPLH CDCSLRWLSE WVKAGYKEPG IARCSSPEPM ADRLLLTTPT
HRFQCKGPVD INIVAKCNAC LSSPCKNNGT CTQDPVELYR CACPYSYKGK DCTVPINTCI
QNPCQHGGTC HLSDSHKDGF SCSCPLGFEG QRCEINPDDC EDNDCENNAT CVDGINNYVC
ICPPNYTGEL CDEVIDHCVP ELNLCQHEAK CIPLDKGFSC ECVPGYSGKL CETDNDDCVA
HKCRHGAQCV DTINGYTCTC PQGFSGPFCE HPPPMVLLQT SPCDQYECQN GAQCIVVQQE
PTCRCPPGFA GPRCEKLITV NFVGKDSYVE LASAKVRPQA NISLQVATDK DNGILLYKGD
NDPLALELYQ GHVRLVYDSL SSPPTTVYSV ETVNDGQFHS VELVTLNQTL NLVVDKGTPK
SLGKLQKQPA VGINSPLYLG GIPTSTGLSA LRQGTDRPLG GFHGCIHEVR INNELQDFKA
LPPQSLGVSP GCKSCTVCKH GLCRSVEKDS VVCECRPGWT GPLCDQEARD PCLGHRCHHG
KCVATGTSYM CKCAEGYGGD LCDNKNDSAN ACSAFKCHHG QCHISDQGEP YCLCQPGFSG
EHCQQENPCL GQVVREVIRR QKGYASCATA SKVPIMECRG GCGPQCCQPT RSKRRKYVFQ
CTDGSSFVEE VERHLECGCL ACS
