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 27-NOV-2024, entry version 206. 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="https://atlasgeneticsoncology.org/gene/50515/SLIT3"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 6. DR IntAct; O75094; 7. DR MINT; O75094; -. DR STRING; 9606.ENSP00000332164; -. DR TCDB; 9.B.87.1.41; the selenoprotein p receptor (selp-receptor) family. DR GlyConnect; 1750; 1 N-Linked glycan (1 site). DR GlyCosmos; O75094; 14 sites, 2 glycans. DR GlyGen; O75094; 16 sites, 11 N-linked glycans (4 sites), 2 O-linked glycans (3 sites). DR iPTMnet; O75094; -. DR PhosphoSitePlus; O75094; -. DR BioMuta; SLIT3; -. DR jPOST; O75094; -. DR MassIVE; O75094; -. DR PaxDb; 9606-ENSP00000332164; -. DR PeptideAtlas; O75094; -. DR ProteomicsDB; 49755; -. [O75094-1] DR ProteomicsDB; 49756; -. [O75094-2] DR ProteomicsDB; 49757; -. [O75094-3] DR Antibodypedia; 16807; 236 antibodies from 30 providers. DR DNASU; 6586; -. DR Ensembl; ENST00000332966.8; ENSP00000332164.8; ENSG00000184347.16. [O75094-4] DR Ensembl; ENST00000519560.6; ENSP00000430333.2; ENSG00000184347.16. [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 AGR; HGNC:11087; -. 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; 5475408at2759; -. 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; 5 hits in 1144 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 189 other cell types or tissues. DR ExpressionAtlas; O75094; baseline and differential. 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; cd00054; EGF_CA; 5. DR CDD; cd00110; LamG; 1. DR FunFam; 2.10.25.10:FF:000045; Slit guidance ligand 2; 1. DR FunFam; 2.10.25.10:FF:000053; Slit guidance ligand 2; 1. DR FunFam; 2.10.25.10:FF:000054; Slit guidance ligand 2; 1. DR FunFam; 2.10.25.10:FF:000062; Slit guidance ligand 2; 1. DR FunFam; 2.10.25.10:FF:000063; Slit guidance ligand 2; 1. DR FunFam; 2.10.25.10:FF:000099; Slit guidance ligand 2; 1. DR FunFam; 3.80.10.10:FF:000002; Slit guidance ligand 2; 2. DR FunFam; 3.80.10.10:FF:000004; Slit guidance ligand 2; 1. DR FunFam; 3.80.10.10:FF:000376; Slit guidance ligand 2; 1. DR FunFam; 2.10.25.10:FF:000375; Slit guidance ligand 3; 1. DR FunFam; 2.60.120.200:FF:000047; Slit guidance ligand 3; 1. DR FunFam; 3.80.10.10:FF:000032; Slit homolog 2 (Drosophila); 1. DR Gene3D; 2.60.120.200; -; 1. DR Gene3D; 2.10.25.10; Laminin; 9. DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 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 InterPro; IPR051355; Notch/Slit_guidance. DR PANTHER; PTHR45836:SF23; LRRCT DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR45836; SLIT HOMOLOG; 1. DR Pfam; PF00008; EGF; 5. 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; SM00364; LRR_BAC; 5. DR SMART; SM00368; LRR_RI; 5. DR SMART; SM00365; LRR_SD22; 9. DR SMART; SM00369; LRR_TYP; 18. DR SMART; SM00082; LRRCT; 4. DR SMART; SM00013; LRRNT; 4. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1. DR SUPFAM; SSF57196; EGF/Laminin; 4. DR SUPFAM; SSF57184; Growth factor receptor domain; 1. DR SUPFAM; SSF52058; L domain-like; 2. 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 1: Evidence at protein level; KW Alternative splicing; Developmental protein; Differentiation; KW Disulfide bond; EGF-like domain; Glycoprotein; Leucine-rich repeat; KW Neurogenesis; Proteomics identification; Reference proteome; Repeat; KW 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 //