SLIT1_HUMAN
ID SLIT1_HUMAN Reviewed; 1534 AA.
AC O75093; Q5T0V1; Q8WWZ2; Q9UIL7;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 4.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Slit homolog 1 protein;
DE Short=Slit-1;
DE AltName: Full=Multiple epidermal growth factor-like domains protein 4;
DE Short=Multiple EGF-like domains protein 4;
DE Flags: Precursor;
GN Name=SLIT1; Synonyms=KIAA0813, MEGF4, SLIL1;
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 1), AND TISSUE SPECIFICITY.
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).
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.
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 SEQUENCE REVISION.
RA Nakayama M., Nakajima D., Ohara O.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [6]
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 [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 18-1534 (ISOFORM 2).
RX PubMed=12141424;
RA Little M., Rumballe B., Georgas K., Yamada T., Teasdale R.D.;
RT "Conserved modularity and potential for alternate splicing in mouse and
RT human Slit genes.";
RL Int. J. Dev. Biol. 46:385-391(2002).
RN [9]
RP REVIEW.
RX PubMed=12200164; DOI=10.1016/s0959-437x(02)00343-x;
RA Wong K., Park H.T., Wu J.Y., Rao Y.;
RT "Slit proteins: molecular guidance cues for cells ranging from neurons to
RT leukocytes.";
RL Curr. Opin. Genet. Dev. 12:583-591(2002).
CC -!- FUNCTION: Thought to act as molecular guidance cue in cellular
CC migration, and function appears to be mediated by interaction with
CC roundabout homolog receptors. During neural development involved in
CC axonal navigation at the ventral midline of the neural tube and
CC projection of axons to different regions (By similarity). SLIT1 and
CC SLIT2 together seem to be essential for midline guidance in the
CC forebrain by acting as repulsive signal preventing inappropriate
CC midline crossing by axons projecting from the olfactory bulb.
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ROBO1 and GREM1. {ECO:0000250}.
CC -!- INTERACTION:
CC O75093; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-947791, EBI-10173507;
CC O75093; Q6WN34-2: CHRDL2; NbExp=3; IntAct=EBI-947791, EBI-12593838;
CC O75093; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-947791, EBI-3867333;
CC O75093; Q5TD97: FHL5; NbExp=3; IntAct=EBI-947791, EBI-750641;
CC O75093; P49639: HOXA1; NbExp=4; IntAct=EBI-947791, EBI-740785;
CC O75093; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-947791, EBI-11959885;
CC O75093; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-947791, EBI-10171774;
CC O75093; Q52LG2: KRTAP13-2; NbExp=3; IntAct=EBI-947791, EBI-11953846;
CC O75093; Q3SY46: KRTAP13-3; NbExp=3; IntAct=EBI-947791, EBI-10241252;
CC O75093; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-947791, EBI-16439278;
CC O75093; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-947791, EBI-5235829;
CC O75093; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-947791, EBI-4395669;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O75093-1; Sequence=Displayed;
CC Name=2; Synonyms=B;
CC IsoId=O75093-2; Sequence=VSP_009706, VSP_009707, VSP_009708;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in adult forebrain.
CC Expressed in fetal brain, lung and kidney.
CC {ECO:0000269|PubMed:9813312}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA32465.3; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB017167; BAA35184.1; -; mRNA.
DR EMBL; AB011537; BAA32465.3; ALT_INIT; mRNA.
DR EMBL; AL442123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL512424; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49958.1; -; Genomic_DNA.
DR EMBL; BC146851; AAI46852.1; -; mRNA.
DR EMBL; AY029183; AAK31796.1; -; mRNA.
DR CCDS; CCDS7453.1; -. [O75093-1]
DR RefSeq; NP_003052.2; NM_003061.2. [O75093-1]
DR AlphaFoldDB; O75093; -.
DR BioGRID; 112472; 17.
DR IntAct; O75093; 18.
DR MINT; O75093; -.
DR STRING; 9606.ENSP00000266058; -.
DR CarbonylDB; O75093; -.
DR GlyGen; O75093; 18 sites.
DR iPTMnet; O75093; -.
DR PhosphoSitePlus; O75093; -.
DR BioMuta; SLIT1; -.
DR EPD; O75093; -.
DR jPOST; O75093; -.
DR MassIVE; O75093; -.
DR MaxQB; O75093; -.
DR PaxDb; O75093; -.
DR PeptideAtlas; O75093; -.
DR PRIDE; O75093; -.
DR ProteomicsDB; 49753; -. [O75093-1]
DR ProteomicsDB; 49754; -. [O75093-2]
DR Antibodypedia; 1515; 194 antibodies from 26 providers.
DR DNASU; 6585; -.
DR Ensembl; ENST00000266058.9; ENSP00000266058.4; ENSG00000187122.17. [O75093-1]
DR GeneID; 6585; -.
DR KEGG; hsa:6585; -.
DR MANE-Select; ENST00000266058.9; ENSP00000266058.4; NM_003061.3; NP_003052.2.
DR UCSC; uc001kmw.3; human. [O75093-1]
DR CTD; 6585; -.
DR DisGeNET; 6585; -.
DR GeneCards; SLIT1; -.
DR HGNC; HGNC:11085; SLIT1.
DR HPA; ENSG00000187122; Group enriched (brain, pituitary gland).
DR MIM; 603742; gene.
DR neXtProt; NX_O75093; -.
DR OpenTargets; ENSG00000187122; -.
DR PharmGKB; PA35938; -.
DR VEuPathDB; HostDB:ENSG00000187122; -.
DR eggNOG; KOG4237; Eukaryota.
DR GeneTree; ENSGT00940000157322; -.
DR HOGENOM; CLU_001431_2_0_1; -.
DR InParanoid; O75093; -.
DR OMA; ETKCQNN; -.
DR PhylomeDB; O75093; -.
DR TreeFam; TF332887; -.
DR PathwayCommons; O75093; -.
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 Reactome; R-HSA-8985801; Regulation of cortical dendrite branching.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR SignaLink; O75093; -.
DR SIGNOR; O75093; -.
DR BioGRID-ORCS; 6585; 14 hits in 1070 CRISPR screens.
DR ChiTaRS; SLIT1; human.
DR GeneWiki; SLIT1; -.
DR GenomeRNAi; 6585; -.
DR Pharos; O75093; Tbio.
DR PRO; PR:O75093; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; O75093; protein.
DR Bgee; ENSG00000187122; Expressed in cortical plate and 140 other tissues.
DR ExpressionAtlas; O75093; baseline and differential.
DR Genevisible; O75093; HS.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB.
DR GO; GO:0043395; F:heparan sulfate proteoglycan binding; IEA:Ensembl.
DR GO; GO:0008201; F:heparin binding; IBA:GO_Central.
DR GO; GO:0048495; F:Roundabout binding; IPI:UniProtKB.
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:0033563; P:dorsal/ventral axon guidance; IEA:Ensembl.
DR GO; GO:0048853; P:forebrain morphogenesis; NAS:UniProtKB.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:UniProtKB.
DR GO; GO:0050919; P:negative chemotaxis; IDA:UniProtKB.
DR GO; GO:0048843; P:negative regulation of axon extension involved in axon guidance; IEA:Ensembl.
DR GO; GO:0051964; P:negative regulation of synapse assembly; ISS:UniProtKB.
DR GO; GO:0007097; P:nuclear migration; IEA:Ensembl.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; IEA:Ensembl.
DR GO; GO:0021510; P:spinal cord development; IEA:Ensembl.
DR GO; GO:0022028; P:tangential migration from the subventricular zone to the olfactory bulb; IEA:Ensembl.
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; IPR003645; Fol_N.
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; 5.
DR Pfam; PF12661; hEGF; 2.
DR Pfam; PF02210; Laminin_G_2; 1.
DR Pfam; PF13855; LRR_8; 6.
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; 7.
DR SMART; SM00274; FOLN; 4.
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; 8.
DR PROSITE; PS50026; EGF_3; 9.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
DR PROSITE; PS51450; LRR; 21.
PE 1: Evidence at protein 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..1534
FT /note="Slit homolog 1 protein"
FT /id="PRO_0000007722"
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 273..309
FT /note="LRRNT 2"
FT REPEAT 310..331
FT /note="LRR 7"
FT REPEAT 334..355
FT /note="LRR 8"
FT REPEAT 358..379
FT /note="LRR 9"
FT REPEAT 382..403
FT /note="LRR 10"
FT REPEAT 406..427
FT /note="LRR 11"
FT DOMAIN 439..489
FT /note="LRRCT 2"
FT DOMAIN 504..540
FT /note="LRRNT 3"
FT REPEAT 541..562
FT /note="LRR 12"
FT REPEAT 566..587
FT /note="LRR 13"
FT REPEAT 590..611
FT /note="LRR 14"
FT REPEAT 614..635
FT /note="LRR 15"
FT REPEAT 638..659
FT /note="LRR 16"
FT DOMAIN 671..721
FT /note="LRRCT 3"
FT DOMAIN 725..761
FT /note="LRRNT 4"
FT REPEAT 762..783
FT /note="LRR 17"
FT REPEAT 785..806
FT /note="LRR 18"
FT REPEAT 809..830
FT /note="LRR 19"
FT REPEAT 833..854
FT /note="LRR 20"
FT DOMAIN 866..916
FT /note="LRRCT 4"
FT DOMAIN 927..962
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 964..1003
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1005..1041
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1043..1081
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1083..1119
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1127..1163
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1166..1339
FT /note="Laminin G-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1340..1374
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1377..1413
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1418..1454
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1459..1534
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 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 571
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 630
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 762
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 801
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 806
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1026
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1079
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 286..295
FT /evidence="ECO:0000250"
FT DISULFID 443..466
FT /evidence="ECO:0000250"
FT DISULFID 445..487
FT /evidence="ECO:0000250"
FT DISULFID 513..519
FT /evidence="ECO:0000250"
FT DISULFID 517..526
FT /evidence="ECO:0000250"
FT DISULFID 675..698
FT /evidence="ECO:0000250"
FT DISULFID 677..719
FT /evidence="ECO:0000250"
FT DISULFID 929..940
FT /evidence="ECO:0000250"
FT DISULFID 934..950
FT /evidence="ECO:0000250"
FT DISULFID 952..961
FT /evidence="ECO:0000250"
FT DISULFID 968..979
FT /evidence="ECO:0000250"
FT DISULFID 973..991
FT /evidence="ECO:0000250"
FT DISULFID 993..1002
FT /evidence="ECO:0000250"
FT DISULFID 1009..1020
FT /evidence="ECO:0000250"
FT DISULFID 1014..1029
FT /evidence="ECO:0000250"
FT DISULFID 1031..1040
FT /evidence="ECO:0000250"
FT DISULFID 1047..1060
FT /evidence="ECO:0000250"
FT DISULFID 1054..1069
FT /evidence="ECO:0000250"
FT DISULFID 1071..1080
FT /evidence="ECO:0000250"
FT DISULFID 1087..1098
FT /evidence="ECO:0000250"
FT DISULFID 1092..1107
FT /evidence="ECO:0000250"
FT DISULFID 1109..1118
FT /evidence="ECO:0000250"
FT DISULFID 1131..1142
FT /evidence="ECO:0000250"
FT DISULFID 1136..1151
FT /evidence="ECO:0000250"
FT DISULFID 1153..1162
FT /evidence="ECO:0000250"
FT DISULFID 1313..1339
FT /evidence="ECO:0000250"
FT DISULFID 1342..1352
FT /evidence="ECO:0000250"
FT DISULFID 1347..1362
FT /evidence="ECO:0000250"
FT DISULFID 1364..1373
FT /evidence="ECO:0000250"
FT DISULFID 1381..1391
FT /evidence="ECO:0000250"
FT DISULFID 1386..1401
FT /evidence="ECO:0000250"
FT DISULFID 1403..1412
FT /evidence="ECO:0000250"
FT DISULFID 1422..1432
FT /evidence="ECO:0000250"
FT DISULFID 1427..1442
FT /evidence="ECO:0000250"
FT DISULFID 1444..1453
FT /evidence="ECO:0000250"
FT DISULFID 1459..1498
FT /evidence="ECO:0000250"
FT DISULFID 1477..1512
FT /evidence="ECO:0000250"
FT DISULFID 1488..1528
FT /evidence="ECO:0000250"
FT DISULFID 1492..1530
FT /evidence="ECO:0000250"
FT VAR_SEQ 338
FT /note="I -> IRPLSFCSPCR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12141424"
FT /id="VSP_009706"
FT VAR_SEQ 790..813
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12141424"
FT /id="VSP_009707"
FT VAR_SEQ 830..1534
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12141424"
FT /id="VSP_009708"
FT VARIANT 824
FT /note="P -> L (in dbSNP:rs2817673)"
FT /id="VAR_049003"
FT CONFLICT 99
FT /note="A -> V (in Ref. 2; BAA32465)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="Q -> R (in Ref. 1; BAA35184)"
FT /evidence="ECO:0000305"
FT CONFLICT 829
FT /note="Q -> P (in Ref. 8; AAK31796)"
FT /evidence="ECO:0000305"
FT CONFLICT 966
FT /note="D -> N (in Ref. 1; BAA35184)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1534 AA; 167926 MW; 47B11CE6704A3E1D CRC64;
MALTPGWGSS AGPVRPELWL LLWAAAWRLG ASACPALCTC TGTTVDCHGT GLQAIPKNIP
RNTERLELNG NNITRIHKND FAGLKQLRVL QLMENQIGAV ERGAFDDMKE LERLRLNRNQ
LHMLPELLFQ NNQALSRLDL SENAIQAIPR KAFRGATDLK NLQLDKNQIS CIEEGAFRAL
RGLEVLTLNN NNITTIPVSS FNHMPKLRTF RLHSNHLFCD CHLAWLSQWL RQRPTIGLFT
QCSGPASLRG LNVAEVQKSE FSCSGQGEAG RVPTCTLSSG SCPAMCTCSN GIVDCRGKGL
TAIPANLPET MTEIRLELNG IKSIPPGAFS PYRKLRRIDL SNNQIAEIAP DAFQGLRSLN
SLVLYGNKIT DLPRGVFGGL YTLQLLLLNA NKINCIRPDA FQDLQNLSLL SLYDNKIQSL
AKGTFTSLRA IQTLHLAQNP FICDCNLKWL ADFLRTNPIE TSGARCASPR RLANKRIGQI
KSKKFRCSAK EQYFIPGTED YQLNSECNSD VVCPHKCRCE ANVVECSSLK LTKIPERIPQ
STAELRLNNN EISILEATGM FKKLTHLKKI NLSNNKVSEI EDGAFEGAAS VSELHLTANQ
LESIRSGMFR GLDGLRTLML RNNRISCIHN DSFTGLRNVR LLSLYDNQIT TVSPGAFDTL
QSLSTLNLLA NPFNCNCQLA WLGGWLRKRK IVTGNPRCQN PDFLRQIPLQ DVAFPDFRCE
EGQEEGGCLP RPQCPQECAC LDTVVRCSNK HLRALPKGIP KNVTELYLDG NQFTLVPGQL
STFKYLQLVD LSNNKISSLS NSSFTNMSQL TTLILSYNAL QCIPPLAFQG LRSLRLLSLH
GNDISTLQEG IFADVTSLSH LAIGANPLYC DCHLRWLSSW VKTGYKEPGI ARCAGPQDME
GKLLLTTPAK KFECQGPPTL AVQAKCDLCL SSPCQNQGTC HNDPLEVYRC ACPSGYKGRD
CEVSLDSCSS GPCENGGTCH AQEGEDAPFT CSCPTGFEGP TCGVNTDDCV DHACANGGVC
VDGVGNYTCQ CPLQYEGKAC EQLVDLCSPD LNPCQHEAQC VGTPDGPRCE CMPGYAGDNC
SENQDDCRDH RCQNGAQCMD EVNSYSCLCA EGYSGQLCEI PPHLPAPKSP CEGTECQNGA
NCVDQGNRPV CQCLPGFGGP ECEKLLSVNF VDRDTYLQFT DLQNWPRANI TLQVSTAEDN
GILLYNGDND HIAVELYQGH VRVSYDPGSY PSSAIYSAET INDGQFHTVE LVAFDQMVNL
SIDGGSPMTM DNFGKHYTLN SEAPLYVGGM PVDVNSAAFR LWQILNGTGF HGCIRNLYIN
NELQDFTKTQ MKPGVVPGCE PCRKLYCLHG ICQPNATPGP MCHCEAGWVG LHCDQPADGP
CHGHKCVHGQ CVPLDALSYS CQCQDGYSGA LCNQAGALAE PCRGLQCLHG HCQASGTKGA
HCVCDPGFSG ELCEQESECR GDPVRDFHQV QRGYAICQTT RPLSWVECRG SCPGQGCCQG
LRLKRRKFTF ECSDGTSFAE EVEKPTKCGC ALCA
