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   27-MAR-2024, entry version 207.
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; 19.
DR   IntAct; O75093; 18.
DR   MINT; O75093; -.
DR   STRING; 9606.ENSP00000266058; -.
DR   TCDB; 9.B.87.1.40; the selenoprotein p receptor (selp-receptor) family.
DR   CarbonylDB; O75093; -.
DR   GlyCosmos; O75093; 13 sites, No reported glycans.
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; 9606-ENSP00000266058; -.
DR   PeptideAtlas; O75093; -.
DR   ProteomicsDB; 49753; -. [O75093-1]
DR   ProteomicsDB; 49754; -. [O75093-2]
DR   Pumba; O75093; -.
DR   Antibodypedia; 1515; 221 antibodies from 27 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   AGR; HGNC:11085; -.
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   OrthoDB; 5475408at2759; -.
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 1146 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 142 other cell types or tissues.
DR   ExpressionAtlas; O75093; baseline and differential.
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; cd00054; EGF_CA; 6.
DR   CDD; cd00110; LamG; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 2.10.25.10; Laminin; 8.
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; 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   PANTHER; PTHR45836:SF4; PROTEIN SLIT; 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; 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; SM00365; LRR_SD22; 8.
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; 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.
DR   Genevisible; O75093; HS.
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
//