ID   SLIT_DROME              Reviewed;        1504 AA.
AC   P24014; A8DYF5; A8DYF6; Q24526; Q8MLB9; Q9V7F8; Q9V7F9; Q9XYV4;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   28-FEB-2003, sequence version 2.
DT   27-MAR-2024, entry version 230.
DE   RecName: Full=Protein slit;
DE            Short=dSlit;
DE   AltName: Full=Slit-FL {ECO:0000303|PubMed:32994163};
DE   Contains:
DE     RecName: Full=Protein slit N-product;
DE              Short=Slit-N {ECO:0000303|PubMed:32994163};
DE   Contains:
DE     RecName: Full=Protein slit C-product;
DE              Short=Slit-C {ECO:0000303|PubMed:32994163};
DE   Flags: Precursor;
GN   Name=sli; ORFNames=CG43758;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Embryo;
RX   PubMed=2176636; DOI=10.1101/gad.4.12a.2169;
RA   Rothberg J.M., Jacobs J.R., Goodman C.S., Artavanis-Tsakonas S.;
RT   "Slit: an extracellular protein necessary for development of midline glia
RT   and commissural axon pathways contains both EGF and LRR domains.";
RL   Genes Dev. 4:2169-2187(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Embryo;
RX   PubMed=10102267; DOI=10.1016/s0092-8674(00)80589-9;
RA   Kidd T., Bland K.S., Goodman C.S.;
RT   "Slit is the midline repellent for the robo receptor in Drosophila.";
RL   Cell 96:785-794(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [4]
RP   GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 898-1435, FUNCTION, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=Canton-S;
RX   PubMed=3144436; DOI=10.1016/0092-8674(88)90249-8;
RA   Rothberg J.M., Hartley D.A., Walther Z., Artavanis-Tsakonas S.;
RT   "slit: an EGF-homologous locus of D. melanogaster involved in the
RT   development of the embryonic central nervous system.";
RL   Cell 55:1047-1059(1988).
RN   [6]
RP   FUNCTION, INTERACTION WITH ROBO, AND CLEAVAGE.
RX   PubMed=10102268; DOI=10.1016/s0092-8674(00)80590-5;
RA   Brose K., Bland K.S., Wang K.H., Arnott D., Henzel W., Goodman C.S.,
RA   Tessier-Lavigne M., Kidd T.;
RT   "Slit proteins bind Robo receptors and have an evolutionarily conserved
RT   role in repulsive axon guidance.";
RL   Cell 96:795-806(1999).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=32994163; DOI=10.1242/dev.196055;
RA   Kellermeyer R., Heydman L.M., Gillis T., Mastick G.S., Song M., Kidd T.;
RT   "Proteolytic cleavage of Slit by the Tolkin protease converts an axon
RT   repulsion cue to an axon growth cue in vivo.";
RL   Development 147:0-0(2020).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 542-733, AND DISULFIDE BONDS IN
RP   THE LRR REGION.
RX   PubMed=15496984; DOI=10.1038/sj.emboj.7600446;
RA   Howitt J.A., Clout N.J., Hohenester E.;
RT   "Binding site for Robo receptors revealed by dissection of the leucine-rich
RT   repeat region of Slit.";
RL   EMBO J. 23:4406-4412(2004).
CC   -!- FUNCTION: A short-range repellent, controlling axon crossing of the
CC       midline and a long-range chemorepellent, controlling mesoderm migration
CC       and patterning away from the midline. May interact with extracellular
CC       matrix molecules. Repulsive ligand for the guidance receptor roundabout
CC       (robo) and prevents inappropriate midline crossing by Robo-expressing
CC       axons. {ECO:0000269|PubMed:10102267, ECO:0000269|PubMed:10102268,
CC       ECO:0000269|PubMed:2176636, ECO:0000269|PubMed:3144436}.
CC   -!- FUNCTION: [Protein slit]: Promotes midline repulsion of axons but not
CC       longitudinal axon guidance. {ECO:0000269|PubMed:32994163}.
CC   -!- FUNCTION: [Protein slit N-product]: Promotes longitudinal axon growth.
CC       {ECO:0000269|PubMed:32994163}.
CC   -!- SUBUNIT: Interacts with robo. {ECO:0000269|PubMed:10102268}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2176636,
CC       ECO:0000269|PubMed:3144436, ECO:0000269|PubMed:32994163}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=C; Synonyms=E;
CC         IsoId=P24014-1; Sequence=Displayed;
CC       Name=A; Synonyms=D;
CC         IsoId=P24014-2; Sequence=VSP_001408;
CC       Name=B;
CC         IsoId=P24014-3; Sequence=VSP_001408, VSP_001409;
CC   -!- TISSUE SPECIFICITY: In embryos, highest expression occurs around the
CC       midline glia and low expression is observed around CNS axons lateral to
CC       the midline. Expression can be seen on the commissural axons traversing
CC       the glial cells but it is absent from the cell bodies of these neurons.
CC       {ECO:0000269|PubMed:10102267, ECO:0000269|PubMed:2176636,
CC       ECO:0000269|PubMed:3144436, ECO:0000269|PubMed:32994163}.
CC   -!- TISSUE SPECIFICITY: [Protein slit N-product]: In abdominal muscles,
CC       strongly localizes to muscle attachment sites.
CC       {ECO:0000269|PubMed:32994163}.
CC   -!- DISRUPTION PHENOTYPE: Flies lacking sli exhibit disruption of the
CC       developing midline cells and the commissural axon pathways.
CC       {ECO:0000269|PubMed:3144436}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA72722.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; X53959; CAA37910.1; -; mRNA.
DR   EMBL; AF126540; AAD26567.1; -; mRNA.
DR   EMBL; AE013599; AAF58097.1; -; Genomic_DNA.
DR   EMBL; AE013599; AAF58098.1; -; Genomic_DNA.
DR   EMBL; AE013599; AAM70966.1; -; Genomic_DNA.
DR   EMBL; AE013599; ABV53816.1; -; Genomic_DNA.
DR   EMBL; AE013599; ABV53817.1; -; Genomic_DNA.
DR   EMBL; M23543; AAA72722.1; ALT_INIT; Genomic_DNA.
DR   PIR; A36665; A36665.
DR   PIR; B36665; B36665.
DR   RefSeq; NP_001097333.1; NM_001103863.3. [P24014-2]
DR   RefSeq; NP_001097334.1; NM_001103864.3. [P24014-1]
DR   RefSeq; NP_476727.1; NM_057379.4. [P24014-1]
DR   RefSeq; NP_476728.1; NM_057380.4. [P24014-2]
DR   RefSeq; NP_476729.1; NM_057381.4. [P24014-3]
DR   PDB; 1W8A; X-ray; 2.80 A; A=542-733.
DR   PDBsum; 1W8A; -.
DR   AlphaFoldDB; P24014; -.
DR   SMR; P24014; -.
DR   BioGRID; 62473; 41.
DR   IntAct; P24014; 7.
DR   STRING; 7227.FBpp0303578; -.
DR   GlyCosmos; P24014; 13 sites, No reported glycans.
DR   GlyGen; P24014; 13 sites.
DR   PaxDb; 7227-FBpp0303575; -.
DR   EnsemblMetazoa; FBtr0330729; FBpp0303573; FBgn0264089. [P24014-2]
DR   EnsemblMetazoa; FBtr0330730; FBpp0303574; FBgn0264089. [P24014-3]
DR   EnsemblMetazoa; FBtr0330731; FBpp0303575; FBgn0264089. [P24014-1]
DR   EnsemblMetazoa; FBtr0330732; FBpp0303576; FBgn0264089. [P24014-2]
DR   EnsemblMetazoa; FBtr0330733; FBpp0303577; FBgn0264089. [P24014-1]
DR   GeneID; 36746; -.
DR   KEGG; dme:Dmel_CG43758; -.
DR   UCSC; CG8355-RD; d. melanogaster.
DR   UCSC; CG8355-RE; d. melanogaster.
DR   AGR; FB:FBgn0264089; -.
DR   CTD; 36746; -.
DR   FlyBase; FBgn0264089; sli.
DR   VEuPathDB; VectorBase:FBgn0264089; -.
DR   eggNOG; KOG4237; Eukaryota.
DR   GeneTree; ENSGT00940000167217; -.
DR   InParanoid; P24014; -.
DR   OMA; ETKCQNN; -.
DR   PhylomeDB; P24014; -.
DR   Reactome; R-DME-376176; Signaling by ROBO receptors.
DR   Reactome; R-DME-428890; Role of ABL in ROBO-SLIT signaling.
DR   Reactome; R-DME-9010553; Regulation of expression of SLITs and ROBOs.
DR   SignaLink; P24014; -.
DR   BioGRID-ORCS; 36746; 0 hits in 3 CRISPR screens.
DR   EvolutionaryTrace; P24014; -.
DR   GenomeRNAi; 36746; -.
DR   PRO; PR:P24014; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0264089; Expressed in central nervous system and 16 other cell types or tissues.
DR   ExpressionAtlas; P24014; baseline and differential.
DR   GO; GO:0030424; C:axon; IDA:FlyBase.
DR   GO; GO:0009986; C:cell surface; IDA:FlyBase.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0071666; C:Slit-Robo signaling complex; IDA:FlyBase.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0008201; F:heparin binding; IDA:FlyBase.
DR   GO; GO:0048495; F:Roundabout binding; IPI:FlyBase.
DR   GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR   GO; GO:0016199; P:axon midline choice point recognition; IMP:FlyBase.
DR   GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR   GO; GO:0007502; P:digestive tract mesoderm development; IMP:FlyBase.
DR   GO; GO:0035050; P:embryonic heart tube development; IMP:FlyBase.
DR   GO; GO:0007427; P:epithelial cell migration, open tracheal system; IMP:FlyBase.
DR   GO; GO:0008347; P:glial cell migration; IMP:UniProtKB.
DR   GO; GO:0008406; P:gonad development; IMP:FlyBase.
DR   GO; GO:0050929; P:induction of negative chemotaxis; IMP:UniProtKB.
DR   GO; GO:0007509; P:mesoderm migration involved in gastrulation; IMP:UniProtKB.
DR   GO; GO:0008078; P:mesodermal cell migration; IMP:FlyBase.
DR   GO; GO:0030182; P:neuron differentiation; IMP:FlyBase.
DR   GO; GO:0001764; P:neuron migration; IMP:FlyBase.
DR   GO; GO:0003151; P:outflow tract morphogenesis; IMP:FlyBase.
DR   GO; GO:0030335; P:positive regulation of cell migration; IMP:FlyBase.
DR   GO; GO:0022409; P:positive regulation of cell-cell adhesion; IMP:FlyBase.
DR   GO; GO:0010632; P:regulation of epithelial cell migration; IMP:FlyBase.
DR   GO; GO:2000274; P:regulation of epithelial cell migration, open tracheal system; IMP:FlyBase.
DR   GO; GO:0035385; P:Roundabout signaling pathway; IGI:FlyBase.
DR   GO; GO:0007432; P:salivary gland boundary specification; IMP:FlyBase.
DR   GO; GO:0016201; P:synaptic target inhibition; IMP:FlyBase.
DR   CDD; cd00054; EGF_CA; 5.
DR   CDD; cd00110; LamG; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 2.10.25.10; Laminin; 7.
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   PANTHER; PTHR45836:SF23; LRRCT DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR45836; SLIT HOMOLOG; 1.
DR   Pfam; PF00008; EGF; 4.
DR   Pfam; PF12661; hEGF; 1.
DR   Pfam; PF00054; Laminin_G_1; 1.
DR   Pfam; PF00560; LRR_1; 1.
DR   Pfam; PF13855; LRR_8; 6.
DR   Pfam; PF01463; LRRCT; 4.
DR   Pfam; PF01462; LRRNT; 4.
DR   SMART; SM00041; CT; 1.
DR   SMART; SM00181; EGF; 7.
DR   SMART; SM00179; EGF_CA; 6.
DR   SMART; SM00282; LamG; 1.
DR   SMART; SM00364; LRR_BAC; 7.
DR   SMART; SM00368; LRR_RI; 7.
DR   SMART; SM00365; LRR_SD22; 10.
DR   SMART; SM00369; LRR_TYP; 16.
DR   SMART; SM00082; LRRCT; 4.
DR   SMART; SM00013; LRRNT; 4.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 3.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   SUPFAM; SSF52058; L domain-like; 2.
DR   PROSITE; PS00010; ASX_HYDROXYL; 3.
DR   PROSITE; PS01185; CTCK_1; 1.
DR   PROSITE; PS01225; CTCK_2; 1.
DR   PROSITE; PS00022; EGF_1; 7.
DR   PROSITE; PS01186; EGF_2; 5.
DR   PROSITE; PS50026; EGF_3; 7.
DR   PROSITE; PS01187; EGF_CA; 2.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 1.
DR   PROSITE; PS51450; LRR; 20.
DR   Genevisible; P24014; DM.
PE   1: Evidence at protein level;
KW   3D-structure; 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..36
FT   CHAIN           37..1504
FT                   /note="Protein slit"
FT                   /id="PRO_0000007719"
FT   CHAIN           37..1135
FT                   /note="Protein slit N-product"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000007720"
FT   CHAIN           1136..1504
FT                   /note="Protein slit C-product"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000007721"
FT   DOMAIN          64..100
FT                   /note="LRRNT 1"
FT   REPEAT          101..122
FT                   /note="LRR 1"
FT   REPEAT          125..146
FT                   /note="LRR 2"
FT   REPEAT          149..170
FT                   /note="LRR 3"
FT   REPEAT          173..194
FT                   /note="LRR 4"
FT   REPEAT          197..218
FT                   /note="LRR 5"
FT   REPEAT          221..242
FT                   /note="LRR 6"
FT   DOMAIN          254..304
FT                   /note="LRRCT 1"
FT   DOMAIN          310..346
FT                   /note="LRRNT 2"
FT   REPEAT          347..368
FT                   /note="LRR 7"
FT   REPEAT          371..392
FT                   /note="LRR 8"
FT   REPEAT          395..416
FT                   /note="LRR 9"
FT   REPEAT          419..440
FT                   /note="LRR 10"
FT   REPEAT          443..464
FT                   /note="LRR 11"
FT   DOMAIN          476..526
FT                   /note="LRRCT 2"
FT   DOMAIN          534..570
FT                   /note="LRRNT 3"
FT   REPEAT          571..592
FT                   /note="LRR 12"
FT   REPEAT          596..617
FT                   /note="LRR 13"
FT   REPEAT          620..641
FT                   /note="LRR 14"
FT   REPEAT          644..665
FT                   /note="LRR 15"
FT   DOMAIN          677..727
FT                   /note="LRRCT 3"
FT   DOMAIN          730..766
FT                   /note="LRRNT 4"
FT   REPEAT          767..788
FT                   /note="LRR 16"
FT   REPEAT          791..812
FT                   /note="LRR 17"
FT   REPEAT          815..836
FT                   /note="LRR 18"
FT   REPEAT          839..860
FT                   /note="LRR 19"
FT   DOMAIN          872..922
FT                   /note="LRRCT 4"
FT   DOMAIN          931..968
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          970..1007
FT                   /note="EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1009..1046
FT                   /note="EGF-like 3; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1048..1086
FT                   /note="EGF-like 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1088..1124
FT                   /note="EGF-like 5; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1135..1173
FT                   /note="EGF-like 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1176..1349
FT                   /note="Laminin G-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          1377..1416
FT                   /note="EGF-like 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1433..1504
FT                   /note="CTCK"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT   SITE            1135..1136
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        111
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        231
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        381
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        459
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        807
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        812
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        982
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1022
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1084
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1183
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1199
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1267
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1316
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        543..549
FT                   /evidence="ECO:0000269|PubMed:15496984"
FT   DISULFID        547..556
FT                   /evidence="ECO:0000269|PubMed:15496984"
FT   DISULFID        657..733
FT                   /evidence="ECO:0000269|PubMed:15496984"
FT   DISULFID        681..704
FT                   /evidence="ECO:0000269|PubMed:15496984"
FT   DISULFID        683..725
FT                   /evidence="ECO:0000269|PubMed:15496984"
FT   DISULFID        935..946
FT                   /evidence="ECO:0000250"
FT   DISULFID        940..956
FT                   /evidence="ECO:0000250"
FT   DISULFID        958..967
FT                   /evidence="ECO:0000250"
FT   DISULFID        974..985
FT                   /evidence="ECO:0000250"
FT   DISULFID        979..995
FT                   /evidence="ECO:0000250"
FT   DISULFID        997..1006
FT                   /evidence="ECO:0000250"
FT   DISULFID        1013..1025
FT                   /evidence="ECO:0000250"
FT   DISULFID        1019..1034
FT                   /evidence="ECO:0000250"
FT   DISULFID        1036..1045
FT                   /evidence="ECO:0000250"
FT   DISULFID        1052..1065
FT                   /evidence="ECO:0000250"
FT   DISULFID        1059..1074
FT                   /evidence="ECO:0000250"
FT   DISULFID        1076..1085
FT                   /evidence="ECO:0000250"
FT   DISULFID        1092..1103
FT                   /evidence="ECO:0000250"
FT   DISULFID        1097..1112
FT                   /evidence="ECO:0000250"
FT   DISULFID        1114..1123
FT                   /evidence="ECO:0000250"
FT   DISULFID        1139..1149
FT                   /evidence="ECO:0000250"
FT   DISULFID        1144..1161
FT                   /evidence="ECO:0000250"
FT   DISULFID        1163..1172
FT                   /evidence="ECO:0000250"
FT   DISULFID        1323..1349
FT                   /evidence="ECO:0000250"
FT   DISULFID        1381..1392
FT                   /evidence="ECO:0000250"
FT   DISULFID        1386..1404
FT                   /evidence="ECO:0000250"
FT   DISULFID        1406..1415
FT                   /evidence="ECO:0000250"
FT   DISULFID        1433..1467
FT                   /evidence="ECO:0000250"
FT   DISULFID        1447..1481
FT                   /evidence="ECO:0000250"
FT   DISULFID        1458..1497
FT                   /evidence="ECO:0000250"
FT   DISULFID        1462..1499
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         152..175
FT                   /note="Missing (in isoform A and isoform B)"
FT                   /evidence="ECO:0000303|PubMed:2176636"
FT                   /id="VSP_001408"
FT   VAR_SEQ         1418..1428
FT                   /note="Missing (in isoform B)"
FT                   /evidence="ECO:0000303|PubMed:2176636"
FT                   /id="VSP_001409"
FT   CONFLICT        350..351
FT                   /note="EL -> DV (in Ref. 1; CAA37910 and 2; AAD26567)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        421
FT                   /note="Q -> R (in Ref. 1; CAA37910)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        468
FT                   /note="I -> M (in Ref. 1; CAA37910)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        527
FT                   /note="D -> G (in Ref. 1; CAA37910)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        560
FT                   /note="G -> R (in Ref. 1; CAA37910)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        691..692
FT                   /note="WL -> CV (in Ref. 1; CAA37910)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        751
FT                   /note="R -> A (in Ref. 1; CAA37910)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        843
FT                   /note="L -> V (in Ref. 1; CAA37910)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1207..1208
FT                   /note="AE -> G (in Ref. 5; AAA72722)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1429..1435
FT                   /note="AASTCRK -> GTYIYHA (in Ref. 5; AAA72722)"
FT                   /evidence="ECO:0000305"
FT   STRAND          547..550
FT                   /evidence="ECO:0007829|PDB:1W8A"
FT   STRAND          553..555
FT                   /evidence="ECO:0007829|PDB:1W8A"
FT   STRAND          573..576
FT                   /evidence="ECO:0007829|PDB:1W8A"
FT   HELIX           591..593
FT                   /evidence="ECO:0007829|PDB:1W8A"
FT   STRAND          599..601
FT                   /evidence="ECO:0007829|PDB:1W8A"
FT   TURN            612..617
FT                   /evidence="ECO:0007829|PDB:1W8A"
FT   STRAND          623..625
FT                   /evidence="ECO:0007829|PDB:1W8A"
FT   STRAND          636..639
FT                   /evidence="ECO:0007829|PDB:1W8A"
FT   STRAND          647..649
FT                   /evidence="ECO:0007829|PDB:1W8A"
FT   STRAND          671..673
FT                   /evidence="ECO:0007829|PDB:1W8A"
FT   HELIX           683..685
FT                   /evidence="ECO:0007829|PDB:1W8A"
FT   HELIX           686..695
FT                   /evidence="ECO:0007829|PDB:1W8A"
FT   HELIX           699..701
FT                   /evidence="ECO:0007829|PDB:1W8A"
FT   TURN            708..712
FT                   /evidence="ECO:0007829|PDB:1W8A"
FT   HELIX           715..717
FT                   /evidence="ECO:0007829|PDB:1W8A"
FT   TURN            720..722
FT                   /evidence="ECO:0007829|PDB:1W8A"
SQ   SEQUENCE   1504 AA;  168599 MW;  836A3F5022BF234F CRC64;
     MAAPSRTTLM PPPFRLQLRL LILPILLLLR HDAVHAEPYS GGFGSSAVSS GGLGSVGIHI
     PGGGVGVITE ARCPRVCSCT GLNVDCSHRG LTSVPRKISA DVERLELQGN NLTVIYETDF
     QRLTKLRMLQ LTDNQIHTIE RNSFQDLVSL ERLRLNNNRL KAIPENFVTS SASLLRLDIS
     NNVITTVGRR VFKGAQSLRS LQLDNNQITC LDEHAFKGLV ELEILTLNNN NLTSLPHNIF
     GGLGRLRALR LSDNPFACDC HLSWLSRFLR SATRLAPYTR CQSPSQLKGQ NVADLHDQEF
     KCSGLTEHAP MECGAENSCP HPCRCADGIV DCREKSLTSV PVTLPDDTTE LRLEQNFITE
     LPPKSFSSFR RLRRIDLSNN NISRIAHDAL SGLKQLTTLV LYGNKIKDLP SGVFKGLGSL
     QLLLLNANEI SCIRKDAFRD LHSLSLLSLY DNNIQSLANG TFDAMKSIKT VHLAKNPFIC
     DCNLRWLADY LHKNPIETSG ARCESPKRMH RRRIESLREE KFKCSWDELR MKLSGECRMD
     SDCPAMCHCE GTTVDCTGRG LKEIPRDIPL HTTELLLNDN ELGRISSDGL FGRLPHLVKL
     ELKRNQLTGI EPNAFEGASH IQELQLGENK IKEISNKMFL GLHQLKTLNL YDNQISCVMP
     GSFEHLNSLT SLNLASNPFN CNCHLAWFAE WLRKKSLNGG AARCGAPSKV RDVQIKDLPH
     SEFKCSSENS EGCLGDGYCP PSCTCTGTVV RCSRNQLKEI PRGIPAETSE LYLESNEIEQ
     IHYERIRHLR SLTRLDLSNN QITILSNYTF ANLTKLSTLI ISYNKLQCLQ RHALSGLNNL
     RVLSLHGNRI SMLPEGSFED LKSLTHIALG SNPLYCDCGL KWFSDWIKLD YVEPGIARCA
     EPEQMKDKLI LSTPSSSFVC RGRVRNDILA KCNACFEQPC QNQAQCVALP QREYQCLCQP
     GYHGKHCEFM IDACYGNPCR NNATCTVLEE GRFSCQCAPG YTGARCETNI DDCLGEIKCQ
     NNATCIDGVE SYKCECQPGF SGEFCDTKIQ FCSPEFNPCA NGAKCMDHFT HYSCDCQAGF
     HGTNCTDNID DCQNHMCQNG GTCVDGINDY QCRCPDDYTG KYCEGHNMIS MMYPQTSPCQ
     NHECKHGVCF QPNAQGSDYL CRCHPGYTGK WCEYLTSISF VHNNSFVELE PLRTRPEANV
     TIVFSSAEQN GILMYDGQDA HLAVELFNGR IRVSYDVGNH PVSTMYSFEM VADGKYHAVE
     LLAIKKNFTL RVDRGLARSI INEGSNDYLK LTTPMFLGGL PVDPAQQAYK NWQIRNLTSF
     KGCMKEVWIN HKLVDFGNAQ RQQKITPGCA LLEGEQQEEE DDEQDFMDET PHIKEEPVDP
     CLENKCRRGS RCVPNSNARD GYQCKCKHGQ RGRYCDQGEG STEPPTVTAA STCRKEQVRE
     YYTENDCRSR QPLKYAKCVG GCGNQCCAAK IVRRRKVRMV CSNNRKYIKN LDIVRKCGCT
     KKCY
//