SLIT_DROME
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 03-AUG-2022, entry version 223.
DE RecName: Full=Protein slit;
DE Short=dSlit;
DE Contains:
DE RecName: Full=Protein slit N-product;
DE Contains:
DE RecName: Full=Protein slit C-product;
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 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 -!- SUBUNIT: Interacts with robo. {ECO:0000269|PubMed:10102268}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2176636,
CC ECO:0000269|PubMed:3144436}.
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}.
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.FBpp0303575; -.
DR GlyGen; P24014; 13 sites.
DR PaxDb; P24014; -.
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 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 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 tissues.
DR ExpressionAtlas; P24014; baseline and differential.
DR Genevisible; P24014; DM.
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; cd00110; LamG; 1.
DR Gene3D; 3.80.10.10; -; 5.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR006207; Cys_knot_C.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR Pfam; PF00008; EGF; 4.
DR Pfam; PF12661; hEGF; 1.
DR Pfam; PF00054; Laminin_G_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; SM00369; LRR_TYP; 16.
DR SMART; SM00082; LRRCT; 4.
DR SMART; SM00013; LRRNT; 4.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
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.
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
