GenomeNet

Database: UniProt
Entry: P10040
LinkDB: P10040
Original site: P10040 
ID   CRB_DROME               Reviewed;        2146 AA.
AC   P10040; Q0KI19; Q8MSX5; Q9VC97;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 3.
DT   10-APR-2019, entry version 209.
DE   RecName: Full=Protein crumbs;
DE   AltName: Full=95F;
DE   Flags: Precursor;
GN   Name=crb; ORFNames=CG6383;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR
RP   LOCATION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=Oregon-R; TISSUE=Embryo;
RX   PubMed=2344615; DOI=10.1016/0092-8674(90)90189-L;
RA   Tepass U., Theres C., Knust E.;
RT   "Crumbs encodes an EGF-like protein expressed on apical membranes of
RT   Drosophila epithelial cells and required for organization of
RT   epithelia.";
RL   Cell 61:787-799(1990).
RN   [2]
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.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   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.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   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.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
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.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1578-2146.
RC   STRAIN=Berkeley; TISSUE=Embryo;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
RA   George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
RA   Rubin G.M., Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1661-1952.
RC   TISSUE=Embryo;
RX   PubMed=3107986;
RA   Knust E., Dietrich U., Tepass U., Bremer K.A., Weigel D., Vaessin H.,
RA   Campos-Ortega J.A.;
RT   "EGF homologous sequences encoded in the genome of Drosophila
RT   melanogaster, and their relation to neurogenic genes.";
RL   EMBO J. 6:761-766(1987).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH PATJ.
RX   PubMed=10102271; DOI=10.1016/S0092-8674(00)80593-0;
RA   Bhat M.A., Izaddoost S., Lu Y., Cho K.-O., Choi K.-W., Bellen H.J.;
RT   "Discs Lost, a novel multi-PDZ domain protein, establishes and
RT   maintains epithelial polarity.";
RL   Cell 96:833-845(1999).
RN   [7]
RP   ERRATUM.
RA   Bhat M.A., Izaddoost S., Lu Y., Cho K.-O., Choi K.-W., Bellen H.J.;
RL   Cell 115:765-766(2003).
RN   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PATJ.
RX   PubMed=11076972; DOI=10.1083/jcb.151.4.891;
RA   Tanentzapf G., Smith C., McGlade J., Tepass U.;
RT   "Apical, lateral, and basal polarization cues contribute to the
RT   development of the follicular epithelium during Drosophila
RT   oogenesis.";
RL   J. Cell Biol. 151:891-904(2000).
RN   [9]
RP   IDENTIFICATION IN A SAC COMPLEX WITH PATJ AND SDT.
RX   PubMed=11740560; DOI=10.1038/414638a;
RA   Bachmann A., Schneider M., Theilenberg E., Grawe F., Knust E.;
RT   "Drosophila Stardust is a partner of Crumbs in the control of
RT   epithelial cell polarity.";
RL   Nature 414:638-643(2001).
RN   [10]
RP   FUNCTION, AND INTERACTION WITH THE PAR-6 COMPLEX.
RX   PubMed=12900452; DOI=10.1242/dev.00648;
RA   Nam S.-C., Choi K.-W.;
RT   "Interaction of Par-6 and Crumbs complexes is essential for
RT   photoreceptor morphogenesis in Drosophila.";
RL   Development 130:4363-4372(2003).
RN   [11]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1100, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY.
RC   STRAIN=Oregon-R; TISSUE=Head;
RX   PubMed=17893096; DOI=10.1093/glycob/cwm097;
RA   Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,
RA   Panin V.;
RT   "Identification of N-glycosylated proteins from the central nervous
RT   system of Drosophila melanogaster.";
RL   Glycobiology 17:1388-1403(2007).
RN   [12]
RP   FUNCTION, INTERACTION WITH THE CGX COMPLEX, SUBCELLULAR LOCATION, AND
RP   DISRUPTION PHENOTYPE.
RX   PubMed=25065591; DOI=10.1038/onc.2014.202;
RA   Yeom E., Hong S.T., Choi K.W.;
RT   "Crumbs interacts with Xpd for nuclear division control in
RT   Drosophila.";
RL   Oncogene 34:2777-2789(2015).
CC   -!- FUNCTION: Plays a central role in cell polarity establishment
CC       (PubMed:2344615, PubMed:12900452, PubMed:10102271,
CC       PubMed:11740560). Participates in the assembly, positioning and
CC       maintenance of adherens junctions via its interaction with the SAC
CC       complex (PubMed:11740560, PubMed:12900452, PubMed:10102271,
CC       PubMed:11076972). Controls the coalescence of the spots of zonula
CC       adherens (ZA) into a adhesive ring around the cells
CC       (PubMed:11740560). It may act as a signal (PubMed:2344615).
CC       Involved in morphogenesis of the photoreceptor rhabdomere, for
CC       positioning and growth of rhabdomere and AJ during the crucial
CC       period of photoreceptor extension along the proximodistal axis of
CC       the retina (PubMed:12900452). Component of the crb-galla-Xpd (CGX)
CC       complex which is essential for proper mitotic chromosome
CC       segregation in early embryos (PubMed:25065591). The CGX complex is
CC       also required for cell proliferation in developing wing disks
CC       (PubMed:25065591). In the CGX complex, acts with galla-1 or galla-
CC       2 to recruit Xpd and thus form the functional complex.
CC       {ECO:0000269|PubMed:10102271, ECO:0000269|PubMed:11076972,
CC       ECO:0000269|PubMed:11740560, ECO:0000269|PubMed:12900452,
CC       ECO:0000269|PubMed:2344615, ECO:0000269|PubMed:25065591}.
CC   -!- SUBUNIT: Component of the SAC complex, a complex composed of crb,
CC       Patj and sdt (PubMed:11740560, PubMed:10102271, PubMed:11076972).
CC       May interact with the par-6 complex, which is composed of par-6,
CC       baz and aPKC, via its interaction with Patj (PubMed:12900452,
CC       PubMed:10102271, PubMed:11076972). Interacts with other proteins
CC       with Patj and sdt via its short cytoplasmic tail
CC       (PubMed:11740560). Component of the CGX complex composed of crb,
CC       galla (galla-1 or galla-2) and Xpd (PubMed:25065591). Able to
CC       interact independently (via intracellular domain) with galla-1,
CC       galla-2 and Xpd (PubMed:25065591). {ECO:0000269|PubMed:10102271,
CC       ECO:0000269|PubMed:11076972, ECO:0000269|PubMed:11740560,
CC       ECO:0000269|PubMed:12900452, ECO:0000269|PubMed:25065591}.
CC   -!- INTERACTION:
CC       A1Z9X0:aPKC; NbExp=3; IntAct=EBI-672928, EBI-160861;
CC       Q07436:ex; NbExp=2; IntAct=EBI-672928, EBI-192660;
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000269|PubMed:11076972, ECO:0000269|PubMed:2344615}; Single-
CC       pass type I membrane protein {ECO:0000269|PubMed:11076972,
CC       ECO:0000269|PubMed:2344615}. Cytoplasm, cytoskeleton, spindle
CC       {ECO:0000269|PubMed:25065591}. Note=Specifically localized to the
CC       apical membrane (PubMed:11076972, PubMed:2344615). Expressed in a
CC       mesh punctate pattern that overlaps with metaphase spindle
CC       microtubules (PubMed:25065591). {ECO:0000269|PubMed:11076972,
CC       ECO:0000269|PubMed:2344615, ECO:0000269|PubMed:25065591}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=A;
CC         IsoId=P10040-1; Sequence=Displayed;
CC       Name=B;
CC         IsoId=P10040-2; Sequence=VSP_031870;
CC         Note=No experimental confirmation available.;
CC   -!- PTM: Phosphorylated in the cytoplasmic domain. {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Flies show severe disruptions in the
CC       organization of ectodermally derived epithelia and leading in some
CC       cases to cell death in these tissues (PubMed:2344615). RNAi-
CC       mediated knockdown in germline cells results in severe chromosomal
CC       and spindle microtubule defects such as chromosome bridges, bent
CC       chromosomes, monopolar spindles and fusion with one or more
CC       neighboring spindles (PubMed:25065591).
CC       {ECO:0000269|PubMed:2344615, ECO:0000269|PubMed:25065591}.
CC   -!- SIMILARITY: Belongs to the Crumbs protein family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM49878.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; M33753; AAA28428.1; -; mRNA.
DR   EMBL; AE014297; AAF56276.1; -; Genomic_DNA.
DR   EMBL; AE014297; ABI31202.1; -; Genomic_DNA.
DR   EMBL; AY118509; AAM49878.1; ALT_INIT; mRNA.
DR   EMBL; X05144; CAA28793.1; -; mRNA.
DR   PIR; A35672; A35672.
DR   PIR; B26637; B26637.
DR   RefSeq; NP_001036751.1; NM_001043286.2. [P10040-2]
DR   RefSeq; NP_524480.2; NM_079756.3. [P10040-1]
DR   UniGene; Dm.2365; -.
DR   PDB; 4WSI; X-ray; 2.95 A; X/Y=2110-2146.
DR   PDB; 4YL8; X-ray; 1.50 A; B=2110-2146.
DR   PDBsum; 4WSI; -.
DR   PDBsum; 4YL8; -.
DR   ProteinModelPortal; P10040; -.
DR   SMR; P10040; -.
DR   BioGrid; 67824; 56.
DR   DIP; DIP-40915N; -.
DR   IntAct; P10040; 9.
DR   MINT; P10040; -.
DR   TCDB; 9.B.87.1.11; the selenoprotein p receptor (selp-receptor) family.
DR   iPTMnet; P10040; -.
DR   PaxDb; P10040; -.
DR   PRIDE; P10040; -.
DR   EnsemblMetazoa; FBtr0084603; FBpp0083987; FBgn0259685. [P10040-1]
DR   EnsemblMetazoa; FBtr0111008; FBpp0110307; FBgn0259685. [P10040-2]
DR   GeneID; 42896; -.
DR   KEGG; dme:Dmel_CG6383; -.
DR   CTD; 42896; -.
DR   FlyBase; FBgn0259685; crb.
DR   eggNOG; KOG1217; Eukaryota.
DR   eggNOG; ENOG410XP6K; LUCA.
DR   InParanoid; P10040; -.
DR   KO; K16681; -.
DR   OMA; YFNGSAY; -.
DR   PhylomeDB; P10040; -.
DR   SignaLink; P10040; -.
DR   GenomeRNAi; 42896; -.
DR   PRO; PR:P10040; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0259685; Expressed in 33 organ(s), highest expression level in embryo.
DR   ExpressionAtlas; P10040; differential.
DR   Genevisible; P10040; DM.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:FlyBase.
DR   GO; GO:0016327; C:apicolateral plasma membrane; IDA:FlyBase.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; HDA:FlyBase.
DR   GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR   GO; GO:0016028; C:rhabdomere; IDA:FlyBase.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0035003; C:subapical complex; TAS:FlyBase.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005080; F:protein kinase C binding; IPI:FlyBase.
DR   GO; GO:0030507; F:spectrin binding; TAS:FlyBase.
DR   GO; GO:0034332; P:adherens junction organization; IMP:FlyBase.
DR   GO; GO:0046665; P:amnioserosa maintenance; IMP:FlyBase.
DR   GO; GO:0003383; P:apical constriction; IMP:FlyBase.
DR   GO; GO:0045176; P:apical protein localization; IMP:FlyBase.
DR   GO; GO:0106036; P:assembly of apicomedial cortex actomyosin; IMP:FlyBase.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0061336; P:cell morphogenesis involved in Malpighian tubule morphogenesis; IMP:FlyBase.
DR   GO; GO:0051642; P:centrosome localization; IMP:FlyBase.
DR   GO; GO:0001745; P:compound eye morphogenesis; IMP:FlyBase.
DR   GO; GO:0042051; P:compound eye photoreceptor development; IMP:FlyBase.
DR   GO; GO:0007391; P:dorsal closure; IMP:FlyBase.
DR   GO; GO:0046664; P:dorsal closure, amnioserosa morphology change; IMP:FlyBase.
DR   GO; GO:0035088; P:establishment or maintenance of apical/basal cell polarity; IMP:FlyBase.
DR   GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:FlyBase.
DR   GO; GO:0016332; P:establishment or maintenance of polarity of embryonic epithelium; IMP:FlyBase.
DR   GO; GO:0016334; P:establishment or maintenance of polarity of follicular epithelium; IMP:FlyBase.
DR   GO; GO:0035002; P:liquid clearance, open tracheal system; IGI:FlyBase.
DR   GO; GO:0035090; P:maintenance of apical/basal cell polarity; IMP:FlyBase.
DR   GO; GO:0007443; P:Malpighian tubule morphogenesis; IMP:FlyBase.
DR   GO; GO:0061024; P:membrane organization; IMP:FlyBase.
DR   GO; GO:0045746; P:negative regulation of Notch signaling pathway; IGI:FlyBase.
DR   GO; GO:0046621; P:negative regulation of organ growth; IMP:FlyBase.
DR   GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IGI:FlyBase.
DR   GO; GO:0007399; P:nervous system development; IMP:FlyBase.
DR   GO; GO:0098813; P:nuclear chromosome segregation; IMP:FlyBase.
DR   GO; GO:0007424; P:open tracheal system development; IMP:FlyBase.
DR   GO; GO:0045494; P:photoreceptor cell maintenance; IMP:FlyBase.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:FlyBase.
DR   GO; GO:0035332; P:positive regulation of hippo signaling; IMP:FlyBase.
DR   GO; GO:0050821; P:protein stabilization; IMP:FlyBase.
DR   GO; GO:0045570; P:regulation of imaginal disc growth; IMP:FlyBase.
DR   GO; GO:0033157; P:regulation of intracellular protein transport; IMP:FlyBase.
DR   GO; GO:0032880; P:regulation of protein localization; IMP:FlyBase.
DR   GO; GO:0042052; P:rhabdomere development; IMP:FlyBase.
DR   GO; GO:0061541; P:rhabdomere morphogenesis; IMP:FlyBase.
DR   GO; GO:0007435; P:salivary gland morphogenesis; IMP:FlyBase.
DR   GO; GO:0035239; P:tube morphogenesis; IMP:FlyBase.
DR   GO; GO:0045186; P:zonula adherens assembly; IMP:FlyBase.
DR   GO; GO:0045218; P:zonula adherens maintenance; IMP:FlyBase.
DR   InterPro; IPR013320; ConA-like_dom_sf.
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   Pfam; PF00008; EGF; 17.
DR   Pfam; PF07645; EGF_CA; 2.
DR   Pfam; PF12661; hEGF; 3.
DR   Pfam; PF00054; Laminin_G_1; 2.
DR   Pfam; PF02210; Laminin_G_2; 1.
DR   SMART; SM00181; EGF; 28.
DR   SMART; SM00179; EGF_CA; 23.
DR   SMART; SM00282; LamG; 3.
DR   SUPFAM; SSF49899; SSF49899; 4.
DR   SUPFAM; SSF57184; SSF57184; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 16.
DR   PROSITE; PS00022; EGF_1; 25.
DR   PROSITE; PS01186; EGF_2; 17.
DR   PROSITE; PS50026; EGF_3; 27.
DR   PROSITE; PS01187; EGF_CA; 13.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 3.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell cycle; Cell division;
KW   Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton;
KW   Developmental protein; Differentiation; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Membrane; Mitosis; Phosphoprotein;
KW   Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     88
FT   CHAIN        89   2146       Protein crumbs.
FT                                /FTId=PRO_0000007499.
FT   TOPO_DOM     89   2082       Extracellular. {ECO:0000255}.
FT   TRANSMEM   2083   2109       Helical. {ECO:0000255}.
FT   TOPO_DOM   2110   2146       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      265    301       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      304    341       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      346    384       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      386    423       EGF-like 4; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      425    461       EGF-like 5; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      462    498       EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      543    579       EGF-like 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      609    644       EGF-like 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      646    683       EGF-like 9; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      685    721       EGF-like 10; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      723    759       EGF-like 11; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      761    798       EGF-like 12; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      800    836       EGF-like 13; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      838    900       EGF-like 14. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      902    938       EGF-like 15; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      940    976       EGF-like 16; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      978   1019       EGF-like 17. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1021   1203       Laminin G-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     1205   1241       EGF-like 18. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1248   1483       Laminin G-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     1479   1515       EGF-like 19. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1555   1757       Laminin G-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     1758   1792       EGF-like 20. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1794   1830       EGF-like 21; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1832   1868       EGF-like 22; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1871   1909       EGF-like 23. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1912   1948       EGF-like 24. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1950   1987       EGF-like 25; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1989   2027       EGF-like 26; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     2028   2068       EGF-like 27. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   CARBOHYD     94     94       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    196    196       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    236    236       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    237    237       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    334    334       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    398    398       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    548    548       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    563    563       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    734    734       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    744    744       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    858    858       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    882    882       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    974    974       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1006   1006       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1100   1100       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:17893096}.
FT   CARBOHYD   1112   1112       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1136   1136       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1190   1190       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1243   1243       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1253   1253       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1352   1352       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1361   1361       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1439   1439       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1452   1452       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1543   1543       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1737   1737       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1749   1749       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1806   1806       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1846   1846       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1882   1882       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1891   1891       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1897   1897       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2027   2027       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2033   2033       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2066   2066       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    269    280       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    274    289       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    291    300       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    308    319       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    313    329       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    331    340       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    350    361       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    355    372       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    374    383       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    390    401       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    395    410       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    412    422       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    429    440       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    434    449       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    451    460       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    466    477       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    471    486       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    488    497       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    547    560       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    554    567       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    569    578       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    611    622       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    616    632       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    634    643       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    650    662       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    657    671       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    673    682       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    689    700       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    694    709       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    711    720       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    727    738       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    732    747       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    749    758       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    765    776       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    770    785       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    787    797       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    804    815       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    809    824       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    826    835       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    842    853       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    847    888       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    890    899       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    906    917       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    911    926       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    928    937       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    944    955       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    950    964       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    966    975       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    982    993       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    987   1007       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1009   1018       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1171   1203       {ECO:0000255|PROSITE-ProRule:PRU00122}.
FT   DISULFID   1209   1220       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1214   1229       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1231   1240       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1483   1494       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1488   1503       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1505   1514       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1713   1757       {ECO:0000255|PROSITE-ProRule:PRU00122}.
FT   DISULFID   1760   1771       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1765   1780       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1782   1791       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1798   1809       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1803   1818       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1820   1829       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1836   1847       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1841   1856       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1858   1867       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1875   1886       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1880   1900       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1916   1927       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1921   1936       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1938   1947       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1954   1965       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1959   1974       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1976   1986       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1993   2006       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2000   2015       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2017   2026       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2032   2044       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2038   2056       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2058   2067       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   VAR_SEQ     526    526       G -> ASDMEPLTPLELDILDATLCPSEKKKRYISPEWLKR
FT                                KRCELKLS (in isoform B). {ECO:0000305}.
FT                                /FTId=VSP_031870.
FT   CONFLICT   1661   1673       VDPTPAFSTDIDQ -> WWIRRQLFPRTSTK (in Ref.
FT                                5; CAA28793). {ECO:0000305}.
FT   CONFLICT   1719   1719       V -> L (in Ref. 1; AAA28428).
FT                                {ECO:0000305}.
FT   CONFLICT   1952   1952       N -> K (in Ref. 5; CAA28793).
FT                                {ECO:0000305}.
FT   STRAND     2116   2119       {ECO:0000244|PDB:4YL8}.
FT   TURN       2121   2123       {ECO:0000244|PDB:4YL8}.
FT   HELIX      2131   2135       {ECO:0000244|PDB:4WSI}.
SQ   SEQUENCE   2146 AA;  233572 MW;  8E23B9E32B761115 CRC64;
     MAKIANASLS QQQKQRQAET ATTTTTTVAA SVETATTTAR SRDRTKSAAQ ITSHLLKRAI
     SVYSSPQWIP LFILIYLATD VASVAVPTKE AYFNGSTYLR LTTPMPIWDH SAISFRSCRG
     GEILAQQYNK NSIVISVLND FLQISLAGPA VHGPNNRLDV KLPYQLLDNR WHTLQFKYEY
     GNLYLHVDRA ASIFANSTYN SQFLTNQDIG YKDAILILGN SFSGCLLDGP GLQFVNNSTV
     QNVVFGHCPL TPGPCSDHDL FTRLPDNFCL NDPCMGHGTC SSSPEGYECR CTARYSGKNC
     QKDNGSPCAK NPCENGGSCL ENSRGDYQCF CDPNHSGQHC ETEVNIHPLC QTNPCLNNGA
     CVVIGGSGAL TCECPKGYAG ARCEVDTDEC ASQPCQNNGS CIDRINGFSC DCSGTGYTGA
     FCQTNVDECD KNPCLNGGRC FDTYGWYTCQ CLDGWGGEIC DRPMTCQTQQ CLNGGTCLDK
     PIGFQCLCPP EYTGELCQIA PSCAQQCPID SECVGGKCVC KPGSSGYNCQ TSTGDGASAL
     ALTPINCNAT NGKCLNGGTC SMNGTHCYCA VGYSGDRCEK AENCSPLNCQ EPMVCVQNQC
     LCPENKVCNQ CATQPCQNGG ECVDLPNGDY ECKCTRGWTG RTCGNDVDEC TLHPKICGNG
     ICKNEKGSYK CYCTPGFTGV HCDSDVDECL SFPCLNGATC HNKINAYECV CQPGYEGENC
     EVDIDECGSN PCSNGSTCID RINNFTCNCI PGMTGRICDI DIDDCVGDPC LNGGQCIDQL
     GGFRCDCSGT GYEGENCELN IDECLSNPCT NGAKCLDRVK DYFCDCHNGY KGKNCEQDIN
     ECESNPCQYN GNCLERSNIT LYQMSRITDL PKVFSQPFSF ENASGYECVC VPGIIGKNCE
     ININECDSNP CSKHGNCNDG IGTYTCECEP GFEGTHCEIN IDECDRYNPC QRGTCYDQID
     DYDCDCDANY GGKNCSVLLK GCDQNPCLNG GACLPYLINE VTHLYNCTCE NGFQGDKCEK
     TTTLSMVATS LISVTTEREE GYDINLQFRT TLPNGVLAFG TTGEKNEPVS YILELINGRL
     NLHSSLLNKW EGVFIGSKLN DSNWHKVFVA INTSHLVLSA NDEQAIFPVG SYETANNSQP
     SFPRTYLGGT IPNLKSYLRH LTHQPSAFVG CMQDIMVNGK WIFPDEQDAN ISYTKLENVQ
     SGCPRTEQCK PNPCHSNGEC TDLWHTFACH CPRPFFGHTC QHNMTAATFG HENTTHSAVI
     VETTDVARRA IRSILDISMF IRTREPTGQV FYLGTDPRKA PTKNIGDSYV AAKLHGGELL
     VKMQFSGTPE AYTVGGQKLD NGYNHLIEVV RNQTLVQVKL NGTEYFRKTL STTGLLDAQV
     LYLGGPAPTR ESLLGATTEP GIIPVPGAGI PIEDTTVPKE ADDSRDYFKG IIQDVKVSNG
     SLNLIVEMYS LNVTDVQVNA KPLGAVTIDR ASVLPGEVSD DLCRKNPCLH NAECRNTWND
     YTCKCPNGYK GKNCQEIEFC QHVTCPGQSL CQNLDDGYEC VTNTTFTGQE RSPLAFFYFQ
     EQQSDDIVSE ASPKQTLKPV IDIAFRTRAG GTLLYIDNVD GFFEIGVNGG RVTITWKLSA
     LHFGESARFE KENTDGEWSR IYLRAHNSKL EGGWKGWESM VDPTPAFSTD IDQAAFQSLI
     ATSTQVYLGG MPESRQARGS TLSAQQGSQF KGCVGEARVG DLLLPYFSMA ELYSRTNVSV
     QQKAQFRLNA TRPEEGCILC FQSDCKNDGF CQSPSDEYAC TCQPGFEGDD CGTDIDECLN
     TECLNNGTCI NQVAAFFCQC QPGFEGQHCE QNIDECADQP CHNGGNCTDL IASYVCDCPE
     DYMGPQCDVL KQMTCENEPC RNGSTCQNGF NASTGNNFTC TCVPGFEGPL CDIPFCEITP
     CDNGGLCLTT GAVPMCKCSL GYTGRLCEQD INECESNPCQ NGGQCKDLVG RYECDCQGTG
     FEGIRCENDI DECNMEGDYC GGLGRCFNKP GSFQCICQKP YCGAYCNFTD PCNATDLCSN
     GGRCVESCGA KPDYYCECPE GFAGKNCTAP ITAKEDGPST TDIAIIVIPV VVVLLLIAGA
     LLGTFLVMAR NKRATRGTYS PSAQEYCNPR LEMDNVLKPP PEERLI
//
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