ID A0A452FTA7_CAPHI Unreviewed; 1409 AA.
AC A0A452FTA7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Crumbs cell polarity complex component 1 {ECO:0000313|Ensembl:ENSCHIP00000027469.1};
GN Name=CRB1 {ECO:0000313|Ensembl:ENSCHIP00000027469.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000027469.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000027469.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000027469.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; LWLT01000016; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005691110.2; XM_005691053.3.
DR STRING; 9925.ENSCHIP00000027469; -.
DR Ensembl; ENSCHIT00000035337.1; ENSCHIP00000027469.1; ENSCHIG00000023383.1.
DR GeneID; 102171360; -.
DR KEGG; chx:102171360; -.
DR CTD; 23418; -.
DR GeneTree; ENSGT00940000155152; -.
DR OMA; NCTEFQG; -.
DR OrthoDB; 2877476at2759; -.
DR Proteomes; UP000291000; Chromosome 16.
DR Bgee; ENSCHIG00000023383; Expressed in prefrontal cortex and 4 other cell types or tissues.
DR GO; GO:0005912; C:adherens junction; IEA:Ensembl.
DR GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR GO; GO:0097386; C:glial cell projection; IEA:Ensembl.
DR GO; GO:0005902; C:microvillus; IEA:Ensembl.
DR GO; GO:0001750; C:photoreceptor outer segment; IEA:Ensembl.
DR GO; GO:0035003; C:subapical complex; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0001974; P:blood vessel remodeling; IEA:Ensembl.
DR GO; GO:0071482; P:cellular response to light stimulus; IEA:Ensembl.
DR GO; GO:0050908; P:detection of light stimulus involved in visual perception; IEA:Ensembl.
DR GO; GO:0061159; P:establishment of bipolar cell polarity involved in cell morphogenesis; IEA:Ensembl.
DR GO; GO:0042462; P:eye photoreceptor cell development; IEA:Ensembl.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0010001; P:glial cell differentiation; IEA:Ensembl.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IEA:Ensembl.
DR GO; GO:0035845; P:photoreceptor cell outer segment organization; IEA:Ensembl.
DR GO; GO:0007009; P:plasma membrane organization; IEA:Ensembl.
DR GO; GO:0060060; P:post-embryonic retina morphogenesis in camera-type eye; IEA:Ensembl.
DR GO; GO:0008104; P:protein localization; IEA:Ensembl.
DR GO; GO:0010842; P:retina layer formation; IEA:Ensembl.
DR CDD; cd00054; EGF_CA; 13.
DR CDD; cd00110; LamG; 3.
DR Gene3D; 2.60.120.200; -; 3.
DR Gene3D; 2.10.25.10; Laminin; 17.
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 PANTHER; PTHR24044:SF420; NEUROGENIC LOCUS PROTEIN DELTA; 1.
DR PANTHER; PTHR24044; NOTCH LIGAND FAMILY MEMBER; 1.
DR Pfam; PF00008; EGF; 11.
DR Pfam; PF12661; hEGF; 2.
DR Pfam; PF02210; Laminin_G_2; 3.
DR PRINTS; PR00010; EGFBLOOD.
DR SMART; SM00181; EGF; 17.
DR SMART; SM00179; EGF_CA; 16.
DR SMART; SM00282; LamG; 3.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR SUPFAM; SSF57196; EGF/Laminin; 5.
DR SUPFAM; SSF57184; Growth factor receptor domain; 3.
DR PROSITE; PS00010; ASX_HYDROXYL; 7.
DR PROSITE; PS00022; EGF_1; 14.
DR PROSITE; PS01186; EGF_2; 9.
DR PROSITE; PS50026; EGF_3; 18.
DR PROSITE; PS01187; EGF_CA; 4.
DR PROSITE; PS50025; LAM_G_DOMAIN; 3.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Notch signaling pathway {ECO:0000256|ARBA:ARBA00022976};
KW Reference proteome {ECO:0000313|Proteomes:UP000291000};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1409
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019282127"
FT TRANSMEM 1347..1372
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 30..68
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 70..108
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 110..146
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 148..184
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 186..222
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 224..260
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 262..299
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 301..337
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 339..396
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 398..440
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 442..482
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 486..672
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 674..710
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 716..887
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 889..925
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 953..1139
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1141..1177
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1179..1215
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1217..1253
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1258..1298
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1300..1336
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 79..96
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 98..107
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 136..145
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 174..183
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 212..221
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 250..259
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 327..336
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 386..395
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 472..481
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 700..709
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 915..924
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1167..1176
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1183..1193
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1205..1214
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1243..1252
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1288..1297
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1326..1335
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1409 AA; 151784 MW; C5689AA638366B4B CRC64;
MALRTVSHRL LLCLSLSLLI SIKSSFCNKN DTKCVSNSCQ NNSTCKDFSK DKSCRCSDTA
IHGDKDCGEE EDPCLSSPCP EHATCVRVPG ERRSLCRCPP GHSRAGCDTA AGPCGPSSCL
HGGVCHRDSG PPVCVCPTGY TGRFCELDLD ECASSPCLHG AVCQDGGDGY SCFCVPGYQG
RRCDVEVDEC VSEPCQNAAT CLNEIGRYTC LCPRGFSGVN CELEVDECWS QPCLNGATCQ
DAVGAYFCDC APGFLGNRCE LNTDECASGP CLHGGLCVDG ANRYTCTCAG SGFTGTRCET
PLPPCWSQPC HNNAICEDSA DRYTCRCRPG YTGAQCETDL DGCGSGPCQA GGRCVELPSE
TGRERLARLL SASRRPEAFP RYLCICPPGL TGVHCEEDVD ECSSSPCRNG GTCENSPEGY
ACRCPFDPRS GVFFGGRDCS DILLGCADHP CLNNGTCFPH VHDGRHRFDC LCPAGYTGSR
CGTVTTLSFE GSGFLWVSSG SAPAQESGCT IALRFQTVQP AALLLFRGDQ DAFMMLEVLA
GFVHLTVQVG NRPKVVLLIP HDTSDGGWHT VEATFAEAVT LALRDDSCTG TCIARAPSPF
ESAGSSACAL QNSFLGGLPE GRAHSGDALF NVYKMPSAPS LVGCLQDVHL DSNAITAESI
SSDQSLNVRA GCTRKDWCES QPCQNRGRCL NLWLGHQCEC YRPYRGRGCH GEYVAGRFGQ
DDSPGYAVFH LNKDYEEDLA LSMFVRTRRP AGLLLALGNG TYQYLRVWLE HGRLGMLTPG
SPKLLVTFVL SDGNVHLVSL KIKPNKIELY QSSQNLGFLS APTWKLQKGD VLYVGGLPNR
RETEVSGGFF KGCIQDIRLN NENLEFFPNS TSSAAHNAVL VNVTEGCPGD SLCEPNPCHH
GGVCYPLWDD FSCSCPANTA GKACQELRWC ELGPCPPGAQ CLQLPRGFEC IANAVFNGQS
HELIFRSNGN ITRELTNVTF GFRTRDAHAI ILHAEKEPEF LRIHIRDSRL LFQLQSGNSL
YTLSLTSLQP VSDGVWYQVT ISMTDPGAQA SRWQMEVDGQ TPPVTSTVAA GSLSFLKDDT
NVYVGDRASN STRALRGCLS TIAISGLYLS YFENVGGLMN RPQEERFLKV SGPPVETGCL
QLDACRSGPC LHGGRCKDTY SSHRCTCPAG RSGPHCELDV DECLSRPCIH GNCSAPAGAG
YHCRCEPGFT GVNCESEVDH CQRHQCANGA TCISDANGYS CRCPGNFTGR FCRYLRLPST
FCGNEKTNLT CYNGGNCTEF QGEMKCACWP GFTGERCDKD IDECASDPCL HGGRCHDLLN
GFRCTCALAF AGPRCELDLA DDLLSDVFAA IGSVTLALLL ILFLAVVASV LASNKRATQG
SYSPSRQEKD GSRVEMWSVM DAPAAERLI
//