ID A0A2K6RKY7_RHIRO Unreviewed; 1287 AA.
AC A0A2K6RKY7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Crumbs cell polarity complex component 2 {ECO:0000313|Ensembl:ENSRROP00000041680.1};
GN Name=CRB2 {ECO:0000313|Ensembl:ENSRROP00000041680.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000041680.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000041680.1}
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 RefSeq; XP_010380760.1; XM_010382458.1.
DR STRING; 61622.ENSRROP00000041680; -.
DR Ensembl; ENSRROT00000066182.1; ENSRROP00000041680.1; ENSRROG00000044022.1.
DR GeneID; 104677438; -.
DR KEGG; rro:104677438; -.
DR CTD; 286204; -.
DR GeneTree; ENSGT00950000183101; -.
DR OMA; NCELNLN; -.
DR OrthoDB; 2877476at2759; -.
DR Proteomes; UP000233200; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0016327; C:apicolateral plasma membrane; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0035003; C:subapical complex; IEA:Ensembl.
DR GO; GO:0019828; F:aspartic-type endopeptidase inhibitor activity; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0072359; P:circulatory system development; IEA:Ensembl.
DR GO; GO:0030010; P:establishment of cell polarity; IEA:Ensembl.
DR GO; GO:0055111; P:ingression involved in gastrulation with mouth forming second; IEA:Ensembl.
DR GO; GO:0045199; P:maintenance of epithelial cell apical/basal polarity; IEA:Ensembl.
DR GO; GO:0001707; P:mesoderm formation; IEA:Ensembl.
DR GO; GO:0014028; P:notochord formation; IEA:Ensembl.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IEA:Ensembl.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; IEA:Ensembl.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IEA:Ensembl.
DR GO; GO:0010470; P:regulation of gastrulation; IEA:Ensembl.
DR GO; GO:0046549; P:retinal cone cell development; IEA:Ensembl.
DR GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
DR CDD; cd00054; EGF_CA; 11.
DR CDD; cd00110; LamG; 3.
DR Gene3D; 2.60.120.200; -; 3.
DR Gene3D; 2.10.25.10; Laminin; 14.
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; IPR001791; Laminin_G.
DR PANTHER; PTHR24044:SF489; NEUROGENIC LOCUS NOTCH HOMOLOG PROTEIN 4; 1.
DR PANTHER; PTHR24044; NOTCH LIGAND FAMILY MEMBER; 1.
DR Pfam; PF00008; EGF; 7.
DR Pfam; PF12661; hEGF; 4.
DR Pfam; PF02210; Laminin_G_2; 1.
DR PRINTS; PR00010; EGFBLOOD.
DR PRINTS; PR01983; NOTCH.
DR SMART; SM00181; EGF; 15.
DR SMART; SM00179; EGF_CA; 12.
DR SMART; SM00282; LamG; 3.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR SUPFAM; SSF57196; EGF/Laminin; 11.
DR PROSITE; PS00010; ASX_HYDROXYL; 7.
DR PROSITE; PS00022; EGF_1; 14.
DR PROSITE; PS01186; EGF_2; 8.
DR PROSITE; PS50026; EGF_3; 15.
DR PROSITE; PS01187; EGF_CA; 3.
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 Reference proteome {ECO:0000313|Proteomes:UP000233200};
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..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..1287
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014328909"
FT TRANSMEM 1227..1250
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 69..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..223
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 225..261
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 263..320
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 322..358
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 360..396
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 398..438
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 433..605
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 607..643
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 649..807
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 809..845
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 871..1056
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1058..1094
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1096..1132
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1136..1173
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1175..1211
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
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 251..260
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 310..319
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 348..357
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 386..395
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 428..437
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 633..642
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 835..844
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1084..1093
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1100..1110
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1122..1131
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1163..1172
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1201..1210
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1287 AA; 134446 MW; B92AC73A14917B82 CRC64;
MALARPGTRD PQPLAYVLLL LLLLWAPALS LLAGTVPSEP PSACASDPCG PGTECQATKS
GGYTCGPTEP RGCATQPCHH GALCVPQGPD PDGFRCYCVP GFQGPRCELD IDECASRPCH
HGATCRNLAD HYECHCPLGY AGVTCETEVD ECASAPCVHG GSCLDGVGSF RCVCAPGYGG
TRCQLDLDEC QSQPCAHGGM CHDLVNGFRC DCAGTGYEGT HCEQEVLECA SAPCAHNASC
LEGLGSFRCL CWPGYSGELC EVDEDECASS PCQHGGRCLQ RSDPALYGGV QATLPGAFSF
PHAAGFVCHC PPGFEGADCG VEVDECASRP CLNGGRCQDL PNGFQCHCPD GYAGPTCEAD
VDECLSDPCL HGGTCSDTVA GYLCRCPDTW GGHDCSVQLI GCQGHTCPLA ATCIPIFESG
VHSYVCHCPP GTHGPFCGQN TTFSVMAGSP IQASVPAGGS LGLALRFRTT LPAGTLATRS
DTKESLELAL VAATLQATLW SHGTTVLVLR LPDLGLNDGH WHQVEVVLHL ATLELRLWHE
GCPARLCVAS GPVALAPTAS ATPLPAGISS AQLGDVNFAG CLQDVRVDGH LLLPEDLGEN
VLLGCERREQ CQPLPCVHGG SCVDLWTHFR CNCPRPHRGP TCADEIPAAT FGLGGAPSSA
SFLLQELPGP NLTVSFLLRT REPAGLLLQF ANESAAGLTV FLSEGRIRAE VPGGPAVVLP
GRWDDGLRHL VTLSFGPDQL QDLGQHMHVG GRLLAADSQP WGGPFRGCLQ DLRLDGRHLP
FFPLPLDNSS QPSELGGRQS WNLTAGCVSE DMCSPDPCFN GGTCLVTWND FHCTCPANFT
GPTCAQQLWC PGQPCLPPAM CEEVPDGFVC VAEATFREGP PVAFSGHNAS SRRSLGGLSL
AFRTRDSEAW LLRAAAGTLA GVWLAVRNGS LAGAVRGGHG LSGAVLPIPG PRVADGAWHR
VRLAMERPAA APSRWLLWLD GAATPVALRG LAGDLGFLQG PGAAHVLLAE NFTGCLGRVA
LGGLPLPLAR PRPGVAPGAR EYFAAWPGTP DPILGCRGAP VCAPSPCLHG GACRDLFDAF
ACACDLGWEG PRCEAHVNPC HSAPCARGRC HAHPDGRFEC HCPPGFGGPR CRLPVSSKEC
NLNITCLDGS PCEGGSPAAN CSCLEGLAGQ RCQVPTVPCE TNPCLNGGTC RAAGGVSECI
CNARFSGQFC EVVKGVPLPL PFPLLEVAVP AACACLLLLL LGLLSGILAA RKRRQSEGTY
SPSQQEVAGA RLEMDSVLKV PPEERLI
//
