ID M3YRJ2_MUSPF Unreviewed; 1195 AA.
AC M3YRJ2;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 67.
DE SubName: Full=Crumbs cell polarity complex component 2 {ECO:0000313|Ensembl:ENSMPUP00000013951.1};
GN Name=CRB2 {ECO:0000313|Ensembl:ENSMPUP00000013951.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000013951.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000013951.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-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; AEYP01042816; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01042817; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 9669.ENSMPUP00000013951; -.
DR Ensembl; ENSMPUT00000014174.1; ENSMPUP00000013951.1; ENSMPUG00000014059.1.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00950000183101; -.
DR HOGENOM; CLU_000827_2_0_1; -.
DR InParanoid; M3YRJ2; -.
DR OMA; EPQGCAT; -.
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; 12.
DR CDD; cd00110; LamG; 2.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 2.10.25.10; Laminin; 13.
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; PTHR24049; CRUMBS FAMILY MEMBER; 1.
DR PANTHER; PTHR24049:SF19; PROTEIN CRUMBS HOMOLOG 2; 1.
DR Pfam; PF00008; EGF; 9.
DR Pfam; PF12661; hEGF; 3.
DR Pfam; PF02210; Laminin_G_2; 1.
DR PRINTS; PR00010; EGFBLOOD.
DR SMART; SM00181; EGF; 15.
DR SMART; SM00179; EGF_CA; 13.
DR SMART; SM00282; LamG; 2.
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; 9.
DR PROSITE; PS50026; EGF_3; 15.
DR PROSITE; PS01187; EGF_CA; 4.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
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}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1135..1158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 36..75
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 77..113
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 115..151
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 153..190
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 192..228
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 230..287
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 289..325
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 327..363
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 365..405
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 402..573
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 575..611
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 777..813
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 969..1005
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1007..1043
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1047..1084
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1085..1119
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 65..74
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 103..112
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 141..150
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 218..227
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 277..286
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 315..324
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 353..362
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 395..404
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 601..610
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 803..812
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 995..1004
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1011..1021
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1033..1042
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1074..1083
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1109..1118
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1195 AA; 125436 MW; 9A0B7A750F0CC391 CRC64;
GMVPSEAPSV CASAPCAPGT ACQAMENGSY TCGPTEPQGC ATQPCHHGAL CVPQGPDPHG
FRCYCVPGFQ GPRCELDIDE CASRPCHHGA TCHNLADRYE CRCPLGYAGV TCEEEVDECA
SAPCLHGGSC LDGVGSYRCV CAPGYGGASC QLDLDECQSQ PCAHGGECHD LVNGFRCDCA
DTGYEGARCE QEVLECESAP CANNASCLEG LGSFRCLCWP GYSGPQCEVD EDECESGPCQ
HGGQCLQRSD PALYGGAQAT FPGTFSFRHA AGFLCRCPPG FEGEECGVDV DECASQPCLH
GGRCQDLPNG FQCHCPDGYT GLACQEDVDE CLSEPCLHGG TCDDTVAGYV CRCPEAWGGH
DCSVQLTGCQ GHTCPPAATC IPIFKAEVHS YACHCPPGTH GPFCGQNTTF SVVAGSPVQT
SVPAGGPRGL ALRFRTTLPA GALAARTDAQ DSLELALAGG TLQATLWSHG NTTALTLKLP
DLALNDGHWH KVEVSLRLGV LELQLWHEDC PARLCVASSP VAPAPGTSEA PTPARFCSAQ
LGGTAFEGCL EDVYVDGHLL LPEDLGENVL LGCERREQCQ PPPCAHGGVC VDMWTRFLCK
CPRPYSGPTC ADEVPAATFG LGGTLSSASF LLRQLPGPNL TMSFLLRTRE PAGLLLQLAN
DSVAGLTVFL SEGQIQAEVL GSPTLVLPGR WDDGLRHLVT LSFGPDQLQG LGQQVHVGGR
LLPADAQPWG GPFRGCLQDL RLNDLHLPFF PLLLGNSSQP SELGSRQSRN LTMGCVSEDT
CSPDPCLNGG ICLVTWNDFH CTCPVNFTGP TCAQQLWCPG QPCLPPATCE EVPDGFVCVG
EATFREGPAA TFSGHNASSR LSLSGLSLAF RTRDSEAGLL RATAGAHAAV WLAIRNGXLR
GLAGDLGFLR GPGAARLLLA ENFTGCLGRV AVGGLPLPLA RPRPGAAPGS REHFSAWPGT
PVPRLGCHGA RVCVPSPCLH GGSCRDLFDA FACSCVPGWE GLRCDARADP CRSAPCARGR
CHSRPDGRFE CRCPPGFVGP RCRSPVLPEE CSLNFTCLNG GPCEGGPQGT NCSCQEGFGG
QRCQVPCKVN PCVNGGTCRA AGGLYECICS ARFSGRFCEV VKGLPLPLPF PLLEVAVPAA
CACLLLLLLG LLSGILAARK RRQSEGTYSP SQQEVAGARL EMDSVLKVPP EERLI
//