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Database: UniProt
Entry: M3YRJ2_MUSPF
LinkDB: M3YRJ2_MUSPF
Original site: M3YRJ2_MUSPF 
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
//
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