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Database: UniProt
Entry: A0A8C3C6R2_CAIMO
LinkDB: A0A8C3C6R2_CAIMO
Original site: A0A8C3C6R2_CAIMO 
ID   A0A8C3C6R2_CAIMO        Unreviewed;      1045 AA.
AC   A0A8C3C6R2;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   28-JAN-2026, entry version 19.
DE   SubName: Full=Multiple EGF like domains 11 {ECO:0000313|Ensembl:ENSCMMP00000015990.1};
OS   Cairina moschata (Muscovy duck).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC   Anatinae; Cairina.
OX   NCBI_TaxID=8855 {ECO:0000313|Ensembl:ENSCMMP00000015990.1, ECO:0000313|Proteomes:UP000694556};
RN   [1] {ECO:0000313|Ensembl:ENSCMMP00000015990.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Vignal A., Thebault N., Warren W.C.;
RT   "Common duck and Muscovy duck high density SNP chip.";
RL   Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCMMP00000015990.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [3] {ECO:0000313|Ensembl:ENSCMMP00000015990.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2025) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162};
CC       Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}.
CC   -!- SIMILARITY: Belongs to the MEGF family.
CC       {ECO:0000256|ARBA:ARBA00038377}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   AlphaFoldDB; A0A8C3C6R2; -.
DR   Ensembl; ENSCMMT00000017574.1; ENSCMMP00000015990.1; ENSCMMG00000009695.1.
DR   Proteomes; UP000694556; Chromosome 11.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   FunFam; 2.170.300.10:FF:000007; multiple epidermal growth factor-like domains protein 10; 1.
DR   FunFam; 2.10.25.10:FF:000114; Multiple epidermal growth factor-like domains protein 11; 1.
DR   FunFam; 2.170.300.10:FF:000005; multiple epidermal growth factor-like domains protein 11; 1.
DR   FunFam; 2.170.300.10:FF:000006; Multiple epidermal growth factor-like domains protein 11; 1.
DR   FunFam; 2.170.300.10:FF:000021; Platelet endothelial aggregation receptor 1; 1.
DR   FunFam; 2.170.300.10:FF:000041; Tyrosine protein kinase receptor tie-1, putative; 1.
DR   Gene3D; 2.10.25.10; Laminin; 1.
DR   Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 5.
DR   InterPro; IPR000742; EGF.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR057138; EGF_PEAR1L-like.
DR   InterPro; IPR011489; EMI_domain.
DR   InterPro; IPR002049; LE_dom.
DR   InterPro; IPR052485; MEGF_diff_regulators.
DR   PANTHER; PTHR24052; DELTA-RELATED; 1.
DR   PANTHER; PTHR24052:SF13; MULTIPLE EGF LIKE DOMAINS 11; 1.
DR   Pfam; PF00053; EGF_laminin; 3.
DR   Pfam; PF23301; EGF_PEAR1L; 1.
DR   Pfam; PF23106; EGF_Teneurin; 1.
DR   Pfam; PF12661; hEGF; 6.
DR   PRINTS; PR00011; EGFLAMININ.
DR   SMART; SM00181; EGF; 16.
DR   SMART; SM00180; EGF_Lam; 14.
DR   PROSITE; PS00022; EGF_1; 13.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS50026; EGF_3; 7.
DR   PROSITE; PS50027; EGF_LAM_2; 1.
DR   PROSITE; PS51041; EMI; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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   Laminin EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00460};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000694556};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..1045
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5034249366"
FT   TRANSMEM        808..831
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..86
FT                   /note="EMI"
FT                   /evidence="ECO:0000259|PROSITE:PS51041"
FT   DOMAIN          128..158
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          166..201
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          269..304
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          358..393
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          444..479
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          530..565
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          709..739
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          712..753
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DISULFID        148..157
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        191..200
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        294..303
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        383..392
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        469..478
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        555..564
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        729..738
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   1045 AA;  113723 MW;  D293D9ED67D9AB00 CRC64;
     TRPKLFMLHL SLSFFAPSYA VTVQESYAHP FDQIYYTRCT DILNWFKCTR HRISYKTAYR
     RGLRTMYRRR SQCCPGYYES GDYCIPLCTE ECVHGRCVSP DTCHCEPGWG GTDCSSGCDS
     DHWGPHCSNR CQCQNEALCN PITGACVCAD GYQGWRCEEL CDPGSYGKGC QFQCQCHNGA
     TCDHETGECH CAPGYTGVFC EERCPPGSHG AQCELRCPCQ NGGVCHHITG ECSCPPGWMV
     RRLFMLIHHL ELGGLVCAQC QEECPIGTYG FQCTQRCDCQ NGAKCYHVNG ACMCDPGFKG
     IHCQERMCPE GLYGLKCNKR CPCNITNTLS CHPLSGECSC KAGWAGLYCN ETCPPGYYGE
     GCQLTCSCQN GADCDSITGK CTCAPGYMGD DCTITCMEGT YGTNCSSVCN CKNDGTCSPV
     DGLCICKEGW QGMDCSIPCS SGSWGLNCNQ TCYCTNGAAC RPADGFCLCS PGWQGEYCDQ
     PCPDGTYGLN CSERCDCSHA DGCDPVTGYC CCLAGWTGIH CDNICSQGRW GPNCSISCNC
     ENGGSCSPED GTCDCAPGYR GPLCQRICPP GFHGHHCSQP CPQCVHSSGP CHHVSGHCDC
     LPGFFGALCN QVCPSGKYGK NCDEVCQCTE NGTCNPIDGS CQCFPGWIGK DCSQTCPTGF
     WGPDCFHSCN CHNGAMCSPY DGECRCTHGW TGLYCTQRCP TAFYGKNCAN VCQCQNGADC
     DHITGQCTCR TGFTGKQCEQ KCSPGTFGYG CKQLCECMNN ATCDHVTGTC YCSPGFKGIR
     CDQAALMMEE LNPYTKISPA LGSERHSVGA IIGIIILLLI IMVLLALFVW YRRKQKEKGH
     DMPSVSYTPA MRMTNTDYSL SDISQGSGSV HCFSNPSYHT LSCGVTSRFF TSNVDGNSSS
     KVDIIPSHSN SPTPSCFADY MKESVCSSST CSLNSSENPY ATIKDPPILT CKHSESSYVE
     MKSPGHRESP YSEMPTSSTA NKNIYEVEPT VSVVQDARGR SASYLQNPYD LPRNSHIPSH
     YDLLPVRHSP TKREDNPFLC CRMLT
//
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