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Database: UniProt
Entry: A0A091JIT1_EGRGA
LinkDB: A0A091JIT1_EGRGA
Original site: A0A091JIT1_EGRGA 
ID   A0A091JIT1_EGRGA        Unreviewed;       525 AA.
AC   A0A091JIT1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   08-NOV-2023, entry version 36.
DE   SubName: Full=Frizzled-7 {ECO:0000313|EMBL:KFP19828.1};
DE   Flags: Fragment;
GN   ORFNames=Z169_07010 {ECO:0000313|EMBL:KFP19828.1};
OS   Egretta garzetta (Little egret).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Pelecaniformes; Ardeidae; Egretta.
OX   NCBI_TaxID=188379 {ECO:0000313|EMBL:KFP19828.1, ECO:0000313|Proteomes:UP000053119};
RN   [1] {ECO:0000313|EMBL:KFP19828.1, ECO:0000313|Proteomes:UP000053119}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_Z169 {ECO:0000313|EMBL:KFP19828.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Endosome
CC       membrane {ECO:0000256|ARBA:ARBA00004337}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004337}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo family.
CC       {ECO:0000256|ARBA:ARBA00008077}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00090}.
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DR   EMBL; KK502039; KFP19828.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091JIT1; -.
DR   STRING; 188379.A0A091JIT1; -.
DR   Proteomes; UP000053119; Unassembled WGS sequence.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR   CDD; cd07466; CRD_FZ7; 1.
DR   Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR042742; Frizzled-7_CRD.
DR   InterPro; IPR015526; Frizzled/SFRP.
DR   InterPro; IPR000539; Frizzled/Smoothened_7TM.
DR   InterPro; IPR020067; Frizzled_dom.
DR   InterPro; IPR036790; Frizzled_dom_sf.
DR   InterPro; IPR017981; GPCR_2-like_7TM.
DR   PANTHER; PTHR11309; FRIZZLED; 1.
DR   PANTHER; PTHR11309:SF31; FRIZZLED-7; 1.
DR   Pfam; PF01534; Frizzled; 1.
DR   Pfam; PF01392; Fz; 1.
DR   PRINTS; PR00489; FRIZZLED.
DR   SMART; SM00063; FRI; 1.
DR   SMART; SM01330; Frizzled; 1.
DR   SUPFAM; SSF63501; Frizzled cysteine-rich domain; 1.
DR   PROSITE; PS50038; FZ; 1.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00090}; Endosome {ECO:0000256|ARBA:ARBA00022753};
KW   G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053119};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        207..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        241..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        290..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        381..402
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        423..444
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        478..500
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..119
FT                   /note="FZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50038"
FT   DOMAIN          205..507
FT                   /note="G-protein coupled receptors family 2 profile 2"
FT                   /evidence="ECO:0000259|PROSITE:PS50261"
FT   DISULFID        5..66
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT   DISULFID        13..59
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT   DISULFID        80..104
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFP19828.1"
FT   NON_TER         525
FT                   /evidence="ECO:0000313|EMBL:KFP19828.1"
SQ   SEQUENCE   525 AA;  58778 MW;  93687EC7062E062A CRC64;
     DHGFCQPISI PLCTDIAYNQ TILPNLLGHT NQEDAGLEVH QFYPLVKVQC SAELKFFLCS
     MYAPVCTVLE QAIPPCRSLC ERARQGCEAL MNKFGFQWPE RLRCENFPVH GAGEICVGQN
     TSDAPPGPGG AAGRGATAHP TAGYLPDFLT PPQPPSGFSF SCPRQLKVPP YLGYRFLGER
     DCGAPCEPAR PNGLMYFKEA EVRFARLWVG VWSVLCCAST LFTVLTYLVD MRRFSYPERP
     IIFLSGCYFM VAVAYAAGFL LEERVVCLER FSEDGYRTVA QGTKKEGCTI LFMILYFFGM
     ASSIWWVILS LTWFLAAGMK WGHEAIEANS QYFHLAAWAV PAVKTITILA MGQVDGDVLS
     GVCYVGIYSV DSLRGFVLAP LFVYLFIGTS FLLAGFVSLF RIRTIMKHDG TKTEKLEKLM
     VRIGVFSVLY TVPATIVLAC YFYEQAFRGT WEKTWLLQTC KTYAVPCPSH FAPMSPDFTV
     FMIKYLMTMI VGITTGFWIW SGKTLQSWRR FYHRLSTGSK GETAV
//
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