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Database: UniProt
Entry: A0A3Q1BPZ5_AMPOC
LinkDB: A0A3Q1BPZ5_AMPOC
Original site: A0A3Q1BPZ5_AMPOC 
ID   A0A3Q1BPZ5_AMPOC        Unreviewed;       583 AA.
AC   A0A3Q1BPZ5;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Frizzled-8-like {ECO:0000313|Ensembl:ENSAOCP00000016395.1};
OS   Amphiprion ocellaris (Clown anemonefish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000016395.1, ECO:0000313|Proteomes:UP000257160};
RN   [1] {ECO:0000313|Ensembl:ENSAOCP00000016395.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo family.
CC       {ECO:0000256|ARBA:ARBA00008077}.
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DR   AlphaFoldDB; A0A3Q1BPZ5; -.
DR   STRING; 80972.ENSAOCP00000016395; -.
DR   Ensembl; ENSAOCT00000025361.1; ENSAOCP00000016395.1; ENSAOCG00000001558.1.
DR   GeneTree; ENSGT00940000161191; -.
DR   OMA; SWPERMA; -.
DR   Proteomes; UP000257160; Unplaced.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
DR   GO; GO:0060898; P:eye field cell fate commitment involved in camera-type eye formation; IEA:Ensembl.
DR   GO; GO:0021879; P:forebrain neuron differentiation; IEA:Ensembl.
DR   GO; GO:0021529; P:spinal cord oligodendrocyte cell differentiation; IEA:Ensembl.
DR   GO; GO:0021531; P:spinal cord radial glial cell differentiation; IEA:Ensembl.
DR   CDD; cd15250; 7tmF_FZD8; 1.
DR   CDD; cd07461; CRD_FZ8; 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; IPR015526; Frizzled/SFRP.
DR   InterPro; IPR000539; Frizzled/Smoothened_7TM.
DR   InterPro; IPR020067; Frizzled_dom.
DR   InterPro; IPR036790; Frizzled_dom_sf.
DR   InterPro; IPR041776; FZ8_CRD.
DR   InterPro; IPR017981; GPCR_2-like_7TM.
DR   PANTHER; PTHR11309; FRIZZLED; 1.
DR   PANTHER; PTHR11309:SF146; FRIZZLED 8A PROTEIN-RELATED; 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};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000257160};
KW   Signal {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..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..583
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018701703"
FT   TRANSMEM        242..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        277..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        317..350
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        370..389
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        409..435
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        456..479
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        506..528
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          25..146
FT                   /note="FZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50038"
FT   DOMAIN          241..535
FT                   /note="G-protein coupled receptors family 2 profile 2"
FT                   /evidence="ECO:0000259|PROSITE:PS50261"
FT   REGION          154..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        30..91
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT   DISULFID        38..84
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT   DISULFID        75..113
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT   DISULFID        102..143
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT   DISULFID        106..130
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ   SEQUENCE   583 AA;  65696 MW;  80EF2FFACFE45D4E CRC64;
     MEMDLFGIYL LLSLALLPRS SCTTAKEITC QEIAVPLCKG IGYNYTYMPN QFNHDTQDEA
     GLEVHQFWPL VEIQCSPDLK FFLCSMYTPI CLEDYKKPLP PCRSVCERAR AGCAPLMRQY
     GFPWPDRMKC DLLPVQGNPD TLCMDYNRTD STTVSPVLSK PTNHPGKGYN PPKNKPGRPG
     APGKYKPPAA PCEPGCKCLE PMVPVNTDRH PLYNRVKTGQ ISNCAIPCHN PYFTHDERAF
     TAFWIGLWSV LCFVSTFATV ATFLIDMERF KYPERPIIFL SACYMFVSIG YIVRLIAGHE
     KVACNREFDL EHIHYETTGP ALCTVVFLLI YFFGMASSIW WVILSLTWFL AAGMKWGNEA
     IASYSQYFHL AAWLIPSMKS IAVLALSSVD GDSVAGICYV GNQNLDNLRG FVLAPLVIYL
     FIGTMFLLAG FVSLFRIRSV IKQGGTKTDK LEKLMIRIGI FTVLYTVPAT IIVACYFYEQ
     HNRQSWEITH NCSNCLLERD RRVPDYAVFM LKYFMCLLVG ITSGVWIWSG KTLDSWRTFC
     TRCCWGSKGT SGSMYSDVST GLTWRSGTAS SVSCPKQMPL SQV
//
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