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Database: UniProt
Entry: Q4H3F9_CIOIN
LinkDB: Q4H3F9_CIOIN
Original site: Q4H3F9_CIOIN 
ID   Q4H3F9_CIOIN            Unreviewed;       602 AA.
AC   Q4H3F9; A0A1W2VPM7;
DT   30-AUG-2005, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2005, sequence version 1.
DT   08-NOV-2023, entry version 93.
DE   RecName: Full=Frizzled-4 {ECO:0000256|ARBA:ARBA00018149};
GN   Name=Ci-Fz4 {ECO:0000313|EMBL:BAE06468.1};
OS   Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis).
OC   Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC   Cionidae; Ciona.
OX   NCBI_TaxID=7719 {ECO:0000313|EMBL:BAE06468.1};
RN   [1] {ECO:0000313|EMBL:BAE06468.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12736827; DOI=10.1007/s00427-003-0330-z;
RA   Satou Y., Satoh N.;
RT   "Genomewide surveys of developmentally relevant genes in Ciona
RT   intestinalis.";
RL   Dev. Genes Evol. 213:211-212(2003).
RN   [2] {ECO:0000313|EMBL:BAE06468.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15269171; DOI=10.1242/dev.01270;
RA   Imai K.S., Hino K., Yagi K., Satoh N., Satou Y.;
RT   "Gene expression profiles of transcription factors and signaling molecules
RT   in the ascidian embryo: towards a comprehensive understanding of gene
RT   networks.";
RL   Development 131:4047-4058(2004).
RN   [3] {ECO:0000313|EMBL:BAE06468.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Satou Y.;
RT   "Expressed genes in Ciona intestinalis.";
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
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   EMBL; AB210463; BAE06468.1; -; mRNA.
DR   RefSeq; NP_001071724.1; NM_001078256.1.
DR   AlphaFoldDB; Q4H3F9; -.
DR   GeneID; 100177470; -.
DR   KEGG; cin:100177470; -.
DR   CTD; 31659; -.
DR   OrthoDB; 5483535at2759; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR   CDD; cd07448; CRD_FZ4; 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; IPR041765; FZ4_CRD.
DR   InterPro; IPR017981; GPCR_2-like_7TM.
DR   PANTHER; PTHR11309; FRIZZLED; 1.
DR   PANTHER; PTHR11309:SF23; FRIZZLED-4; 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   2: Evidence at transcript level;
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   Receptor {ECO:0000313|EMBL:BAE06468.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        228..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        262..282
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        325..342
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        354..373
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        393..421
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        442..465
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        485..504
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          51..172
FT                   /note="FZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50038"
FT   DOMAIN          226..511
FT                   /note="G-protein coupled receptors family 2 profile 2"
FT                   /evidence="ECO:0000259|PROSITE:PS50261"
FT   DISULFID        56..117
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT   DISULFID        64..110
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT   DISULFID        101..139
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT   DISULFID        128..169
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT   DISULFID        132..156
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ   SEQUENCE   602 AA;  68763 MW;  8EDB1F73AB0E0BE4 CRC64;
     MEIRQTSTYF VAFRLVLTAL IAAEFVSSNR SYKLPTSKYD RRLPSDPIFD EDDNRCEPIQ
     IKMCQGLGYN ATRMPNRFGQ YRQTEAGIEL NSYQVLLQYN CSSELPMFLC AAFLPMCEPG
     LERTIGPCEG MCLSIKKLCL PALKSFGYPW PEILNCSNFP KDNKQNMMCM TGTHPHVKDE
     QPLIRPTKIK RSYCRQPQIS LQSNEGCGWR CGYQQGMFST EDKEFADLWM GVCSGVCFIS
     TVFTVLTFLI DASRFRYPER PIILIAMCYN IYSISYILRL LVGRNNISCQ RNTEGEMFLI
     KEGLGNTGCT VVFLLSYFFG MASYLWWVIL TLTWFLAAGM KWSHEAIERH SSYFHLVAWS
     IPSIKIVIIL ILRHVDGDEL TGMCYVGNQD MNALTGFVLA PLFTYLVIGT SFLLAGFFSL
     FRIKSYMEKE GSKTDKLERL MVKIGVFSVL YIVPASIVIG CYFYEHAVRR LWAQNRNVTP
     SATIYFLRIL MQLIIGVFTG FWVWSKKSMQ SWRQCSHSVL ALSPKHQLKQ TIDNRATCVT
     SQHKLPDVIT PQECIPTHCP HTGHPLFVAM PTSSGAFSRT YRFEGKIQEP LLLSNNRVEG
     IP
//
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