ID A0A183W3H5_TRIRE Unreviewed; 818 AA.
AC A0A183W3H5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Frizzled-4 {ECO:0000313|WBParaSite:TRE_0000728601-mRNA-1};
GN ORFNames=TRE_LOCUS7128 {ECO:0000313|EMBL:VDQ03008.1};
OS Trichobilharzia regenti (Nasal bird schistosome).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Trichobilharzia.
OX NCBI_TaxID=157069 {ECO:0000313|WBParaSite:TRE_0000728601-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:TRE_0000728601-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDQ03008.1, ECO:0000313|Proteomes:UP000280995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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}.
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; UZAO01058099; VDQ03008.1; -; Genomic_DNA.
DR STRING; 157069.A0A183W3H5; -.
DR WBParaSite; TRE_0000728601-mRNA-1; TRE_0000728601-mRNA-1; TRE_0000728601.
DR Proteomes; UP000280995; Unassembled WGS sequence.
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; cd07066; CRD_FZ; 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; IPR017981; GPCR_2-like_7TM.
DR PANTHER; PTHR11309; FRIZZLED; 1.
DR PANTHER; PTHR11309:SF99; FRIZZLED-4; 1.
DR Pfam; PF01534; Frizzled; 2.
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 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:UP000280995};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 368..390
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 464..486
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 492..512
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 524..543
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 563..589
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 663..686
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 731..750
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 125..245
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 366..756
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 288..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 130..191
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 138..184
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 208..232
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 818 AA; 92368 MW; 5879C1CB452CD7E7 CRC64;
MMKIISEETI KLIVINVLIV VQQLIKNSQG IIQIQKSLSK NSDLYFHARD KGLLSFPNNN
LPQYVITRKL RNAAPSIFPS RQKDGEVSEH LKSFIESSQD GHVLNEVYSN RGDDAQQQEI
EEGVDDVNHC VPIHEPICHG LQYTHTWLPN SVGLTTQEEA AKRMNDYRSL INVGCSQYLK
FFLCTIYFPM CTPALNPPAA LQPCQNLCRY VQSKCEPIMK SFSFPWPIEL NCKSLPSDSG
MCIQPQNYDL DKNGQIISQG IPSEAHGAIA ELLPDFSEFL AHQSAQNQHL SGQNNQTNNN
HQNSPSLQDN QSELKNYHLL QKTRLHASKC SIVEVPLYSE QAHNNITCAR RCNVHLFYRP
IEKRFANVWM IVWAILCMGS CTLTIVTFIL NRTRFTYPER PIIYISACYF FYSAGFILHA
LIGRDMVACR NKVETISQSL LSSGASNDGT KKILRNIAHS KNNVSFLITS GHEGTWCTIV
FLILYYFSQA SYIWWVMLAI AWFLSASCKW GCEGIEAVSS ILHMLAWALP ALKTIIILIM
HRIDADELTG LCFVGYQNPT SLLTFILLPQ IIYLLLGILF LFIGFYSLIS VRSNLRQHSK
YLNNPSTATA TIKSNCCNSQ FKGNPVVTTS TSAAPTTVIN TSSPVIAFNN GNIRRLDKLM
IKICIFSMLY IIPTVCVIGV NMYNYINYPK WIKTLDQLDK QGNCLTEFGT TWSLINQCLG
DKQFPSVEAN MLQIFMSLVV GMTSGMWVWC NRKSSETWLN CMRGKRKELS QNNFNFHHHK
CGGALSGAGF VDNPNNNNNN NHLSKIDRKI QPINAADC
//
