ID A0A0V1PHN0_9BILA Unreviewed; 734 AA.
AC A0A0V1PHN0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Frizzled-4 {ECO:0000313|EMBL:KRZ95703.1};
GN Name=fzd4 {ECO:0000313|EMBL:KRZ95703.1};
GN ORFNames=T08_8101 {ECO:0000313|EMBL:KRZ95703.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ95703.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ95703.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ95703.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRZ95703.1}.
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DR EMBL; JYDM01000011; KRZ95703.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1PHN0; -.
DR STRING; 92180.A0A0V1PHN0; -.
DR Proteomes; UP000054924; 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 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; 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 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:UP000054924};
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..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..734
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006884267"
FT TRANSMEM 335..356
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 368..386
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 435..454
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 466..485
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 505..528
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 593..613
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 633..653
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 45..166
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 334..531
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 186..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 50..111
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 58..104
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 95..133
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 122..163
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 126..150
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 734 AA; 83012 MW; C5A6317B484D8B0E CRC64;
MQQRQRRQLL FPLFFWSIVV QLLPAMCHQL PPPMVPLLTV IRQLENEHYC QPIEVTMCKD
LPYNFTSMPN FVGNEDQTEA ELQLTTFLPL IQIQCSSQLK FFLCSVYVPM CTDKVNIPIG
PCRPLCESVR RCCEPMLKQF GFPWPALLNC SKFHPENNAQ AMCMRGPSQD HNSVCFGDTH
VAVDESFALP PHTDPPTTVD DRRYPNNYPH DIYNKYNNHH YHHNHNGHAD TDRYDIQPHH
QNNYNHHNNI RHHNNNNNNI NYPYHHKGDD EKKEERSSPS PSYRSPPTGG GGGGQCNHLR
DNGRGFVRLN KTGQCVQLCR SNVLFDDEQK RNAEILMLVF AAACSVLSIA ALAFQFCKPR
VLLRHPDVPT LYICICYACA TVPYWIRAAG RDSLACTQYP GTVPTTTIIA GFGLQQIRCT
VVAILLYYFT MASHLWWIIL CLGWLLVGPL GYGVDKLQKR SFTFHCFVWF TALIKVIVVF
IMKTVDADEL TGMCFVGNQS RQGLQFLLVP QTIYLVVGLV PLTLGLVIKL RDFLQRGNPQ
QPGRPQPSHT TAQHFFSAPN ASASAFNSPL VQTPTPNPLS QPLLRPDGLT STGLLAAFYV
VPQACLIACY VYEYFNREDW LSDSTKNPSY ETFVVKIVAS FSYGIVCSGF LLWRRTCDRS
MLPRAPVKVQ QTALTAPIPF PGLCMPVMNP HSTSPSATAA ANVAAAQRVA LLKEQQYQRR
FHNLDDHYMA DCIL
//
