ID   A0A0B5CM78_OSCCA        Unreviewed;       585 AA.
AC   A0A0B5CM78;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   11-MAY-2016, entry version 9.
DE   SubName: Full=Frizzled B {ECO:0000313|EMBL:AJE25509.1};
OS   Oscarella carmela (Sponge).
OC   Eukaryota; Metazoa; Porifera; Homoscleromorpha; Homosclerophorida;
OC   Plakinidae; Oscarella.
OX   NCBI_TaxID=386100 {ECO:0000313|EMBL:AJE25509.1};
RN   [1] {ECO:0000313|EMBL:AJE25509.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25801223; DOI=10.1111/ede.12115;
RA   Schenkelaars Q., Fierro-Constain L., Renard E., Hill A.L.,
RA   Borchiellini C.;
RT   "Insights into Frizzled evolution and new perspectives.";
RL   Evol. Dev. 17:160-169(2015).
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo
CC       family. {ECO:0000256|SAAS:SAAS00543939}.
CC   -!- SIMILARITY: Contains FZ (frizzled) domain.
CC       {ECO:0000256|SAAS:SAAS00499052}.
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DR   EMBL; KM365034; AJE25509.1; -; mRNA.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.2000.10; -; 1.
DR   InterPro; IPR000539; Frizzled.
DR   InterPro; IPR015526; Frizzled/SFRP.
DR   InterPro; IPR020067; Frizzled_dom.
DR   InterPro; IPR017981; GPCR_2-like.
DR   PANTHER; PTHR11309; PTHR11309; 2.
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; SSF63501; 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|SAAS:SAAS00427069};
KW   Disulfide bond {ECO:0000256|SAAS:SAAS00499061};
KW   Membrane {ECO:0000256|SAAS:SAAS00499056, ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000256|SAAS:SAAS00499053};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00499066,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00499065,
KW   ECO:0000256|SAM:Phobius};
KW   Wnt signaling pathway {ECO:0000256|SAAS:SAAS00427143}.
FT   SIGNAL        1     23       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        24    585       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002100867.
FT   TRANSMEM    251    273       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    285    305       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    331    358       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    370    393       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    413    441       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    462    485       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    533    554       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       31    162       FZ (frizzled). {ECO:0000259|PROSITE:
FT                                PS50038}.
FT   DOMAIN      249    561       G_PROTEIN_RECEP_F2_4.
FT                                {ECO:0000259|PROSITE:PS50261}.
SQ   SEQUENCE   585 AA;  65354 MW;  F2C98CCD6C339CAC CRC64;
     MLLPALLFAA LAALFNSPVR VEAVDAVPDW VRRANCYEMN VDTCAGIGYN TTLLPNRFGH
     RTLPEAALEI STYVPLIQFK CSPELRFMAC ATFLPICTTD PVTNAKRTLP PCRQMCQRVQ
     TGCEPVVKRW LRGVAWPAAL SCDELPDEMD SLEDGTPPCF DNATQYAIDI PGGPDSGFNT
     TYPPLLPAEE GTEVTVNNSQ LLAKRDSCYR YMSGRKTEGF LCINCNYDEQ AKPGESAGYY
     FKQEDIAFAN YWVGIWAVLC FLSTLFTCLT FLIDRDRFHY PERPIIYLAV CYCVFSLGFI
     ARLFAGDERI ACDQTHGILI KADANHAGCT AIFMVLYFSM MAASVWWVVL TVTWFLAAGM
     KWSNEAIESL ALYYHLVAWI VPLIMTIVAL ILQKIDADEL TRVCFVGAQD VNAMAGFVVA
     PLALFLVVGT IFIIAGFAAL FRIREVIKSD RSRSGKLEKL MIRIGVFSVL YTVPATIVIG
     CYFYEYFARN LWSVHTAPQW NQLGDSSNKT FTFNGDVPST CPQDDSCTQA LPAVFYIKFL
     MSLIVGVTSG VWIWSSKTLA TWNSFISKSC SRLNRGKDRR NETTV
//