FZD8_CHICK
ID FZD8_CHICK Reviewed; 217 AA.
AC Q9IA03; Q9PTW0;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Frizzled-8;
DE Short=Fz-8;
DE Short=cFz-8;
DE Flags: Fragment;
GN Name=FZD8; Synonyms=FZ8;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-157.
RC TISSUE=Embryo;
RX PubMed=10781956; DOI=10.1016/s0925-4773(00)00263-x;
RA Stark M.R., Biggs J.J., Schoenwolf G.C., Rao M.S.;
RT "Characterization of avian frizzled genes in cranial placode development.";
RL Mech. Dev. 93:195-200(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 100-217.
RC TISSUE=Limb bud;
RX PubMed=10512196;
RA Nohno T., Kawakami Y., Wada N., Komaguchi C., Nishimatsu S.;
RT "Differential expression of the frizzled family involved in Wnt signaling
RT during chick limb development.";
RL Cell. Mol. Biol. 45:653-659(1999).
CC -!- FUNCTION: Receptor for Wnt proteins. Most of frizzled receptors are
CC coupled to the beta-catenin canonical signaling pathway, which leads to
CC the activation of disheveled proteins, inhibition of GSK-3 kinase,
CC nuclear accumulation of beta-catenin and activation of Wnt target
CC genes. A second signaling pathway involving PKC and calcium fluxes has
CC been seen for some family members, but it is not yet clear if it
CC represents a distinct pathway or if it can be integrated in the
CC canonical pathway, as PKC seems to be required for Wnt-mediated
CC inactivation of GSK-3 kinase. Both pathways seem to involve
CC interactions with G-proteins. May be involved in transduction and
CC intercellular transmission of polarity information during tissue
CC morphogenesis and/or in differentiated tissues.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Cell
CC membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed in prechordal plate between stages 3 and
CC 15.
CC -!- DOMAIN: The FZ domain is involved in binding with Wnt ligands.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo family.
CC {ECO:0000305}.
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DR EMBL; AF224318; AAF61098.1; -; mRNA.
DR EMBL; AB029453; BAA89403.1; -; mRNA.
DR AlphaFoldDB; Q9IA03; -.
DR SMR; Q9IA03; -.
DR PaxDb; Q9IA03; -.
DR VEuPathDB; HostDB:geneid_395571; -.
DR InParanoid; Q9IA03; -.
DR OrthoDB; 509772at2759; -.
DR PhylomeDB; Q9IA03; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0042813; F:Wnt receptor activity; IBA:GO_Central.
DR GO; GO:0017147; F:Wnt-protein binding; IBA:GO_Central.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR InterPro; IPR015526; Frizzled/SFRP.
DR InterPro; IPR000539; Frizzled/Smoothened_TM.
DR InterPro; IPR017981; GPCR_2-like.
DR PANTHER; PTHR11309; PTHR11309; 1.
DR Pfam; PF01534; Frizzled; 1.
DR PRINTS; PR00489; FRIZZLED.
DR SMART; SM01330; Frizzled; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Developmental protein; G-protein coupled receptor;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix; Wnt signaling pathway.
FT CHAIN <1..>217
FT /note="Frizzled-8"
FT /id="PRO_0000205978"
FT TOPO_DOM <1..26
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 27..47
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 48..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..113
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 135..160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..209
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..>217
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 120..121
FT /note="VV -> LI (in Ref. 1; AAF61098)"
FT /evidence="ECO:0000305"
FT CONFLICT 124..125
FT /note="FT -> AI (in Ref. 1; AAF61098)"
FT /evidence="ECO:0000305"
FT CONFLICT 129..157
FT /note="FLLAGFVSLFRIRSVIKQGGTKTDKLEKL -> YSDVSTGLTWRSGTASSVS
FT YPKQMPLSQV (in Ref. 1)"
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 217
SQ SEQUENCE 217 AA; 24044 MW; D3D399B42CA9F1D7 CRC64;
AGAAELQPEL AVAEHVRYES TGPALCTVVF LLVYFFGMAS SIWWVILSLT WFLAAGMKWG
NEAIAGYAQY FHLAAWLLPS VKSIAVLALS SVDGDPVAGI CYVGNQSLEN LRGFVLAPLV
VYLFTGSLFL LAGFVSLFRI RSVIKQGGTK TDKLEKLMIR IGIFTVLYTV PATIVIACYI
YEQHNREAWE QAQNCSCPGD PHRPKPDYAV FMLKYFM
