FZD5_XENLA
ID FZD5_XENLA Reviewed; 559 AA.
AC P58421;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Frizzled-5;
DE Short=Fz-5;
DE Short=Xfz5;
DE Flags: Precursor;
GN Name=fzd5; Synonyms=fz5;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11335120; DOI=10.1016/s0925-4773(01)00327-6;
RA Sumanas S., Ekker S.C.;
RT "Xenopus frizzled-5: a frizzled family member expressed exclusively in the
RT neural retina of the developing eye.";
RL Mech. Dev. 103:133-136(2001).
CC -!- FUNCTION: Receptor for Wnt proteins. Functions in the canonical
CC Wnt/beta-catenin signaling pathway. The canonical Wnt/beta-catenin
CC signaling pathway leads to the activation of disheveled proteins,
CC inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and
CC activation of Wnt target genes (By similarity). A second signaling
CC pathway involving PKC and calcium fluxes has been seen for some family
CC members, but it is not yet clear if it represents a distinct pathway or
CC if it can be integrated in the canonical pathway, as PKC seems to be
CC required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways
CC seem to involve interactions with G-proteins. May be involved in
CC transduction and intercellular transmission of polarity information
CC during tissue morphogenesis and/or in differentiated tissues
CC (Probable). {ECO:0000250|UniProtKB:Q9EQD0, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9EQD0};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9EQD0}. Golgi
CC apparatus membrane {ECO:0000250|UniProtKB:Q9EQD0}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:Q9EQD0}. Note=Localized at the plasma
CC membrane and also found at the Golgi. {ECO:0000250|UniProtKB:Q9EQD0}.
CC -!- TISSUE SPECIFICITY: Expressed in retina. {ECO:0000269|PubMed:11335120}.
CC -!- DEVELOPMENTAL STAGE: First detected at the late neurula stage in
CC retinal primordia. Throughout the tailbud stage, expressed exclusively
CC in the neural retina within the optic vesicles. During tadpole stage,
CC expression becomes restricted to the ciliary marginal zone.
CC {ECO:0000269|PubMed:11335120}.
CC -!- DOMAIN: Lys-Thr-X-X-X-Trp motif interacts with the PDZ domain of Dvl
CC (Disheveled) family members and is involved in the activation of the
CC Wnt/beta-catenin signaling pathway. {ECO:0000250}.
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; AF300716; AAK51688.1; -; mRNA.
DR RefSeq; NP_001079217.1; NM_001085748.1.
DR AlphaFoldDB; P58421; -.
DR SMR; P58421; -.
DR GeneID; 373834; -.
DR KEGG; xla:373834; -.
DR CTD; 373834; -.
DR Xenbase; XB-GENE-865299; fzd5.S.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR Bgee; 373834; Expressed in intestine and 15 other tissues.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0043010; P:camera-type eye development; TAS:AgBase.
DR GO; GO:0048666; P:neuron development; TAS:AgBase.
DR GO; GO:0045595; P:regulation of cell differentiation; TAS:AgBase.
DR GO; GO:0042127; P:regulation of cell population proliferation; TAS:AgBase.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 1.10.2000.10; -; 1.
DR InterPro; IPR015526; Frizzled/SFRP.
DR InterPro; IPR000539; Frizzled/Smoothened_TM.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR017981; GPCR_2-like.
DR PANTHER; PTHR11309; PTHR11309; 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; SSF63501; 1.
DR PROSITE; PS50038; FZ; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Developmental protein; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Golgi apparatus; Membrane;
KW Receptor; Reference proteome; Signal; Transducer; Transmembrane;
KW Transmembrane helix; Wnt signaling pathway.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..559
FT /note="Frizzled-5"
FT /id="PRO_0000012992"
FT TOPO_DOM 27..220
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 242..257
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..301
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..343
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 365..387
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..408
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 409..434
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 435..455
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 456..483
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 484..504
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 505..559
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..149
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT MOTIF 507..512
FT /note="Lys-Thr-X-X-X-Trp motif, mediates interaction with
FT the PDZ domain of Dvl family members"
FT /evidence="ECO:0000250"
FT MOTIF 557..559
FT /note="PDZ-binding"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 33..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 41..87
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 78..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 105..146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 109..133
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 559 AA; 63518 MW; 581EB243FCB954B7 CRC64;
MGSFRSGVFA LSFVVLLLDY FAPAQAASKA IVCQEITVPM CKGIGYNHTY MPNQFNHDTQ
DEAGMEVHQF WPLVVIQCSL DLKFFLCSMY TPICLPDYRK PLPPCRSVCE RAKAGCSPLM
RKYGFAWPER MNCDRLPEHG DPDTLCMYYN WTETTTTLPP THPPKVKTPT SDCDGVCKCR
EPFVSITRES HPLYNRIKTG QVPNCAMPCF QPYFTQDEKM FVTFWIGLWS ILCFISTFTT
VATFLIDMER FRYPERPIIF LSACYLFVSI GYVVRLIVGH ENVACNKDHI HYETTGPALC
TIVFLLIYFF GMASSIWWVI LTFTWFLAAG MKWGNEAIAS YSQYFHMAAW LIPSVKSIAV
LALSSVDGDP VAGICYVGNQ NLDNLRGFVL APLVVYLFSG TMFLLAGFVS LFRIRSVIKQ
GGTKTDKLEK LMIRIGIFSV LYTVPATIVV ACYIYEQHYR EHWEKTHNCS CPGDKQRYRP
DYAVFMLKYL MCLVVGITSG VWIWSGKTLE SWKRFTGRCC RNSKPINASA YSEASRALTP
RTGLSNLTLP HKQVPLSHV
