FZD1_XENLA
ID FZD1_XENLA Reviewed; 559 AA.
AC Q9I9M5;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Frizzled-1;
DE Short=Fz-1;
DE Short=Xfz1;
DE Flags: Precursor;
GN Name=fzd1; Synonyms=fz1;
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], FUNCTION, COUPLING TO BETA-CATENIN PATHWAY,
RP SUBCELLULAR LOCATION, INTERACTION WITH WNT8, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=10969734; DOI=10.1046/j.1440-169x.2000.00517.x;
RA Brown J.D., Hallagan S.E., McGrew L.L., Miller J.R., Moon R.T.;
RT "The maternal Xenopus beta-catenin signaling pathway, activated by frizzled
RT homologs, induces goosecoid in a cell non-autonomous manner.";
RL Dev. Growth Differ. 42:347-357(2000).
CC -!- FUNCTION: Receptor for Wnt proteins. Functions in the canonical
CC Wnt/beta-catenin signaling pathway (PubMed:10969734). The canonical
CC Wnt/beta-catenin signaling pathway leads to the activation of
CC disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation
CC of beta-catenin and activation of Wnt target genes (PubMed:10969734). A
CC second signaling pathway involving PKC and calcium fluxes has been seen
CC for some family members, but it is not yet clear if it represents a
CC distinct pathway or if it can be integrated in the canonical pathway,
CC as PKC seems to be required for Wnt-mediated inactivation of GSK-3
CC kinase. Both pathways seem to involve interactions with G-proteins. May
CC be involved in transduction and intercellular transmission of polarity
CC information during tissue morphogenesis and/or in differentiated
CC tissues (Probable). {ECO:0000269|PubMed:10969734, ECO:0000305}.
CC -!- SUBUNIT: Interacts with wnt8. {ECO:0000305|PubMed:10969734}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10969734};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: In the embryo, expressed in the heart, pronephros
CC and otic vesicles. {ECO:0000269|PubMed:10969734}.
CC -!- DEVELOPMENTAL STAGE: Abundant in unfertilized eggs. Not detected in
CC late gastrula or early neurula stages. Expressed in mid-neurula stages
CC and maintained through tadpole stages. {ECO:0000269|PubMed:10969734}.
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; AF231711; AAF36979.1; -; mRNA.
DR RefSeq; NP_001079207.1; NM_001085738.1.
DR AlphaFoldDB; Q9I9M5; -.
DR SMR; Q9I9M5; -.
DR GeneID; 373817; -.
DR KEGG; xla:373817; -.
DR CTD; 373817; -.
DR Xenbase; XB-GENE-865493; fzd1.L.
DR OMA; RSHGMMY; -.
DR OrthoDB; 330751at2759; -.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 373817; Expressed in internal ear and 19 other tissues.
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:0042813; F:Wnt receptor activity; IEA:InterPro.
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; IPR026550; FZD1/2.
DR InterPro; IPR017981; GPCR_2-like.
DR PANTHER; PTHR11309; PTHR11309; 1.
DR PANTHER; PTHR11309:SF34; PTHR11309:SF34; 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 1: Evidence at protein level;
KW Cell membrane; Developmental protein; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Signal; Transducer; Transmembrane; Transmembrane helix;
KW Wnt signaling pathway.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..559
FT /note="Frizzled-1"
FT /id="PRO_0000012977"
FT TOPO_DOM 36..239
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 295..321
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 343..364
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..385
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 386..408
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..429
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 430..455
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 456..476
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 477..513
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 514..534
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 535..559
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 46..165
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT MOTIF 537..542
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 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 51..112
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 59..105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 96..133
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 122..162
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 126..150
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 559 AA; 62870 MW; 7953BCA9AC7C3B2D CRC64;
MKHSHLLQRC SAQLCTRGSS LILSLLLSVC LSVEGQYNGE KGISIPDHGY CQPISIPLCT
DIAYNQTIMP NLLGHTNQED AGLEVHQFYP LVKVQCSPEL KFFLCSIYAP VCTVLEQALP
PCRSLCDRAR QGCEALMNKF GFQWPESLRC EKFPINGAGE LCVGQNTTES GTPTPAVPET
WTSNSRTYYR DKFMCPRALK VPAYVNYHFL GEKDCGAPCE VGKVHGLMYF APEELNFARI
WIGIWSVLCC ASTLFTVLTY LVDMKRFSYP ERPIIFLSGC YTMVAIAYIA GFLLEDKVVC
NERFAEDGYK TVAQGTKKEG CTFLFMMLYF FSMASSIWWV ILSLTWFLAA GMKWGHEAIE
ANSQYFHLAA WAVPAIKTIT ILAVGQVDGD TLSGVCFVGI NNVDALRGFV LAPLFVYLFI
GTSFLLAGFV SLFRIRTIMK HDGTKTEKLE KLMVRIGIFS VLYTVPATIV IACYFYEQAF
REQWEKSWIS QSCKTYAIPC PSTGHPPMSP DFTVFMIKYL MTLIVGITSG FWIWSGKTLN
SWRKFYTRLT NSKQGETTV
