FRIZ_DROVI
ID FRIZ_DROVI Reviewed; 580 AA.
AC Q24760; B4LIE5;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 3.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Frizzled;
DE AltName: Full=Frizzled-1;
DE Short=dFz1;
DE Flags: Precursor;
GN Name=fz; ORFNames=GJ11377;
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Ovary;
RX PubMed=8770598; DOI=10.1093/genetics/142.1.205;
RA Jones K.H., Liu J., Adler P.N.;
RT "Molecular analysis of EMS-induced frizzled mutations in Drosophila
RT melanogaster.";
RL Genetics 142:205-215(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15010-1051.87;
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
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. Required to coordinate the cytoskeletons
CC of epidermal cells to produce a parallel array of cuticular hairs and
CC bristles.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB38383.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L43163; AAB38383.1; ALT_INIT; mRNA.
DR EMBL; L43340; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L43341; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L43342; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L43343; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L43344; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH940647; EDW70732.1; -; Genomic_DNA.
DR RefSeq; XP_002048390.2; XM_002048354.2.
DR AlphaFoldDB; Q24760; -.
DR SMR; Q24760; -.
DR STRING; 7244.FBpp0225794; -.
DR EnsemblMetazoa; FBtr0227302; FBpp0225794; FBgn0014841.
DR GeneID; 6624400; -.
DR KEGG; dvi:6624400; -.
DR eggNOG; KOG3577; Eukaryota.
DR HOGENOM; CLU_007873_2_1_1; -.
DR InParanoid; Q24760; -.
DR OMA; RSHGMMY; -.
DR OrthoDB; 330751at2759; -.
DR PhylomeDB; Q24760; -.
DR Proteomes; UP000008792; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
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 GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:UniProtKB.
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; IPR026552; FZD7.
DR InterPro; IPR017981; GPCR_2-like.
DR PANTHER; PTHR11309; PTHR11309; 1.
DR PANTHER; PTHR11309:SF31; PTHR11309:SF31; 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; Membrane; Receptor;
KW Reference proteome; Signal; Transducer; Transmembrane; Transmembrane helix;
KW Wnt signaling pathway.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..580
FT /note="Frizzled"
FT /id="PRO_0000224181"
FT TOPO_DOM 18..248
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..279
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 301..342
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..363
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 364..379
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 380..400
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 401..424
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 425..445
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 446..470
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 471..491
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 492..531
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 532..552
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 553..580
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 48..166
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT MOTIF 555..560
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 578..580
FT /note="PDZ-binding"
FT /evidence="ECO:0000250"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 53..114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 61..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 98..134
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 124..163
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 128..151
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT CONFLICT 11
FT /note="L -> M (in Ref. 1; AAB38383)"
FT /evidence="ECO:0000305"
FT CONFLICT 19..26
FT /note="QRYDQTPL -> TIDTV (in Ref. 1; AAB38383)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="S -> T (in Ref. 1; AAB38383)"
FT /evidence="ECO:0000305"
FT CONFLICT 482
FT /note="A -> G (in Ref. 1; AAB38383)"
FT /evidence="ECO:0000305"
FT CONFLICT 506
FT /note="D -> H (in Ref. 1; AAB38383)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 580 AA; 64709 MW; A70793856213CD13 CRC64;
MLLQPLLLLL LPALLQSAQR YDQTPLDASS YYRSDLTGSS ASSLDGFPHH NRCEPITISI
CKNIPYNMTI MPNLIGHTKQ EEAGLEVHQF APLVKIGCSA DLQLFLCSLY VPVCTILERP
IPPCRSLCES ARVCETLMKT YNFNWPENLE CSKFPVHGGE DLCVAENTTA SSSTPAPTRS
APKVTTRKHQ ISVDSPHRNI GFVCPVQLKT PLGMGYELKV GGKDLHDCGA PCHAMFFPER
ERTVLRYWVG SWAAICVASC LFTVLTFLID SSRFRYPERA IVFLAVCYLV VGCAYVAGLG
AGDSVSCREP FPPPVKLGRL QMMSTITQGH RQTTACTVLF MALYFCCMAA FAWWSCLAFA
WFLAAGLKWG HEAIENKSHL FHLVAWAVPA LQTISVLALA KVEGDILSGV CFVGQLDTHS
LGGFLILPLC IYLSIGALFL LAGFISLFRI RTVMKTDGKR TDKLERLMLR IGFFSGLFIL
PALGLLGCLF YEYYNFDEWM IQWHRDICKP FSIPCPAARP PGTPEARPIF QIYMVKYLCS
MLVGVTSSVW LYSSKTMVSW RNFVERLQGK EPRTRAQAYV
