FZD7_MOUSE
ID FZD7_MOUSE Reviewed; 572 AA.
AC Q61090; G3X953;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Frizzled-7;
DE Short=Fz-7;
DE Short=mFz7;
DE Flags: Precursor;
GN Name=Fzd7;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8626800; DOI=10.1074/jbc.271.8.4468;
RA Wang Y., Macke J.P., Abella B.S., Andreasson K., Worley P., Gilbert D.J.,
RA Copeland N.G., Jenkins N.A., Nathans J.;
RT "A large family of putative transmembrane receptors homologous to the
RT product of the Drosophila tissue polarity gene frizzled.";
RL J. Biol. Chem. 271:4468-4476(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP COUPLING TO BETA-CATENIN PATHWAY.
RX PubMed=10395542; DOI=10.1016/s0960-9822(99)80310-8;
RA Sheldahl L.C., Park M., Malbon C.C., Moon R.T.;
RT "Protein kinase C is differentially stimulated by Wnt and Frizzled homologs
RT in a G-protein-dependent manner.";
RL Curr. Biol. 9:695-698(1999).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10097073; DOI=10.1073/pnas.96.7.3546;
RA Hsieh J.C., Rattner A., Smallwood P.M., Nathans J.;
RT "Biochemical characterization of Wnt-frizzled interactions using a soluble,
RT biologically active vertebrate Wnt protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:3546-3551(1999).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH DVL1.
RX PubMed=15353129; DOI=10.1038/sj.cr.7290232;
RA Pan W.J., Pang S.Z., Huang T., Guo H.Y., Wu D., Li L.;
RT "Characterization of function of three domains in dishevelled-1: DEP domain
RT is responsible for membrane translocation of dishevelled-1.";
RL Cell Res. 14:324-330(2004).
RN [7]
RP INTERACTION WITH MAGI3.
RX PubMed=15195140; DOI=10.1038/sj.onc.1207817;
RA Yao R., Natsume Y., Noda T.;
RT "MAGI-3 is involved in the regulation of the JNK signaling pathway as a
RT scaffold protein for frizzled and Ltap.";
RL Oncogene 23:6023-6030(2004).
CC -!- FUNCTION: Receptor for Wnt proteins. Most 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. Activation by WNT8 induces expression of
CC beta-catenin target genes. Following ligand activation, binds to
CC CCDC88C/DAPLE which displaces DVL1 from FZD7 and leads to inhibition of
CC canonical Wnt signaling, activation of G-proteins by CCDC88C and
CC triggering of non-canonical Wnt responses (By similarity). May be
CC involved in transduction and intercellular transmission of polarity
CC information during tissue morphogenesis and/or in differentiated
CC tissues. {ECO:0000250|UniProtKB:O75084, ECO:0000269|PubMed:10097073,
CC ECO:0000269|PubMed:15353129}.
CC -!- SUBUNIT: Interacts with MAGI3 (PubMed:15195140). Interacts with DVL1
CC (PubMed:15353129). Interacts with CCDC88C/DAPLE; the interaction
CC displaces DVL1 from FZD7, leading to inhibition of canonical Wnt
CC signaling and triggering of non-canonical Wnt responses (By
CC similarity). Interacts with MYOC (By similarity). Binds to SDCBP; this
CC interaction is increased by inositol trisphosphate (IP3) (By
CC similarity). Interacts with glypican GPC3 (By similarity).
CC {ECO:0000250|UniProtKB:O75084, ECO:0000269|PubMed:15195140,
CC ECO:0000269|PubMed:15353129}.
CC -!- INTERACTION:
CC Q61090; Q62108: Dlg4; NbExp=4; IntAct=EBI-8473104, EBI-300895;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10097073,
CC ECO:0000269|PubMed:15353129}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:10097073, ECO:0000269|PubMed:15353129}. Endosome
CC membrane {ECO:0000250|UniProtKB:O75084}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:O75084}. Note=Associated to the plasma membrane
CC in the presence of FZD7 and phosphatidylinositol 4,5-bisphosphate
CC (PIP2). Localized in recycling endosomes in other conditions.
CC {ECO:0000250|UniProtKB:O75084}.
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 -!- PTM: Ubiquitinated by ZNRF3, leading to its degradation by the
CC proteasome. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo family.
CC {ECO:0000305}.
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DR EMBL; U43320; AAC52432.1; -; mRNA.
DR EMBL; AC132574; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466548; EDL00127.1; -; Genomic_DNA.
DR CCDS; CCDS14985.1; -.
DR RefSeq; NP_032083.3; NM_008057.3.
DR AlphaFoldDB; Q61090; -.
DR SMR; Q61090; -.
DR BioGRID; 199780; 2.
DR CORUM; Q61090; -.
DR IntAct; Q61090; 4.
DR MINT; Q61090; -.
DR STRING; 10090.ENSMUSP00000109884; -.
DR GlyGen; Q61090; 2 sites.
DR iPTMnet; Q61090; -.
DR PhosphoSitePlus; Q61090; -.
DR MaxQB; Q61090; -.
DR PaxDb; Q61090; -.
DR PeptideAtlas; Q61090; -.
DR PRIDE; Q61090; -.
DR ProteomicsDB; 271656; -.
DR Antibodypedia; 19943; 519 antibodies from 39 providers.
DR DNASU; 14369; -.
DR Ensembl; ENSMUST00000114246; ENSMUSP00000109884; ENSMUSG00000041075.
DR GeneID; 14369; -.
DR KEGG; mmu:14369; -.
DR UCSC; uc011wlq.1; mouse.
DR CTD; 8324; -.
DR MGI; MGI:108570; Fzd7.
DR VEuPathDB; HostDB:ENSMUSG00000041075; -.
DR eggNOG; KOG3577; Eukaryota.
DR GeneTree; ENSGT00940000158239; -.
DR HOGENOM; CLU_007873_2_1_1; -.
DR InParanoid; Q61090; -.
DR OMA; SFSCPRQ; -.
DR OrthoDB; 330751at2759; -.
DR PhylomeDB; Q61090; -.
DR TreeFam; TF317907; -.
DR Reactome; R-MMU-4086400; PCP/CE pathway.
DR Reactome; R-MMU-4608870; Asymmetric localization of PCP proteins.
DR BioGRID-ORCS; 14369; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Fzd7; mouse.
DR PRO; PR:Q61090; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q61090; protein.
DR Bgee; ENSMUSG00000041075; Expressed in ureter smooth muscle and 265 other tissues.
DR Genevisible; Q61090; MM.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0055038; C:recycling endosome membrane; ISO:MGI.
DR GO; GO:0005109; F:frizzled binding; ISO:MGI.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISO:MGI.
DR GO; GO:0042813; F:Wnt receptor activity; IMP:MGI.
DR GO; GO:0017147; F:Wnt-protein binding; IPI:MGI.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IMP:MGI.
DR GO; GO:0060231; P:mesenchymal to epithelial transition; ISO:MGI.
DR GO; GO:2000726; P:negative regulation of cardiac muscle cell differentiation; ISO:MGI.
DR GO; GO:0010812; P:negative regulation of cell-substrate adhesion; IMP:BHF-UCL.
DR GO; GO:0042666; P:negative regulation of ectodermal cell fate specification; ISO:MGI.
DR GO; GO:0035567; P:non-canonical Wnt signaling pathway; IGI:MGI.
DR GO; GO:0038031; P:non-canonical Wnt signaling pathway via JNK cascade; ISO:MGI.
DR GO; GO:0060054; P:positive regulation of epithelial cell proliferation involved in wound healing; ISO:MGI.
DR GO; GO:0042327; P:positive regulation of phosphorylation; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0014834; P:skeletal muscle satellite cell maintenance involved in skeletal muscle regeneration; IMP:MGI.
DR GO; GO:0048103; P:somatic stem cell division; IMP:MGI.
DR GO; GO:0019827; P:stem cell population maintenance; ISO:MGI.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IMP:MGI.
DR GO; GO:0033077; P:T cell differentiation in thymus; IMP:MGI.
DR CDD; cd07466; CRD_FZ7; 1.
DR Gene3D; 1.10.2000.10; -; 1.
DR InterPro; IPR042742; Frizzled-7_CRD.
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 1: Evidence at protein level;
KW Cell membrane; Developmental protein; Disulfide bond; Endosome;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Signal; Transducer; Transmembrane; Transmembrane helix;
KW Ubl conjugation; Wnt signaling pathway.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..572
FT /note="Frizzled-7"
FT /id="PRO_0000012997"
FT TOPO_DOM 33..254
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 276..286
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..334
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..377
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..398
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 399..421
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 422..442
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 443..468
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 469..489
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 490..526
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 527..547
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 548..572
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 44..163
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT MOTIF 550..555
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 570..572
FT /note="PDZ-binding"
FT SITE 567
FT /note="Essential for SDCBP-mediated plasma membrane
FT phosphatidylinositol-4,5-bisphosphate recognition"
FT /evidence="ECO:0000250|UniProtKB:O75084"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 57..103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 94..131
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 120..160
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 124..148
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT CONFLICT 262
FT /note="C -> S (in Ref. 1; AAC52432)"
FT /evidence="ECO:0000305"
FT CONFLICT 516
FT /note="G -> R (in Ref. 1; AAC52432)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 572 AA; 63733 MW; D0B7DF37B9736183 CRC64;
MRGPGTAASH SPLGLCALVL ALLGALPTDT RAQPYHGEKG ISVPDHGFCQ PISIPLCTDI
AYNQTILPNL LGHTNQEDAG LEVHQFYPLV KVQCSPELRF FLCSMYAPVC TVLDQAIPPC
RSLCERARQG CEALMNKFGF QWPERLRCEN FPVHGAGEIC VGQNTSDGSG GAGGSPTAYP
TAPYLPDPPF TAMSPSDGRG RLSFPFSCPR QLKVPPYLGY RFLGERDCGA PCEPGRANGL
MYFKEEERRF ARLWVGVWSV LCCASTLFTV LTYLVDMRRF SYPERPIIFL SGCYFMVAVA
HVAGFLLEDR AVCVERFSDD GYRTVAQGTK KEGCTILFMV LYFFGMASSI WWVILSLTWF
LAAGMKWGHE AIEANSQYFH LAAWAVPAVK TITILAMGQV DGDLLSGVCY VGLSSVDALR
GFVLAPLFVY LFIGTSFLLA GFVSLFRIRT IMKHDGTKTE KLEKLMVRIG VFSVLYTVPA
TIVLACYFYE QAFREHWERT WLLQTCKSYA VPCPPGHFSP MSPDFTVFMI KYLMTMIVGI
TTGFWIWSGK TLQSWRRFYH RLSHSSKGET AV
