FZD2_MOUSE
ID FZD2_MOUSE Reviewed; 570 AA.
AC Q9JIP6; Q810M0; Q9JIP5; Q9WUJ2;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Frizzled-2;
DE Short=Fz-2;
DE Short=mFz2;
DE AltName: Full=Frizzled-10;
DE Short=Fz-10;
DE Short=mFz10;
DE Flags: Precursor;
GN Name=Fzd2; Synonyms=Fzd10;
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].
RC STRAIN=ICR; TISSUE=Fetal intestine;
RX PubMed=10903145; DOI=10.1042/bj3490829;
RA Malik T.H., Shivdasani R.A.;
RT "Structure and expression of a novel frizzled gene isolated from the
RT developing mouse gut.";
RL Biochem. J. 349:829-834(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Limb;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 172-312.
RC STRAIN=C57BL/6J; TISSUE=Prostate;
RA Johnson M.A., Greenberg N.M.;
RT "Characterization of the wnt signaling cascade in the TRAMP transgenic
RT mouse model of prostate cancer.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
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 genes
CC (By similarity). A second signaling pathway involving PKC and calcium
CC fluxes has been seen for some family members, but it is not yet clear
CC if it 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 {ECO:0000250|UniProtKB:Q14332}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Cell
CC membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in embryonic and adult heart, lung,
CC chondrocytes and brain. Also expressed in the developing
CC gastrointestinal tract (strongest in foregut), much weaker expression
CC in the adult. No expression in fetal liver and adult spleen. Up-
CC regulated in esophageal squamous cell carcinomas.
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; AF206321; AAF74056.1; -; mRNA.
DR EMBL; AF206322; AAF74057.1; -; mRNA.
DR EMBL; BC049774; AAH49774.2; -; mRNA.
DR EMBL; BC055727; AAH55727.1; -; mRNA.
DR EMBL; AF139183; AAD28286.1; -; mRNA.
DR CCDS; CCDS25501.1; -.
DR RefSeq; NP_065256.1; NM_020510.2.
DR AlphaFoldDB; Q9JIP6; -.
DR SMR; Q9JIP6; -.
DR BioGRID; 208235; 1.
DR IntAct; Q9JIP6; 1.
DR MINT; Q9JIP6; -.
DR STRING; 10090.ENSMUSP00000091463; -.
DR GlyGen; Q9JIP6; 2 sites.
DR iPTMnet; Q9JIP6; -.
DR PhosphoSitePlus; Q9JIP6; -.
DR MaxQB; Q9JIP6; -.
DR PaxDb; Q9JIP6; -.
DR PeptideAtlas; Q9JIP6; -.
DR PRIDE; Q9JIP6; -.
DR ProteomicsDB; 272924; -.
DR Antibodypedia; 17503; 358 antibodies from 37 providers.
DR DNASU; 57265; -.
DR Ensembl; ENSMUST00000057893; ENSMUSP00000091463; ENSMUSG00000050288.
DR GeneID; 57265; -.
DR KEGG; mmu:57265; -.
DR UCSC; uc011yft.1; mouse.
DR CTD; 2535; -.
DR MGI; MGI:1888513; Fzd2.
DR VEuPathDB; HostDB:ENSMUSG00000050288; -.
DR eggNOG; KOG3577; Eukaryota.
DR GeneTree; ENSGT00940000161812; -.
DR HOGENOM; CLU_007873_2_1_1; -.
DR InParanoid; Q9JIP6; -.
DR OMA; EIHFSRI; -.
DR OrthoDB; 330751at2759; -.
DR PhylomeDB; Q9JIP6; -.
DR TreeFam; TF317907; -.
DR Reactome; R-MMU-4086398; Ca2+ pathway.
DR Reactome; R-MMU-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-MMU-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR Reactome; R-MMU-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
DR BioGRID-ORCS; 57265; 1 hit in 76 CRISPR screens.
DR ChiTaRS; Fzd2; mouse.
DR PRO; PR:Q9JIP6; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9JIP6; protein.
DR Bgee; ENSMUSG00000050288; Expressed in metanephric mesenchyme and 244 other tissues.
DR Genevisible; Q9JIP6; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0042813; F:Wnt receptor activity; IDA:MGI.
DR GO; GO:0017147; F:Wnt-protein binding; IBA:GO_Central.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:0007267; P:cell-cell signaling; IDA:MGI.
DR GO; GO:0090103; P:cochlea morphogenesis; IGI:MGI.
DR GO; GO:0045446; P:endothelial cell differentiation; IDA:MGI.
DR GO; GO:0007199; P:G protein-coupled receptor signaling pathway coupled to cGMP nucleotide second messenger; ISO:MGI.
DR GO; GO:0060022; P:hard palate development; IMP:MGI.
DR GO; GO:0060119; P:inner ear receptor cell development; IGI:MGI.
DR GO; GO:0003149; P:membranous septum morphogenesis; IGI:MGI.
DR GO; GO:0003150; P:muscular septum morphogenesis; IGI:MGI.
DR GO; GO:0003151; P:outflow tract morphogenesis; IGI:MGI.
DR GO; GO:0090179; P:planar cell polarity pathway involved in neural tube closure; IGI:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0007608; P:sensory perception of smell; IMP:MGI.
DR GO; GO:0060412; P:ventricular septum morphogenesis; IGI:MGI.
DR GO; GO:0016055; P:Wnt signaling pathway; ISO:MGI.
DR GO; GO:0007223; P:Wnt signaling pathway, calcium modulating pathway; ISO:MGI.
DR CDD; cd07464; CRD_FZ2; 1.
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; IPR041778; FZ2_CRD.
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 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 Ubl conjugation; Wnt signaling pathway.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..570
FT /note="Frizzled-2"
FT /id="PRO_0000012979"
FT TOPO_DOM 29..252
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 274..284
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 306..332
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..353
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 354..375
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 376..396
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 397..419
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..440
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 441..466
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 467..487
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 488..524
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 525..545
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 546..570
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 39..158
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT REGION 166..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 548..553
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 568..570
FT /note="PDZ-binding"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 44..105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 52..98
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 89..126
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 115..155
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 119..143
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT CONFLICT 307
FT /note="E -> K (in Ref. 3; AAD28286)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 570 AA; 64059 MW; 79EE7F71D10FC51A CRC64;
MRARSALPRS ALPRLLLPLL LLPAAGPAQF HGEKGISIPD HGFCQPISIP LCTDIAYNQT
IMPNLLGHTN QEDAGLEVHQ FYPLVKVQCS PELRFFLCSM YAPVCTVLEQ AIPPCRSICE
RARQGCEALM NKFGFQWPER LRCEHFPRHG AEQICVGQNH SEDGAPALLT TAPPSGLQPG
AGGTPGGPGG GGSPPRYATL EHPFHCPRVL KVPSYLSYKF LGERDCAAPC EPARPDGSMF
FSQEETRFAR LWILTWSVLC CASTFFTVTT YLVDMQRFRY PERPIIFLSG CYTMVSVAYI
AGFVLQERVV CNERFSEDGY RTVVQGTKKE GCTILFMMLY FFSMASSIWW VILSLTWFLA
AGMKWGHEAI EANSQYFHLA AWAVPAVKTI TILAMGQIDG DLLSGVCFVG LNSLDPLRGF
VLAPLFVYLF IGTSFLLAGF VSLFRIRTIM KHDGTKTEKL ERLMVRIGVF SVLYTVPATI
VIACYFYEQA FREHWERSWV SQHCKSLAIP CPAHYTPRMS PDFTVYMIKY LMTLIVGITS
GFWIWSGKTL HSWRKFYTRL TNSRHGETTV
