FZD1_MOUSE
ID FZD1_MOUSE Reviewed; 642 AA.
AC O70421; O08974; Q7TS82;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Frizzled-1;
DE Short=Fz-1;
DE Short=mFz1;
DE Flags: Precursor;
GN Name=Fzd1;
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=C57BL/6J; TISSUE=Embryo;
RX PubMed=11334716; DOI=10.1016/s0945-053x(00)00138-4;
RA Xu L., Tan L., Goldring M.B., Olsen B.R., Li Y.;
RT "Expression of frizzled genes in mouse costochondral chondrocytes.";
RL Matrix Biol. 20:147-151(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 302-376.
RC TISSUE=Prostate;
RA Johnson M.A., Greenberg N.M.;
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH WNT7B, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15923619; DOI=10.1128/mcb.25.12.5022-5030.2005;
RA Wang Z., Shu W., Lu M.M., Morrisey E.E.;
RT "Wnt7b activates canonical signaling in epithelial and vascular smooth
RT muscle cells through interactions with Fzd1, Fzd10, and LRP5.";
RL Mol. Cell. Biol. 25:5022-5030(2005).
CC -!- FUNCTION: Receptor for Wnt proteins (PubMed:15923619). Activated by
CC WNT7B (PubMed:15923619). Activated by WNT3A, WNT3, WNT1 and to a lesser
CC extent WNT2, but apparently not by WNT4, WNT5A, WNT5B, WNT6, WNT7A or
CC WNT7B (By similarity). Contradictory results showing activation by
CC WNT7B have been described for mouse (PubMed:15923619). Functions in the
CC canonical Wnt/beta-catenin signaling pathway (PubMed:15923619). The
CC canonical 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:15923619). 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:0000250|UniProtKB:Q9UP38,
CC ECO:0000269|PubMed:15923619, ECO:0000305}.
CC -!- SUBUNIT: Interacts with MYOC (By similarity). Interacts with WNT7B
CC (PubMed:15923619). {ECO:0000250|UniProtKB:Q9UP38,
CC ECO:0000269|PubMed:15923619}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15923619};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in chondrocytes.
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}.
CC -!- CAUTION: Activation by specific Wnt family members may depend on the
CC cells used for the experiment. Contradictory results have been reported
CC for activation by WNT7B in human and mouse. {ECO:0000305}.
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DR EMBL; AF054623; AAC12873.2; -; mRNA.
DR EMBL; AK143101; BAE25269.1; -; mRNA.
DR EMBL; CH466600; EDL14633.1; -; Genomic_DNA.
DR EMBL; BC053010; AAH53010.1; -; mRNA.
DR EMBL; AF005202; AAC01952.1; -; mRNA.
DR CCDS; CCDS19072.1; -.
DR RefSeq; NP_067432.2; NM_021457.3.
DR AlphaFoldDB; O70421; -.
DR SMR; O70421; -.
DR BioGRID; 199775; 3.
DR IntAct; O70421; 5.
DR MINT; O70421; -.
DR STRING; 10090.ENSMUSP00000058629; -.
DR GlyGen; O70421; 2 sites.
DR iPTMnet; O70421; -.
DR PhosphoSitePlus; O70421; -.
DR MaxQB; O70421; -.
DR PaxDb; O70421; -.
DR PeptideAtlas; O70421; -.
DR PRIDE; O70421; -.
DR ProteomicsDB; 273399; -.
DR Antibodypedia; 4574; 463 antibodies from 35 providers.
DR DNASU; 14362; -.
DR Ensembl; ENSMUST00000054294; ENSMUSP00000058629; ENSMUSG00000044674.
DR GeneID; 14362; -.
DR KEGG; mmu:14362; -.
DR UCSC; uc008wig.2; mouse.
DR CTD; 8321; -.
DR MGI; MGI:1196625; Fzd1.
DR VEuPathDB; HostDB:ENSMUSG00000044674; -.
DR eggNOG; KOG3577; Eukaryota.
DR GeneTree; ENSGT00940000162584; -.
DR HOGENOM; CLU_007873_2_1_1; -.
DR InParanoid; O70421; -.
DR OMA; RSHGMMY; -.
DR OrthoDB; 330751at2759; -.
DR PhylomeDB; O70421; -.
DR TreeFam; TF317907; -.
DR Reactome; R-MMU-4086400; PCP/CE 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 BioGRID-ORCS; 14362; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Fzd1; mouse.
DR PRO; PR:O70421; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; O70421; protein.
DR Bgee; ENSMUSG00000044674; Expressed in gastrula and 236 other tissues.
DR Genevisible; O70421; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0005886; C:plasma 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: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:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0042813; F:Wnt receptor activity; ISS:ParkinsonsUK-UCL.
DR GO; GO:0017147; F:Wnt-protein binding; IPI:MGI.
DR GO; GO:0036520; P:astrocyte-dopaminergic neuron signaling; IMP:ARUK-UCL.
DR GO; GO:0035425; P:autocrine signaling; ISO:MGI.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IMP:ARUK-UCL.
DR GO; GO:0044338; P:canonical Wnt signaling pathway involved in mesenchymal stem cell differentiation; ISO:MGI.
DR GO; GO:0044339; P:canonical Wnt signaling pathway involved in osteoblast differentiation; ISO:MGI.
DR GO; GO:0007267; P:cell-cell signaling; IDA:MGI.
DR GO; GO:0045446; P:endothelial cell differentiation; IDA:MGI.
DR GO; GO:0060022; P:hard palate 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:0030514; P:negative regulation of BMP signaling pathway; IDA:MGI.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:MGI.
DR GO; GO:1903204; P:negative regulation of oxidative stress-induced neuron death; IMP:ParkinsonsUK-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP: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:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:1905606; P:regulation of presynapse assembly; IDA:SynGO.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
DR GO; GO:0060412; P:ventricular septum morphogenesis; IGI:MGI.
DR GO; GO:0016055; P:Wnt signaling pathway; ISO:MGI.
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 Ubl conjugation; Wnt signaling pathway.
FT SIGNAL 1..68
FT /evidence="ECO:0000255"
FT CHAIN 69..642
FT /note="Frizzled-1"
FT /id="PRO_0000012974"
FT TOPO_DOM 69..317
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 339..349
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 371..397
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..418
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 419..440
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..461
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 462..484
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 485..505
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 506..531
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 532..552
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 553..593
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 594..614
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 615..642
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 106..225
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT REGION 26..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 620..625
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 640..642
FT /note="PDZ-binding"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 111..172
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 119..165
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 156..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 182..222
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 186..210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT CONFLICT 122
FT /note="I -> M (in Ref. 1; AAC12873)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="P -> G (in Ref. 1; AAC12873)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="R -> P (in Ref. 1; AAC12873)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="F -> S (in Ref. 1; AAC12873)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="K -> N (in Ref. 1; AAC12873)"
FT /evidence="ECO:0000305"
FT CONFLICT 474
FT /note="V -> L (in Ref. 1; AAC12873)"
FT /evidence="ECO:0000305"
FT CONFLICT 615
FT /note="W -> R (in Ref. 1; AAC12873)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 642 AA; 71127 MW; 7674583F819014E2 CRC64;
MAEEAAPSES RAAGRLSLEL CAEALPGRRE EVGHEDTASH RRPRADPRRW ASGLLLLLWL
LEAPLLLGVR AQAAGQVSGP GQQAPPPPQP QQSGQQYNGE RGISIPDHGY CQPISIPLCT
DIAYNQTIMP NLLGHTNQED AGLEVHQFYP LVKVQCSAEL KFFLCSMYAP VCTVLEQALP
PCRSLCERAR QGCEALMNKF GFQWPDTLKC EKFPVHGAGE LCVGQNTSDK GTPTPSLLPE
FWTSNPQHGG GGYRGGYPGG AGTVERGKFS CPRALRVPSY LNYHFLGEKD CGAPCEPTKV
YGLMYFGPEE LRFSRTWIGI WSVLCCASTL FTVLTYLVDM RRFSYPERPI IFLSGCYTAV
AVAYIAGFLL EDRVVCNDKF AEDGARTVAQ GTKKEGCTIL FMMLYFFSMA SSIWWVILSL
TWFLAAGMKW GHEAIEANSQ YFHLAAWAVP AIKTITILAL GQVDGDVLSG VCFVGLNNVD
ALRGFVLAPL FVYLFIGTSF LLAGFVSLFR IRTIMKHDGT KTEKLEKLMV RIGVFSVLYT
VPATIVIACY FYEQAFRDQW ERSWVAQSCK SYAIPCPHLQ GGGGVPPHPP MSPDFTVFMI
KYLMTLIVGI TSGFWIWSGK TLNSWRKFYT RLTNSKQGET TV
