FZD10_MOUSE
ID FZD10_MOUSE Reviewed; 582 AA.
AC Q8BKG4;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Frizzled-10;
DE Short=Fz-10;
DE AltName: CD_antigen=CD350;
DE Flags: Precursor;
GN Name=Fzd10; Synonyms=Fz10;
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=CD-1;
RX PubMed=14758554; DOI=10.1007/s00427-004-0386-4;
RA Nunnally A.P., Parr B.A.;
RT "Analysis of Fz10 expression in mouse embryos.";
RL Dev. Genes Evol. 214:144-148(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
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 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). 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. A second signaling
CC pathway involving PKC and calcium fluxes has been seen for some family
CC members, but it is not yet clear if it represents a distinct pathway or
CC if it can be integrated in the canonical pathway, as PKC seems to be
CC required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways
CC seem to involve interactions with G-proteins. May be involved in
CC transduction and intercellular transmission of polarity information
CC during tissue morphogenesis and/or in differentiated tissues
CC (Probable). {ECO:0000269|PubMed:15923619}.
CC -!- SUBUNIT: Interacts with MYOC (By similarity). Interacts with WNT7B
CC (PubMed:15923619). {ECO:0000250|UniProtKB:Q9ULW2,
CC ECO:0000269|PubMed:15923619}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15923619};
CC Multi-pass membrane protein {ECO:0000255}.
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; AY509002; AAR92468.1; -; mRNA.
DR EMBL; AK052950; BAC35217.1; -; mRNA.
DR CCDS; CCDS51652.1; -.
DR RefSeq; NP_780493.1; NM_175284.3.
DR AlphaFoldDB; Q8BKG4; -.
DR SMR; Q8BKG4; -.
DR BioGRID; 220362; 2.
DR STRING; 10090.ENSMUSP00000114114; -.
DR GlyGen; Q8BKG4; 3 sites.
DR PhosphoSitePlus; Q8BKG4; -.
DR MaxQB; Q8BKG4; -.
DR PaxDb; Q8BKG4; -.
DR PRIDE; Q8BKG4; -.
DR ProteomicsDB; 271655; -.
DR Antibodypedia; 2928; 266 antibodies from 33 providers.
DR DNASU; 93897; -.
DR Ensembl; ENSMUST00000117102; ENSMUSP00000114114; ENSMUSG00000081683.
DR GeneID; 93897; -.
DR KEGG; mmu:93897; -.
DR UCSC; uc008zsh.1; mouse.
DR CTD; 11211; -.
DR MGI; MGI:2136761; Fzd10.
DR VEuPathDB; HostDB:ENSMUSG00000081683; -.
DR eggNOG; KOG3577; Eukaryota.
DR GeneTree; ENSGT00940000161861; -.
DR HOGENOM; CLU_007873_2_1_1; -.
DR InParanoid; Q8BKG4; -.
DR OMA; LMGHDDQ; -.
DR OrthoDB; 509772at2759; -.
DR PhylomeDB; Q8BKG4; -.
DR TreeFam; TF317907; -.
DR BioGRID-ORCS; 93897; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Fzd2; mouse.
DR PRO; PR:Q8BKG4; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8BKG4; protein.
DR Bgee; ENSMUSG00000081683; Expressed in manus and 143 other tissues.
DR ExpressionAtlas; Q8BKG4; baseline and differential.
DR Genevisible; Q8BKG4; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0042813; F:Wnt receptor activity; ISO:MGI.
DR GO; GO:0017147; F:Wnt-protein binding; IPI:MGI.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:0034260; P:negative regulation of GTPase activity; ISO:MGI.
DR GO; GO:0038031; P:non-canonical Wnt signaling pathway via JNK cascade; ISO:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
DR GO; GO:0043507; P:positive regulation of JUN kinase activity; ISO:MGI.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISO:MGI.
DR GO; GO:0016055; P:Wnt signaling pathway; IGI: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; IPR026549; FZD10.
DR InterPro; IPR017981; GPCR_2-like.
DR PANTHER; PTHR11309; PTHR11309; 1.
DR PANTHER; PTHR11309:SF86; PTHR11309:SF86; 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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..582
FT /note="Frizzled-10"
FT /id="PRO_0000013006"
FT TOPO_DOM 22..226
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248..263
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 285..312
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 334..352
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..373
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 374..394
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..415
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 416..444
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 445..465
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 466..503
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 504..524
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 525..582
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..151
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT REGION 153..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 527..532
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 580..582
FT /note="PDZ-binding"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 486
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 35..96
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 43..89
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 80..118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 107..148
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 111..135
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 582 AA; 65318 MW; 3ED4F5340B1505E0 CRC64;
MQHPGPRLWL VLQVMIGSCT AISSMDLERP GDGKCQPVEI PMCKDIGYNT TRMPNLMGHE
NQREAAIQLH EFAPLVEYGC HSHLRFFLCS LYAPMCTEQV STPIPACRVM CEQARLKCSP
IMEQFKFRWP DSLDCSKLPN KNDPNYLCME APNNGSDEPS RGSGMFPPLF RPQRPHSAQE
HPLKDGGPGR AGCDNPGKFH HVEKSESCAP LCTPGVDVYW SRDDKRFAVV WLAIWSVLCF
FSSAFTVLTF LIDPSRFRYP ERPIIFLSMC YCVYSVGYII RLFAGAESIA CDRDSGQLYV
IQEGLESTGC TLVFLVLYYF GMASSLWWVV LTLTWFLAAG KKWGHEAIEA NSSYFHLAAW
AIPAVKTILI LVMRRVAGDE LTGVCYVGSM DVNALTGFVL VPLACYLVIG TSFILSGFVA
LFHIRRVMKT GGENTDKLEK LMVRIGVFSL LYTVPATCVI ACYFYERLNM DYWKMLATQH
KCKMNNQTKT PDCLMTTSIP AVEVFMVKVS MLLVVGITSG VWVWTSKTLQ SWQHVCSRGL
KRKSRRKPAS VVTSAGIYKK AQHPQKPHLG KYELPAQPSA CV
