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   27-MAR-2024, entry version 149.
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   GlyCosmos; Q8BKG4; 3 sites, No reported glycans.
DR   GlyGen; Q8BKG4; 3 sites.
DR   PhosphoSitePlus; Q8BKG4; -.
DR   MaxQB; Q8BKG4; -.
DR   PaxDb; 10090-ENSMUSP00000114114; -.
DR   ProteomicsDB; 271655; -.
DR   Antibodypedia; 2928; 302 antibodies from 34 providers.
DR   DNASU; 93897; -.
DR   Ensembl; ENSMUST00000117102.4; ENSMUSP00000114114.3; ENSMUSG00000081683.6.
DR   GeneID; 93897; -.
DR   KEGG; mmu:93897; -.
DR   UCSC; uc008zsh.1; mouse.
DR   AGR; MGI:2136761; -.
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; VMCEQVK; -.
DR   OrthoDB; 5483535at2759; -.
DR   PhylomeDB; Q8BKG4; -.
DR   TreeFam; TF317907; -.
DR   BioGRID-ORCS; 93897; 1 hit in 77 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 144 other cell types or tissues.
DR   ExpressionAtlas; Q8BKG4; baseline and differential.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
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:0035567; P:non-canonical Wnt signaling pathway; ISO:MGI.
DR   GO; GO:0046330; P:positive regulation of JNK cascade; 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   CDD; cd15037; 7tmF_FZD10; 1.
DR   Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR015526; Frizzled/SFRP.
DR   InterPro; IPR000539; Frizzled/Smoothened_7TM.
DR   InterPro; IPR020067; Frizzled_dom.
DR   InterPro; IPR036790; Frizzled_dom_sf.
DR   InterPro; IPR017981; GPCR_2-like_7TM.
DR   PANTHER; PTHR11309; FRIZZLED; 1.
DR   PANTHER; PTHR11309:SF86; FRIZZLED-10; 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; Frizzled cysteine-rich domain; 1.
DR   PROSITE; PS50038; FZ; 1.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR   Genevisible; Q8BKG4; MM.
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
//