FZD10_HUMAN
ID FZD10_HUMAN Reviewed; 581 AA.
AC Q9ULW2;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Frizzled-10;
DE Short=Fz-10;
DE Short=hFz10;
DE AltName: Full=FzE7;
DE AltName: CD_antigen=CD350;
DE Flags: Precursor;
GN Name=FZD10;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Fetal kidney, and Fetal lung;
RX PubMed=10448064; DOI=10.1006/bbrc.1999.1161;
RA Koike J., Takagi A., Miwa T., Hirai M., Terada M., Katoh M.;
RT "Molecular cloning of Frizzled-10, a novel member of the Frizzled gene
RT family.";
RL Biochem. Biophys. Res. Commun. 262:39-43(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 265-325.
RC TISSUE=Esophageal carcinoma;
RX PubMed=9707618; DOI=10.1073/pnas.95.17.10164;
RA Tanaka S., Akiyoshi T., Mori M., Wands J.R., Sugimachi K.;
RT "A novel frizzled gene identified in human esophageal carcinoma mediates
RT APC/beta-catenin signals.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:10164-10169(1998).
RN [4]
RP INTERACTION WITH MYOC, AND SUBCELLULAR LOCATION.
RX PubMed=19188438; DOI=10.1128/mcb.01274-08;
RA Kwon H.S., Lee H.S., Ji Y., Rubin J.S., Tomarev S.I.;
RT "Myocilin is a modulator of Wnt signaling.";
RL Mol. Cell. Biol. 29:2139-2154(2009).
CC -!- FUNCTION: Receptor for Wnt proteins. Functions in the canonical
CC Wnt/beta-catenin signaling pathway (By similarity). The canonical
CC 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:0000250|UniProtKB:Q8BKG4, ECO:0000305}.
CC -!- SUBUNIT: Interacts with WNT7B (By similarity). Interacts with MYOC
CC (PubMed:19188438). {ECO:0000250|UniProtKB:Q8BKG4,
CC ECO:0000269|PubMed:19188438}.
CC -!- INTERACTION:
CC Q9ULW2; O95273: CCNDBP1; NbExp=3; IntAct=EBI-8803802, EBI-748961;
CC Q9ULW2; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-8803802, EBI-3867333;
CC Q9ULW2; Q9Y5L2: HILPDA; NbExp=2; IntAct=EBI-8803802, EBI-8803836;
CC Q9ULW2; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-8803802, EBI-11959885;
CC Q9ULW2; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-8803802, EBI-10171774;
CC Q9ULW2; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-8803802, EBI-22310682;
CC Q9ULW2; P07237: P4HB; NbExp=3; IntAct=EBI-8803802, EBI-395883;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:19188438};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highest levels in the placenta and fetal kidney,
CC followed by fetal lung and brain. In adult brain, abundantly expressed
CC in the cerebellum, followed by cerebral cortex, medulla and spinal
CC cord; very low levels in total brain, frontal lobe, temporal lobe and
CC putamen. Weak expression detected in adult brain, heart, lung, skeletal
CC muscle, pancreas, spleen and prostate. {ECO:0000269|PubMed:10448064}.
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; AB027464; BAA84093.1; -; mRNA.
DR EMBL; BC074997; AAH74997.1; -; mRNA.
DR EMBL; BC074998; AAH74998.1; -; mRNA.
DR CCDS; CCDS9267.1; -.
DR PIR; JC7086; JC7086.
DR RefSeq; NP_009128.1; NM_007197.3.
DR AlphaFoldDB; Q9ULW2; -.
DR SMR; Q9ULW2; -.
DR BioGRID; 116380; 70.
DR IntAct; Q9ULW2; 55.
DR STRING; 9606.ENSP00000229030; -.
DR ChEMBL; CHEMBL4523492; -.
DR GlyGen; Q9ULW2; 3 sites.
DR iPTMnet; Q9ULW2; -.
DR PhosphoSitePlus; Q9ULW2; -.
DR BioMuta; FZD10; -.
DR DMDM; 17433091; -.
DR jPOST; Q9ULW2; -.
DR MassIVE; Q9ULW2; -.
DR MaxQB; Q9ULW2; -.
DR PaxDb; Q9ULW2; -.
DR PeptideAtlas; Q9ULW2; -.
DR PRIDE; Q9ULW2; -.
DR ProteomicsDB; 85140; -.
DR ABCD; Q9ULW2; 5 sequenced antibodies.
DR Antibodypedia; 2928; 266 antibodies from 33 providers.
DR DNASU; 11211; -.
DR Ensembl; ENST00000229030.5; ENSP00000229030.4; ENSG00000111432.5.
DR GeneID; 11211; -.
DR KEGG; hsa:11211; -.
DR MANE-Select; ENST00000229030.5; ENSP00000229030.4; NM_007197.4; NP_009128.1.
DR UCSC; uc001uii.4; human.
DR CTD; 11211; -.
DR DisGeNET; 11211; -.
DR GeneCards; FZD10; -.
DR HGNC; HGNC:4039; FZD10.
DR HPA; ENSG00000111432; Tissue enhanced (esophagus, skin).
DR MIM; 606147; gene.
DR neXtProt; NX_Q9ULW2; -.
DR OpenTargets; ENSG00000111432; -.
DR PharmGKB; PA28456; -.
DR VEuPathDB; HostDB:ENSG00000111432; -.
DR eggNOG; KOG3577; Eukaryota.
DR GeneTree; ENSGT00940000161861; -.
DR HOGENOM; CLU_007873_2_1_1; -.
DR InParanoid; Q9ULW2; -.
DR OMA; LMGHDDQ; -.
DR OrthoDB; 509772at2759; -.
DR PhylomeDB; Q9ULW2; -.
DR TreeFam; TF317907; -.
DR PathwayCommons; Q9ULW2; -.
DR Reactome; R-HSA-373080; Class B/2 (Secretin family receptors).
DR SignaLink; Q9ULW2; -.
DR SIGNOR; Q9ULW2; -.
DR BioGRID-ORCS; 11211; 8 hits in 1031 CRISPR screens.
DR GeneWiki; FZD10; -.
DR GenomeRNAi; 11211; -.
DR Pharos; Q9ULW2; Tbio.
DR PRO; PR:Q9ULW2; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9ULW2; protein.
DR Bgee; ENSG00000111432; Expressed in gingival epithelium and 123 other tissues.
DR ExpressionAtlas; Q9ULW2; baseline and differential.
DR Genevisible; Q9ULW2; HS.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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; IDA:WormBase.
DR GO; GO:0017147; F:Wnt-protein binding; IBA:GO_Central.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:WormBase.
DR GO; GO:0071300; P:cellular response to retinoic acid; ISS:UniProtKB.
DR GO; GO:0034260; P:negative regulation of GTPase activity; IMP:BHF-UCL.
DR GO; GO:0030182; P:neuron differentiation; ISS:UniProtKB.
DR GO; GO:0038031; P:non-canonical Wnt signaling pathway via JNK cascade; IMP:BHF-UCL.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IMP:BHF-UCL.
DR GO; GO:0043507; P:positive regulation of JUN kinase activity; IMP:BHF-UCL.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:BHF-UCL.
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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..581
FT /note="Frizzled-10"
FT /id="PRO_0000013005"
FT TOPO_DOM 21..225
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..262
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..311
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 333..351
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..372
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 373..393
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 394..414
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 415..443
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 444..464
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 465..502
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 503..523
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 524..581
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..150
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT REGION 560..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 526..531
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 579..581
FT /note="PDZ-binding"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 485
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 34..95
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 42..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 79..117
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 106..147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 110..134
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 581 AA; 65336 MW; E9B7E51FA7C87B26 CRC64;
MQRPGPRLWL VLQVMGSCAA ISSMDMERPG DGKCQPIEIP MCKDIGYNMT RMPNLMGHEN
QREAAIQLHE FAPLVEYGCH GHLRFFLCSL YAPMCTEQVS TPIPACRVMC EQARLKCSPI
MEQFNFKWPD SLDCRKLPNK NDPNYLCMEA PNNGSDEPTR GSGLFPPLFR PQRPHSAQEH
PLKDGGPGRG GCDNPGKFHH VEKSASCAPL CTPGVDVYWS REDKRFAVVW LAIWAVLCFF
SSAFTVLTFL IDPARFRYPE RPIIFLSMCY CVYSVGYLIR LFAGAESIAC DRDSGQLYVI
QEGLESTGCT LVFLVLYYFG MASSLWWVVL TLTWFLAAGK KWGHEAIEAN SSYFHLAAWA
IPAVKTILIL VMRRVAGDEL TGVCYVGSMD VNALTGFVLI PLACYLVIGT SFILSGFVAL
FHIRRVMKTG GENTDKLEKL MVRIGLFSVL YTVPATCVIA CYFYERLNMD YWKILAAQHK
CKMNNQTKTL DCLMAASIPA VEIFMVKIFM LLVVGITSGM WIWTSKTLQS WQQVCSRRLK
KKSRRKPASV ITSGGIYKKA QHPQKTHHGK YEIPAQSPTC V
