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Database: UniProt
Entry: O75084
LinkDB: O75084
Original site: O75084 
ID   FZD7_HUMAN              Reviewed;         574 AA.
AC   O75084; O94816; Q53S59; Q96B74;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2004, sequence version 2.
DT   03-SEP-2014, entry version 131.
DE   RecName: Full=Frizzled-7;
DE            Short=Fz-7;
DE            Short=hFz7;
DE   AltName: Full=FzE3;
DE   Flags: Precursor;
GN   Name=FZD7;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND COUPLING TO BETA-CATENIN PATHWAY.
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
RT   mediates APC/beta-catenin signals.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:10164-10169(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 4.";
RL   Nature 434:724-731(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Fetal lung;
RX   PubMed=9813155; DOI=10.1006/bbrc.1998.9607;
RA   Sagara N., Toda G., Hirai M., Terada M., Katoh M.;
RT   "Molecular cloning, differential expression, and chromosomal
RT   localization of human frizzled-1, frizzled-2, and frizzled-7.";
RL   Biochem. Biophys. Res. Commun. 252:117-122(1998).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   INTERACTION WITH MYOC.
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).
RN   [7]
RP   VARIANT SER-24.
RX   PubMed=17224074; DOI=10.1186/bcr1637;
RA   Chanock S.J., Burdett L., Yeager M., Llaca V., Langeroed A.,
RA   Presswalla S., Kaaresen R., Strausberg R.L., Gerhard D.S.,
RA   Kristensen V., Perou C.M., Boerresen-Dale A.-L.;
RT   "Somatic sequence alterations in twenty-one genes selected by
RT   expression profile analysis of breast carcinomas.";
RL   Breast Cancer Res. 9:R5-R5(2007).
CC   -!- FUNCTION: Receptor for Wnt proteins. Most of frizzled receptors
CC       are coupled to the beta-catenin canonical signaling pathway, which
CC       leads to the activation of disheveled proteins, inhibition of GSK-
CC       3 kinase, nuclear accumulation of beta-catenin and activation of
CC       Wnt target genes. A second signaling pathway involving PKC and
CC       calcium fluxes has been seen for some family members, but it is
CC       not yet clear if it represents a distinct pathway or if it can be
CC       integrated in the canonical pathway, as PKC seems to be required
CC       for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem
CC       to involve interactions with G-proteins. May be involved in
CC       transduction and intercellular transmission of polarity
CC       information during tissue morphogenesis and/or in differentiated
CC       tissues.
CC   -!- SUBUNIT: Interacts with MAGI3 and DVL1 (By similarity). Interacts
CC       with MYOC.
CC   -!- INTERACTION:
CC       O00560:SDCBP; NbExp=4; IntAct=EBI-746917, EBI-727004;
CC       P56703:WNT3; NbExp=3; IntAct=EBI-746917, EBI-3644922;
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By
CC       similarity). Cell membrane; Multi-pass membrane protein (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: High expression in adult skeletal muscle and
CC       fetal kidney, followed by fetal lung, adult heart, brain, and
CC       placenta. Specifically expressed in squamous cell esophageal
CC       carcinomas.
CC   -!- DOMAIN: Lys-Thr-X-X-X-Trp motif interacts with the PDZ doman of
CC       Dvl (Disheveled) family members and is involved in the activation
CC       of the Wnt/beta-catenin signaling pathway (By similarity).
CC   -!- DOMAIN: The FZ domain is involved in binding with Wnt ligands (By
CC       similarity).
CC   -!- PTM: Ubiquitinated by ZNRF3, leading to its degradation by the
CC       proteasome (By similarity).
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo
CC       family.
CC   -!- SIMILARITY: Contains 1 FZ (frizzled) domain.
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DR   EMBL; AB010881; BAA32424.1; -; mRNA.
DR   EMBL; AB017365; BAA34668.1; -; mRNA.
DR   EMBL; AC069148; AAX93250.1; -; Genomic_DNA.
DR   EMBL; CH471063; EAW70298.1; -; Genomic_DNA.
DR   EMBL; BC015915; AAH15915.1; -; mRNA.
DR   CCDS; CCDS2351.1; -.
DR   PIR; JE0339; JE0339.
DR   RefSeq; NP_003498.1; NM_003507.1.
DR   UniGene; Hs.173859; -.
DR   ProteinModelPortal; O75084; -.
DR   SMR; O75084; 49-155, 204-565.
DR   BioGrid; 113920; 4.
DR   IntAct; O75084; 6.
DR   MINT; MINT-1461434; -.
DR   STRING; 9606.ENSP00000286201; -.
DR   MEROPS; I93.001; -.
DR   PhosphoSite; O75084; -.
DR   MaxQB; O75084; -.
DR   PaxDb; O75084; -.
DR   PRIDE; O75084; -.
DR   DNASU; 8324; -.
DR   Ensembl; ENST00000286201; ENSP00000286201; ENSG00000155760.
DR   GeneID; 8324; -.
DR   KEGG; hsa:8324; -.
DR   UCSC; uc002uyw.1; human.
DR   CTD; 8324; -.
DR   GeneCards; GC02P202863; -.
DR   HGNC; HGNC:4045; FZD7.
DR   MIM; 603410; gene.
DR   neXtProt; NX_O75084; -.
DR   PharmGKB; PA28462; -.
DR   eggNOG; NOG257258; -.
DR   HOGENOM; HOG000233237; -.
DR   HOVERGEN; HBG006977; -.
DR   InParanoid; O75084; -.
DR   KO; K02432; -.
DR   OMA; CVERFSE; -.
DR   OrthoDB; EOG7M3J01; -.
DR   PhylomeDB; O75084; -.
DR   TreeFam; TF317907; -.
DR   Reactome; REACT_172581; PCP/CE pathway.
DR   Reactome; REACT_18372; Class B/2 (Secretin family receptors).
DR   Reactome; REACT_207044; TCF dependent signaling in response to WNT.
DR   SignaLink; O75084; -.
DR   ChiTaRS; FZD7; human.
DR   GeneWiki; FZD7; -.
DR   GenomeRNAi; 8324; -.
DR   NextBio; 31171; -.
DR   PRO; PR:O75084; -.
DR   Bgee; O75084; -.
DR   CleanEx; HS_FZD7; -.
DR   Genevestigator; O75084; -.
DR   GO; GO:0045177; C:apical part of cell; IBA:RefGenome.
DR   GO; GO:0005737; C:cytoplasm; IBA:RefGenome.
DR   GO; GO:0016021; C:integral component of membrane; TAS:BHF-UCL.
DR   GO; GO:0032589; C:neuron projection membrane; IBA:RefGenome.
DR   GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0005109; F:frizzled binding; IPI:UniProtKB.
DR   GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0030165; F:PDZ domain binding; IPI:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0042813; F:Wnt-activated receptor activity; IBA:RefGenome.
DR   GO; GO:0017147; F:Wnt-protein binding; IPI:BHF-UCL.
DR   GO; GO:0007409; P:axonogenesis; IBA:RefGenome.
DR   GO; GO:0007420; P:brain development; IBA:RefGenome.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:UniProtKB.
DR   GO; GO:0071300; P:cellular response to retinoic acid; ISS:UniProtKB.
DR   GO; GO:0007199; P:G-protein coupled receptor signaling pathway coupled to cGMP nucleotide second messenger; IBA:RefGenome.
DR   GO; GO:0008406; P:gonad development; IBA:RefGenome.
DR   GO; GO:0060231; P:mesenchymal to epithelial transition; IMP:BHF-UCL.
DR   GO; GO:0010812; P:negative regulation of cell-substrate adhesion; IMP:BHF-UCL.
DR   GO; GO:0042666; P:negative regulation of ectodermal cell fate specification; 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:0060054; P:positive regulation of epithelial cell proliferation involved in wound healing; IMP:BHF-UCL.
DR   GO; GO:0046330; P:positive regulation of JNK cascade; IC:BHF-UCL.
DR   GO; GO:0042327; P:positive regulation of phosphorylation; IDA:BHF-UCL.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL.
DR   GO; GO:0035412; P:regulation of catenin import into nucleus; IMP:BHF-UCL.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:BHF-UCL.
DR   GO; GO:0014834; P:satellite cell maintenance involved in skeletal muscle regeneration; IEA:Ensembl.
DR   GO; GO:0048103; P:somatic stem cell division; IEA:Ensembl.
DR   GO; GO:0019827; P:stem cell maintenance; IMP:BHF-UCL.
DR   GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR   GO; GO:0033077; P:T cell differentiation in thymus; IEA:Ensembl.
DR   GO; GO:0001944; P:vasculature development; IBA:RefGenome.
DR   GO; GO:0007223; P:Wnt signaling pathway, calcium modulating pathway; IBA:RefGenome.
DR   Gene3D; 1.10.2000.10; -; 1.
DR   InterPro; IPR000539; Frizzled.
DR   InterPro; IPR015526; Frizzled/SFRP.
DR   InterPro; IPR020067; Frizzled_dom.
DR   InterPro; IPR026552; FZD7.
DR   InterPro; IPR017981; GPCR_2-like.
DR   PANTHER; PTHR11309; PTHR11309; 1.
DR   PANTHER; PTHR11309:SF31; PTHR11309:SF31; 1.
DR   Pfam; PF01534; Frizzled; 1.
DR   Pfam; PF01392; Fz; 1.
DR   PRINTS; PR00489; FRIZZLED.
DR   SMART; SM00063; FRI; 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; Complete proteome; Developmental protein;
KW   Disulfide bond; G-protein coupled receptor; Glycoprotein; Membrane;
KW   Polymorphism; Receptor; Reference proteome; Signal; Transducer;
KW   Transmembrane; Transmembrane helix; Ubl conjugation;
KW   Wnt signaling pathway.
FT   SIGNAL        1     32       Potential.
FT   CHAIN        33    574       Frizzled-7.
FT                                /FTId=PRO_0000012996.
FT   TOPO_DOM     33    256       Extracellular (Potential).
FT   TRANSMEM    257    277       Helical; Name=1; (Potential).
FT   TOPO_DOM    278    288       Cytoplasmic (Potential).
FT   TRANSMEM    289    309       Helical; Name=2; (Potential).
FT   TOPO_DOM    310    336       Extracellular (Potential).
FT   TRANSMEM    337    357       Helical; Name=3; (Potential).
FT   TOPO_DOM    358    379       Cytoplasmic (Potential).
FT   TRANSMEM    380    400       Helical; Name=4; (Potential).
FT   TOPO_DOM    401    423       Extracellular (Potential).
FT   TRANSMEM    424    444       Helical; Name=5; (Potential).
FT   TOPO_DOM    445    470       Cytoplasmic (Potential).
FT   TRANSMEM    471    491       Helical; Name=6; (Potential).
FT   TOPO_DOM    492    528       Extracellular (Potential).
FT   TRANSMEM    529    549       Helical; Name=7; (Potential).
FT   TOPO_DOM    550    574       Cytoplasmic (Potential).
FT   DOMAIN       44    163       FZ.
FT   MOTIF       552    557       Lys-Thr-X-X-X-Trp motif, mediates
FT                                interaction with the PDZ domain of Dvl
FT                                family members (By similarity).
FT   MOTIF       572    574       PDZ-binding.
FT   CARBOHYD     63     63       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    164    164       N-linked (GlcNAc...) (Potential).
FT   DISULFID     49    110       By similarity.
FT   DISULFID     57    103       By similarity.
FT   DISULFID     94    131       By similarity.
FT   DISULFID    120    160       By similarity.
FT   DISULFID    124    148       By similarity.
FT   VARIANT      24     24       G -> D (in dbSNP:rs35111363).
FT                                /FTId=VAR_049292.
FT   VARIANT      24     24       G -> S.
FT                                /FTId=VAR_033024.
FT   VARIANT     196    196       G -> E (in dbSNP:rs34908164).
FT                                /FTId=VAR_033941.
FT   VARIANT     487    487       A -> V (in dbSNP:rs35600847).
FT                                /FTId=VAR_033942.
FT   CONFLICT      8      8       A -> V (in Ref. 1; BAA32424).
FT   CONFLICT     15     15       L -> F (in Ref. 1; BAA32424).
FT   CONFLICT    201    201       R -> K (in Ref. 1; BAA32424).
FT   CONFLICT    308    308       L -> F (in Ref. 1; BAA32424).
FT   CONFLICT    408    408       S -> N (in Ref. 1; BAA32424).
FT   CONFLICT    415    415       L -> F (in Ref. 1; BAA32424).
FT   CONFLICT    433    433       L -> F (in Ref. 1; BAA32424).
FT   CONFLICT    447    447       L -> F (in Ref. 1; BAA32424).
FT   CONFLICT    534    534       Y -> C (in Ref. 1; BAA32424).
SQ   SEQUENCE   574 AA;  63620 MW;  801934246B426DF5 CRC64;
     MRDPGAAAPL SSLGLCALVL ALLGALSAGA GAQPYHGEKG ISVPDHGFCQ PISIPLCTDI
     AYNQTILPNL LGHTNQEDAG LEVHQFYPLV KVQCSPELRF FLCSMYAPVC TVLDQAIPPC
     RSLCERARQG CEALMNKFGF QWPERLRCEN FPVHGAGEIC VGQNTSDGSG GPGGGPTAYP
     TAPYLPDLPF TALPPGASDG RGRPAFPFSC PRQLKVPPYL GYRFLGERDC GAPCEPGRAN
     GLMYFKEEER RFARLWVGVW SVLCCASTLF TVLTYLVDMR RFSYPERPII FLSGCYFMVA
     VAHVAGFLLE DRAVCVERFS DDGYRTVAQG TKKEGCTILF MVLYFFGMAS SIWWVILSLT
     WFLAAGMKWG HEAIEANSQY FHLAAWAVPA VKTITILAMG QVDGDLLSGV CYVGLSSVDA
     LRGFVLAPLF VYLFIGTSFL LAGFVSLFRI RTIMKHDGTK TEKLEKLMVR IGVFSVLYTV
     PATIVLACYF YEQAFREHWE RTWLLQTCKS YAVPCPPGHF PPMSPDFTVF MIKYLMTMIV
     GITTGFWIWS GKTLQSWRRF YHRLSHSSKG ETAV
//
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