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 29-MAY-2013, entry version 119.
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 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).
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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 IPI; IPI00024012; -.
DR PIR; JE0339; JE0339.
DR RefSeq; NP_003498.1; NM_003507.1.
DR UniGene; Hs.173859; -.
DR ProteinModelPortal; O75084; -.
DR IntAct; O75084; 4.
DR MINT; MINT-1461434; -.
DR STRING; 9606.ENSP00000286201; -.
DR PhosphoSite; 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; EOG4V437C; -.
DR PhylomeDB; O75084; -.
DR Pathway_Interaction_DB; syndecan_4_pathway; Syndecan-4-mediated signaling events.
DR Reactome; REACT_111102; Signal Transduction.
DR SignaLink; O75084; -.
DR ChiTaRS; FZD7; human.
DR GenomeRNAi; 8324; -.
DR NextBio; 31171; -.
DR Bgee; O75084; -.
DR CleanEx; HS_FZD7; -.
DR Genevestigator; O75084; -.
DR GermOnline; ENSG00000155760; Homo sapiens.
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 to membrane; TAS:BHF-UCL.
DR GO; GO:0032589; C:neuron projection membrane; IBA:RefGenome.
DR GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0042813; F:Wnt-activated receptor activity; IBA:RefGenome.
DR GO; GO:0007409; P:axonogenesis; IBA:RefGenome.
DR GO; GO:0007420; P:brain development; IBA:RefGenome.
DR GO; GO:0060070; P:canonical Wnt receptor 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:0038031; P:non-canonical Wnt receptor 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-dependent; IDA:BHF-UCL.
DR GO; GO:0035412; P:regulation of catenin import into nucleus; IMP:BHF-UCL.
DR GO; GO:0014834; P:satellite cell maintenance involved in skeletal muscle regeneration; IEA:Compara.
DR GO; GO:0048103; P:somatic stem cell division; IEA:Compara.
DR GO; GO:0019827; P:stem cell maintenance; IMP:BHF-UCL.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IEA:Compara.
DR GO; GO:0033077; P:T cell differentiation in thymus; IEA:Compara.
DR GO; GO:0001944; P:vasculature development; IBA:RefGenome.
DR GO; GO:0007223; P:Wnt receptor 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; Frizzled_Cys-rich; 1.
DR PROSITE; PS50038; FZ; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE 2: Evidence at transcript 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
//
