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   14-DEC-2022, entry version 194.
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; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   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 mediates
RT   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., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., 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., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., 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., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   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., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., 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 localization
RT   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 project:
RT   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., Presswalla S.,
RA   Kaaresen R., Strausberg R.L., Gerhard D.S., Kristensen V., Perou C.M.,
RA   Boerresen-Dale A.-L.;
RT   "Somatic sequence alterations in twenty-one genes selected by expression
RT   profile analysis of breast carcinomas.";
RL   Breast Cancer Res. 9:R5-R5(2007).
RN   [8]
RP   INTERACTION WITH GPC3.
RX   PubMed=24496449; DOI=10.1242/jcs.140871;
RA   Capurro M., Martin T., Shi W., Filmus J.;
RT   "Glypican-3 binds to Frizzled and plays a direct role in the stimulation of
RT   canonical Wnt signaling.";
RL   J. Cell Sci. 127:1565-1575(2014).
RN   [9]
RP   FUNCTION, AND INTERACTION WITH CCDC88C.
RX   PubMed=26126266; DOI=10.7554/elife.07091;
RA   Aznar N., Midde K.K., Dunkel Y., Lopez-Sanchez I., Pavlova Y., Marivin A.,
RA   Barbazan J., Murray F., Nitsche U., Janssen K.P., Willert K., Goel A.,
RA   Abal M., Garcia-Marcos M., Ghosh P.;
RT   "Daple is a novel non-receptor GEF required for trimeric G protein
RT   activation in Wnt signaling.";
RL   Elife 4:E07091-E07091(2015).
RN   [10]
RP   FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH C.DIFFICILE TCDB
RP   (MICROBIAL INFECTION).
RX   PubMed=27680706; DOI=10.1038/nature19799;
RA   Tao L., Zhang J., Meraner P., Tovaglieri A., Wu X., Gerhard R., Zhang X.,
RA   Stallcup W.B., Miao J., He X., Hurdle J.G., Breault D.T., Brass A.L.,
RA   Dong M.;
RT   "Frizzled proteins are colonic epithelial receptors for C. difficile toxin
RT   B.";
RL   Nature 538:350-355(2016).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 569-574, SITE, INTERACTION WITH
RP   SYNTENIN, MUTAGENESIS OF LYS-569, AND SUBCELLULAR LOCATION.
RX   PubMed=27386966; DOI=10.1038/ncomms12101;
RA   Egea-Jimenez A.L., Gallardo R., Garcia-Pino A., Ivarsson Y.,
RA   Wawrzyniak A.M., Kashyap R., Loris R., Schymkowitz J., Rousseau F.,
RA   Zimmermann P.;
RT   "Frizzled 7 and PIP2 binding by syntenin PDZ2 domain supports Frizzled 7
RT   trafficking and signalling.";
RL   Nat. Commun. 7:12101-12101(2016).
CC   -!- FUNCTION: Receptor for Wnt proteins. Most frizzled receptors are
CC       coupled to the beta-catenin canonical signaling pathway, which leads to
CC       the activation of disheveled proteins, inhibition of GSK-3 kinase,
CC       nuclear accumulation of beta-catenin and activation of Wnt target
CC       genes. A second signaling pathway involving PKC and calcium fluxes has
CC       been seen for some family members, but it is not yet clear if it
CC       represents a distinct pathway or if it can be integrated in the
CC       canonical pathway, as PKC seems to be required for Wnt-mediated
CC       inactivation of GSK-3 kinase. Both pathways seem to involve
CC       interactions with G-proteins. Activation by WNT8 induces expression of
CC       beta-catenin target genes (By similarity). Following ligand activation,
CC       binds to CCDC88C/DAPLE which displaces DVL1 from FZD7 and leads to
CC       inhibition of canonical Wnt signaling, activation of G-proteins by
CC       CCDC88C and triggering of non-canonical Wnt responses
CC       (PubMed:26126266). May be involved in transduction and intercellular
CC       transmission of polarity information during tissue morphogenesis and/or
CC       in differentiated tissues. {ECO:0000250|UniProtKB:Q61090,
CC       ECO:0000269|PubMed:26126266}.
CC   -!- FUNCTION: (Microbial infection) Acts as a receptor for C.difficile
CC       toxin TcdB in the colonic epithelium. {ECO:0000269|PubMed:27680706}.
CC   -!- SUBUNIT: Interacts with MAGI3 (By similarity). Interacts with DVL1 (By
CC       similarity). Interacts with CCDC88C/DAPLE; the interaction displaces
CC       DVL1 from FZD7, leading to inhibition of canonical Wnt signaling and
CC       triggering of non-canonical Wnt responses (PubMed:26126266). Interacts
CC       with MYOC (PubMed:19188438). Binds to SDCBP; this interaction is
CC       increased by inositol trisphosphate (IP3) (PubMed:27386966). Interacts
CC       with glypican GPC3 (PubMed:24496449). {ECO:0000250|UniProtKB:Q61090,
CC       ECO:0000269|PubMed:19188438, ECO:0000269|PubMed:24496449,
CC       ECO:0000269|PubMed:26126266}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with C.difficile toxin TcdB;
CC       frizzled receptors constitute the major host receptors for TcdB in the
CC       colonic epithelium. {ECO:0000269|PubMed:27680706}.
CC   -!- INTERACTION:
CC       O75084; O43315: AQP9; NbExp=3; IntAct=EBI-746917, EBI-17444777;
CC       O75084; Q9BXK5: BCL2L13; NbExp=3; IntAct=EBI-746917, EBI-747430;
CC       O75084; O15552: FFAR2; NbExp=3; IntAct=EBI-746917, EBI-2833872;
CC       O75084; P37235: HPCAL1; NbExp=3; IntAct=EBI-746917, EBI-749311;
CC       O75084; A8MZ59: LEUTX; NbExp=3; IntAct=EBI-746917, EBI-17490413;
CC       O75084; P10620: MGST1; NbExp=3; IntAct=EBI-746917, EBI-2691601;
CC       O75084; P61601: NCALD; NbExp=3; IntAct=EBI-746917, EBI-749635;
CC       O75084; P62166: NCS1; NbExp=5; IntAct=EBI-746917, EBI-746987;
CC       O75084; P04156: PRNP; NbExp=3; IntAct=EBI-746917, EBI-977302;
CC       O75084; O00560: SDCBP; NbExp=4; IntAct=EBI-746917, EBI-727004;
CC       O75084; O43765: SGTA; NbExp=3; IntAct=EBI-746917, EBI-347996;
CC       O75084; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-746917, EBI-744081;
CC       O75084; O14863: SLC30A4; NbExp=3; IntAct=EBI-746917, EBI-13918058;
CC       O75084; Q9NP94: SLC39A2; NbExp=3; IntAct=EBI-746917, EBI-12898013;
CC       O75084; Q9H2J7: SLC6A15; NbExp=3; IntAct=EBI-746917, EBI-11343466;
CC       O75084; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-746917, EBI-10982110;
CC       O75084; Q9UMX0: UBQLN1; NbExp=5; IntAct=EBI-746917, EBI-741480;
CC       O75084; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-746917, EBI-947187;
CC       O75084; P56703: WNT3; NbExp=3; IntAct=EBI-746917, EBI-3644922;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27386966};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:27386966}. Endosome
CC       membrane {ECO:0000269|PubMed:27386966}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:27386966}. Note=Associated to the plasma membrane
CC       in the presence of FZD7 and phosphatidylinositol 4,5-bisphosphate
CC       (PIP2). Localized in recycling endosomes in other conditions.
CC       {ECO:0000269|PubMed:27386966}.
CC   -!- TISSUE SPECIFICITY: High expression in adult skeletal muscle and fetal
CC       kidney, followed by fetal lung, adult heart, brain, and placenta.
CC       Specifically expressed in squamous cell esophageal carcinomas.
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; 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   PDB; 4Z33; X-ray; 2.45 A; C/D=569-574.
DR   PDB; 5T44; X-ray; 1.99 A; A/B=31-168.
DR   PDB; 5URV; X-ray; 2.20 A; A/B=30-168.
DR   PDB; 5WBS; X-ray; 2.88 A; A/B/C/D/E/F/G/H=30-174.
DR   PDB; 6NE2; X-ray; 1.30 A; A=46-163.
DR   PDB; 6NE4; X-ray; 1.65 A; A=46-163.
DR   PDB; 6O3A; X-ray; 2.10 A; E=42-179.
DR   PDB; 6O3B; X-ray; 2.50 A; C/H=42-179.
DR   PDB; 7EVW; EM; 3.22 A; R=38-574.
DR   PDBsum; 4Z33; -.
DR   PDBsum; 5T44; -.
DR   PDBsum; 5URV; -.
DR   PDBsum; 5WBS; -.
DR   PDBsum; 6NE2; -.
DR   PDBsum; 6NE4; -.
DR   PDBsum; 6O3A; -.
DR   PDBsum; 6O3B; -.
DR   PDBsum; 7EVW; -.
DR   AlphaFoldDB; O75084; -.
DR   SMR; O75084; -.
DR   BioGRID; 113920; 76.
DR   IntAct; O75084; 40.
DR   MINT; O75084; -.
DR   STRING; 9606.ENSP00000286201; -.
DR   BindingDB; O75084; -.
DR   ChEMBL; CHEMBL3559688; -.
DR   GuidetoPHARMACOLOGY; 235; -.
DR   GlyGen; O75084; 3 sites, 1 Thr glycan (1 site).
DR   iPTMnet; O75084; -.
DR   PhosphoSitePlus; O75084; -.
DR   BioMuta; FZD7; -.
DR   EPD; O75084; -.
DR   jPOST; O75084; -.
DR   MassIVE; O75084; -.
DR   MaxQB; O75084; -.
DR   PaxDb; O75084; -.
DR   PeptideAtlas; O75084; -.
DR   ProteomicsDB; 49751; -.
DR   ABCD; O75084; 44 sequenced antibodies.
DR   Antibodypedia; 19943; 544 antibodies from 38 providers.
DR   DNASU; 8324; -.
DR   Ensembl; ENST00000286201.3; ENSP00000286201.1; ENSG00000155760.3.
DR   GeneID; 8324; -.
DR   KEGG; hsa:8324; -.
DR   MANE-Select; ENST00000286201.3; ENSP00000286201.1; NM_003507.2; NP_003498.1.
DR   UCSC; uc002uyw.2; human.
DR   AGR; HGNC:4045; -.
DR   CTD; 8324; -.
DR   DisGeNET; 8324; -.
DR   GeneCards; FZD7; -.
DR   HGNC; HGNC:4045; FZD7.
DR   HPA; ENSG00000155760; Low tissue specificity.
DR   MIM; 603410; gene.
DR   neXtProt; NX_O75084; -.
DR   OpenTargets; ENSG00000155760; -.
DR   PharmGKB; PA28462; -.
DR   VEuPathDB; HostDB:ENSG00000155760; -.
DR   eggNOG; KOG3577; Eukaryota.
DR   GeneTree; ENSGT00940000158239; -.
DR   HOGENOM; CLU_007873_2_1_1; -.
DR   InParanoid; O75084; -.
DR   OMA; TWSILCC; -.
DR   OrthoDB; 330751at2759; -.
DR   PhylomeDB; O75084; -.
DR   TreeFam; TF317907; -.
DR   PathwayCommons; O75084; -.
DR   Reactome; R-HSA-373080; Class B/2 (Secretin family receptors).
DR   Reactome; R-HSA-4086400; PCP/CE pathway.
DR   Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
DR   Reactome; R-HSA-9673324; WNT5:FZD7-mediated leishmania damping.
DR   SignaLink; O75084; -.
DR   SIGNOR; O75084; -.
DR   BioGRID-ORCS; 8324; 16 hits in 1076 CRISPR screens.
DR   ChiTaRS; FZD7; human.
DR   GeneWiki; FZD7; -.
DR   GenomeRNAi; 8324; -.
DR   Pharos; O75084; Tchem.
DR   PRO; PR:O75084; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; O75084; protein.
DR   Bgee; ENSG00000155760; Expressed in hair follicle and 183 other tissues.
DR   Genevisible; O75084; HS.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0055038; C:recycling endosome membrane; IDA:UniProtKB.
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:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
DR   GO; GO:0042813; F:Wnt receptor activity; IDA:WormBase.
DR   GO; GO:0017147; F:Wnt-protein binding; IPI:BHF-UCL.
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:0060231; P:mesenchymal to epithelial transition; IMP:BHF-UCL.
DR   GO; GO:2000726; P:negative regulation of cardiac muscle cell differentiation; IGI: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:0045893; P:positive regulation of DNA-templated transcription; IDA: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:0060828; P:regulation of canonical Wnt signaling pathway; IMP:BHF-UCL.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IMP:BHF-UCL.
DR   GO; GO:0014834; P:skeletal muscle 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 population 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:0060071; P:Wnt signaling pathway, planar cell polarity pathway; NAS:ParkinsonsUK-UCL.
DR   CDD; cd07466; CRD_FZ7; 1.
DR   Gene3D; 1.10.2000.10; -; 1.
DR   InterPro; IPR042742; Frizzled-7_CRD.
DR   InterPro; IPR015526; Frizzled/SFRP.
DR   InterPro; IPR000539; Frizzled/Smoothened_TM.
DR   InterPro; IPR020067; Frizzled_dom.
DR   InterPro; IPR036790; Frizzled_dom_sf.
DR   InterPro; IPR026552; FZD7.
DR   InterPro; IPR017981; GPCR_2-like.
DR   PANTHER; PTHR11309; FRIZZLED; 1.
DR   PANTHER; PTHR11309:SF31; FRIZZLED-7; 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.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Developmental protein; Disulfide bond;
KW   Endosome; G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW   Reference proteome; Signal; Transducer; Transmembrane; Transmembrane helix;
KW   Ubl conjugation; Wnt signaling pathway.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..574
FT                   /note="Frizzled-7"
FT                   /id="PRO_0000012996"
FT   TOPO_DOM        33..256
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        257..277
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        278..288
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        289..309
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        310..336
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        337..357
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        358..379
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        380..400
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        401..423
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        424..444
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        445..470
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        471..491
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        492..528
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        529..549
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        550..574
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          44..163
FT                   /note="FZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   MOTIF           552..557
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           572..574
FT                   /note="PDZ-binding"
FT   SITE            569
FT                   /note="Essential for SDCBP-mediated plasma membrane
FT                   phosphatidylinositol-4,5-bisphosphate recognition"
FT                   /evidence="ECO:0000269|PubMed:27386966"
FT   CARBOHYD        63
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        164
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        49..110
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   DISULFID        57..103
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   DISULFID        94..131
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   DISULFID        120..160
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   DISULFID        124..148
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   VARIANT         24
FT                   /note="G -> D (in dbSNP:rs35111363)"
FT                   /id="VAR_049292"
FT   VARIANT         24
FT                   /note="G -> S (in dbSNP:rs755615030)"
FT                   /evidence="ECO:0000269|PubMed:17224074"
FT                   /id="VAR_033024"
FT   VARIANT         196
FT                   /note="G -> E (in dbSNP:rs34908164)"
FT                   /id="VAR_033941"
FT   VARIANT         487
FT                   /note="A -> V (in dbSNP:rs35600847)"
FT                   /id="VAR_033942"
FT   MUTAGEN         569
FT                   /note="K->A: Impaired SDCBP-mediated interaction with
FT                   phosphatidylinositol-4,5-bisphosphate."
FT                   /evidence="ECO:0000269|PubMed:27386966"
FT   CONFLICT        8
FT                   /note="A -> V (in Ref. 1; BAA32424)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        15
FT                   /note="L -> F (in Ref. 1; BAA32424)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        201
FT                   /note="R -> K (in Ref. 1; BAA32424)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        308
FT                   /note="L -> F (in Ref. 1; BAA32424)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        408
FT                   /note="S -> N (in Ref. 1; BAA32424)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        415
FT                   /note="L -> F (in Ref. 1; BAA32424)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        433
FT                   /note="L -> F (in Ref. 1; BAA32424)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        447
FT                   /note="L -> F (in Ref. 1; BAA32424)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        534
FT                   /note="Y -> C (in Ref. 1; BAA32424)"
FT                   /evidence="ECO:0000305"
FT   STRAND          45..47
FT                   /evidence="ECO:0007829|PDB:6O3B"
FT   STRAND          48..51
FT                   /evidence="ECO:0007829|PDB:6NE2"
FT   HELIX           55..57
FT                   /evidence="ECO:0007829|PDB:6NE2"
FT   STRAND          58..61
FT                   /evidence="ECO:0007829|PDB:5T44"
FT   STRAND          64..68
FT                   /evidence="ECO:0007829|PDB:6NE2"
FT   HELIX           76..84
FT                   /evidence="ECO:0007829|PDB:6NE2"
FT   HELIX           87..91
FT                   /evidence="ECO:0007829|PDB:6NE2"
FT   HELIX           98..106
FT                   /evidence="ECO:0007829|PDB:6NE2"
FT   STRAND          112..115
FT                   /evidence="ECO:0007829|PDB:6NE2"
FT   HELIX           121..128
FT                   /evidence="ECO:0007829|PDB:6NE2"
FT   HELIX           131..137
FT                   /evidence="ECO:0007829|PDB:6NE2"
FT   HELIX           144..146
FT                   /evidence="ECO:0007829|PDB:6NE2"
FT   HELIX           148..150
FT                   /evidence="ECO:0007829|PDB:6NE2"
FT   TURN            154..156
FT                   /evidence="ECO:0007829|PDB:6NE2"
FT   STRAND          218..220
FT                   /evidence="ECO:0007829|PDB:7EVW"
FT   TURN            225..229
FT                   /evidence="ECO:0007829|PDB:7EVW"
FT   TURN            246..248
FT                   /evidence="ECO:0007829|PDB:7EVW"
FT   HELIX           249..277
FT                   /evidence="ECO:0007829|PDB:7EVW"
FT   STRAND          279..281
FT                   /evidence="ECO:0007829|PDB:7EVW"
FT   TURN            284..286
FT                   /evidence="ECO:0007829|PDB:7EVW"
FT   HELIX           287..308
FT                   /evidence="ECO:0007829|PDB:7EVW"
FT   STRAND          323..325
FT                   /evidence="ECO:0007829|PDB:7EVW"
FT   HELIX           336..344
FT                   /evidence="ECO:0007829|PDB:7EVW"
FT   TURN            345..348
FT                   /evidence="ECO:0007829|PDB:7EVW"
FT   HELIX           349..365
FT                   /evidence="ECO:0007829|PDB:7EVW"
FT   HELIX           371..374
FT                   /evidence="ECO:0007829|PDB:7EVW"
FT   HELIX           375..377
FT                   /evidence="ECO:0007829|PDB:7EVW"
FT   HELIX           378..399
FT                   /evidence="ECO:0007829|PDB:7EVW"
FT   TURN            406..408
FT                   /evidence="ECO:0007829|PDB:7EVW"
FT   HELIX           418..424
FT                   /evidence="ECO:0007829|PDB:7EVW"
FT   HELIX           426..453
FT                   /evidence="ECO:0007829|PDB:7EVW"
FT   TURN            454..456
FT                   /evidence="ECO:0007829|PDB:7EVW"
FT   TURN            461..463
FT                   /evidence="ECO:0007829|PDB:7EVW"
FT   HELIX           464..473
FT                   /evidence="ECO:0007829|PDB:7EVW"
FT   HELIX           475..494
FT                   /evidence="ECO:0007829|PDB:7EVW"
FT   HELIX           496..501
FT                   /evidence="ECO:0007829|PDB:7EVW"
FT   HELIX           504..507
FT                   /evidence="ECO:0007829|PDB:7EVW"
FT   HELIX           527..543
FT                   /evidence="ECO:0007829|PDB:7EVW"
FT   HELIX           544..548
FT                   /evidence="ECO:0007829|PDB:7EVW"
FT   HELIX           551..565
FT                   /evidence="ECO:0007829|PDB:7EVW"
FT   STRAND          572..574
FT                   /evidence="ECO:0007829|PDB:4Z33"
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
//