FZD7_HUMAN
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-AUG-2022, entry version 192.
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 O-linked 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 PRIDE; O75084; -.
DR ProteomicsDB; 49751; -.
DR ABCD; O75084; 44 sequenced antibodies.
DR Antibodypedia; 19943; 519 antibodies from 39 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 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:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
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: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:0060828; P:regulation of canonical Wnt signaling pathway; IMP:BHF-UCL.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; 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; 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 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 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
