ID FZD6_HUMAN Reviewed; 706 AA. AC O60353; B4DRN0; Q6N0A5; Q6P9C3; Q8WXR9; DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 2. DT 13-FEB-2019, entry version 176. DE RecName: Full=Frizzled-6; DE Short=Fz-6; DE Short=hFz6; DE Flags: Precursor; GN Name=FZD6; 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] (ISOFORM 1), AND VARIANT LEU-345. RC TISSUE=Fetal lung; RX PubMed=9480858; DOI=10.1006/bbrc.1998.8143; RA Tokuhara M., Hirai M., Atomi Y., Terada M., Katoh M.; RT "Molecular cloning of human frizzled-6."; RL Biochem. Biophys. Res. Commun. 243:622-627(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT LEU-345. RA Gazit A., Yaniv A., Aaronson S.A.; RT "Molecular cloning of the human Frizzled 6."; RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=11707601; DOI=10.1073/pnas.241525498; RA Tanner S.M., Austin J.L., Leone G., Rush L.J., Plass C., Heinonen K., RA Mrozek K., Sill H., Knuutila S., Kolitz J.E., Archer K.J., RA Caligiuri M.A., Bloomfield C.D., de La Chapelle A.; RT "BAALC, the human member of a novel mammalian neuroectoderm gene RT lineage, is implicated in hematopoiesis and acute leukemia."; RL Proc. Natl. Acad. Sci. U.S.A. 98:13901-13906(2001). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S., RA Tsutsumi S., Aburatani H., Asai K., Akiyama Y.; RT "Genome-wide discovery and analysis of human seven transmembrane helix RT receptor genes."; RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT RP VAL-33. RC TISSUE=Uterine endothelium; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16421571; DOI=10.1038/nature04406; RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., RA Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., RA Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., RA Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T., RA Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., RA DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., RA Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., RA Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., RA O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., RA Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., RA Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., RA Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., RA Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., RA Lander E.S.; RT "DNA sequence and analysis of human chromosome 8."; RL Nature 439:331-335(2006). RN [8] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT RP LEU-345. RC TISSUE=Placenta; 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 [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [11] RP POSSIBLE INVOLVEMENT IN NEURAL TUBE DEFECTS, AND VARIANTS VAL-33; RP TYR-140; GLU-152; LEU-345; ASP-388; GLN-405; CYS-511; HIS-511; RP ARG-604; THR-620 AND GLU-664. RX PubMed=22045688; DOI=10.1002/humu.21643; RA De Marco P., Merello E., Rossi A., Piatelli G., Cama A., Kibar Z., RA Capra V.; RT "FZD6 is a novel gene for human neural tube defects."; RL Hum. Mutat. 33:384-390(2012). RN [12] RP UBIQUITINATION BY ZNRF3. RX PubMed=22575959; DOI=10.1038/nature11019; RA Hao H.X., Xie Y., Zhang Y., Charlat O., Oster E., Avello M., Lei H., RA Mickanin C., Liu D., Ruffner H., Mao X., Ma Q., Zamponi R., RA Bouwmeester T., Finan P.M., Kirschner M.W., Porter J.A., Serluca F.C., RA Cong F.; RT "ZNRF3 promotes Wnt receptor turnover in an R-spondin-sensitive RT manner."; RL Nature 485:195-200(2012). RN [13] RP VARIANT NDNC10 CYS-511, AND CHARACTERIZATION OF VARIANT NDNC10 RP CYS-511. RX PubMed=21665003; DOI=10.1016/j.ajhg.2011.05.013; RA Frojmark A.S., Schuster J., Sobol M., Entesarian M., Kilander M.B., RA Gabrikova D., Nawaz S., Baig S.M., Schulte G., Klar J., Dahl N.; RT "Mutations in Frizzled 6 cause isolated autosomal-recessive nail RT dysplasia."; RL Am. J. Hum. Genet. 88:852-860(2011). 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. Together with FZD3, is involved in the neural tube CC closure and plays a role in the regulation of the establishment of CC planar cell polarity (PCP), particularly in the orientation of CC asymmetric bundles of stereocilia on the apical faces of a subset CC of auditory and vestibular sensory cells located in the inner ear CC (By similarity). {ECO:0000250|UniProtKB:Q61089}. CC -!- INTERACTION: CC Q8N474:SFRP1; NbExp=3; IntAct=EBI-8754490, EBI-3940687; CC Q9ULT6:ZNRF3; NbExp=2; IntAct=EBI-8754490, EBI-949772; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q61089}; CC Multi-pass membrane protein {ECO:0000255}. Cell membrane CC {ECO:0000250|UniProtKB:Q61089}; Multi-pass membrane protein CC {ECO:0000255}. Cell surface {ECO:0000250|UniProtKB:Q61089}. Apical CC cell membrane; Multi-pass membrane protein {ECO:0000255}. CC Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q61089}; CC Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with CC FZD3 at the apical face of cells (By similarity). CC {ECO:0000250|UniProtKB:Q61089}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O60353-1; Sequence=Displayed; CC Name=2; CC IsoId=O60353-2; Sequence=VSP_044291; CC -!- TISSUE SPECIFICITY: Detected in adult heart, brain, placenta, CC lung, liver, skeletal muscle, kidney, pancreas, thymus, prostate, CC testis, ovary, small intestine and colon. In the fetus, expressed CC in brain, lung, liver and kidney. CC -!- DOMAIN: Lys-Thr-X-X-X-Trp motif interacts with the PDZ domain of CC Dvl (Disheveled) family members and is involved in the activation CC of the 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 -!- DISEASE: Nail disorder, non-syndromic congenital, 10 (NDNC10) CC [MIM:614157]: A nail disorder characterized by a variable degree CC of onychauxis (thick nails), hyponychia, and onycholysis of all CC nails, with claw-shaped fingernails in some individuals. No other CC anomalies of ectodermal tissues, including hair, teeth, sweat CC glands, or skin, are noted, and individuals with dysplastic nails CC have normal hearing and normal psychomotor development. CC {ECO:0000269|PubMed:21665003}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- DISEASE: Note=Rare non-synonymous variants in FZD6 may contribute CC to neural tube defects, congenital malformations of the central CC nervous system and adjacent structures related to defective neural CC tube closure during the first trimester of pregnancy. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AB012911; BAA25686.1; -; mRNA. DR EMBL; AF072873; AAD41637.1; -; mRNA. DR EMBL; AF363578; AAL50384.1; -; Genomic_DNA. DR EMBL; AB065702; BAC05925.1; -; Genomic_DNA. DR EMBL; AK299341; BAG61342.1; -; mRNA. DR EMBL; BX640609; CAE45715.1; -; mRNA. DR EMBL; AC025370; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471060; EAW91867.1; -; Genomic_DNA. DR EMBL; BC060836; AAH60836.2; -; mRNA. DR CCDS; CCDS55268.1; -. [O60353-2] DR CCDS; CCDS6298.1; -. [O60353-1] DR PIR; JE0164; JE0164. DR RefSeq; NP_001158087.1; NM_001164615.1. [O60353-1] DR RefSeq; NP_001158088.1; NM_001164616.1. [O60353-2] DR RefSeq; NP_001304725.1; NM_001317796.1. DR RefSeq; NP_003497.2; NM_003506.3. [O60353-1] DR UniGene; Hs.591863; -. DR UniGene; Hs.676099; -. DR ProteinModelPortal; O60353; -. DR SMR; O60353; -. DR BioGrid; 113919; 17. DR DIP; DIP-59893N; -. DR IntAct; O60353; 12. DR MINT; O60353; -. DR STRING; 9606.ENSP00000351605; -. DR CarbonylDB; O60353; -. DR iPTMnet; O60353; -. DR PhosphoSitePlus; O60353; -. DR SwissPalm; O60353; -. DR BioMuta; FZD6; -. DR EPD; O60353; -. DR jPOST; O60353; -. DR MaxQB; O60353; -. DR PaxDb; O60353; -. DR PeptideAtlas; O60353; -. DR PRIDE; O60353; -. DR ProteomicsDB; 49378; -. DR Ensembl; ENST00000358755; ENSP00000351605; ENSG00000164930. [O60353-1] DR Ensembl; ENST00000522566; ENSP00000429055; ENSG00000164930. [O60353-1] DR Ensembl; ENST00000523739; ENSP00000429528; ENSG00000164930. [O60353-2] DR GeneID; 8323; -. DR KEGG; hsa:8323; -. DR UCSC; uc003ylh.4; human. [O60353-1] DR CTD; 8323; -. DR DisGeNET; 8323; -. DR EuPathDB; HostDB:ENSG00000164930.11; -. DR GeneCards; FZD6; -. DR H-InvDB; HIX0201314; -. DR HGNC; HGNC:4044; FZD6. DR HPA; HPA017991; -. DR MalaCards; FZD6; -. DR MIM; 603409; gene. DR MIM; 614157; phenotype. DR neXtProt; NX_O60353; -. DR OpenTargets; ENSG00000164930; -. DR Orphanet; 280654; Autosomal recessive nail dysplasia. DR PharmGKB; PA28461; -. DR eggNOG; KOG3577; Eukaryota. DR eggNOG; ENOG410XRC8; LUCA. DR GeneTree; ENSGT00940000158485; -. DR HOGENOM; HOG000233237; -. DR HOVERGEN; HBG006977; -. DR InParanoid; O60353; -. DR KO; K02376; -. DR OMA; KACTVLF; -. DR OrthoDB; 330751at2759; -. DR PhylomeDB; O60353; -. DR TreeFam; TF317907; -. DR Reactome; R-HSA-373080; Class B/2 (Secretin family receptors). DR Reactome; R-HSA-4086398; Ca2+ pathway. DR Reactome; R-HSA-4086400; PCP/CE pathway. DR Reactome; R-HSA-4641263; Regulation of FZD by ubiquitination. DR Reactome; R-HSA-5340588; RNF mutants show enhanced WNT signaling and proliferation. DR SIGNOR; O60353; -. DR ChiTaRS; FZD6; human. DR GeneWiki; FZD6; -. DR GenomeRNAi; 8323; -. DR PRO; PR:O60353; -. DR Proteomes; UP000005640; Chromosome 8. DR Bgee; ENSG00000164930; Expressed in 199 organ(s), highest expression level in bronchial epithelial cell. DR ExpressionAtlas; O60353; baseline and differential. DR Genevisible; O60353; HS. DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016327; C:apicolateral plasma membrane; IEA:Ensembl. DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell. DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005887; C:integral component of plasma membrane; ISS:BHF-UCL. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB. DR GO; GO:0042813; F:Wnt-activated receptor activity; IDA:BHF-UCL. DR GO; GO:0017147; F:Wnt-protein binding; ISS:BHF-UCL. DR GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central. DR GO; GO:0033278; P:cell proliferation in midbrain; IEA:Ensembl. DR GO; GO:0035880; P:embryonic nail plate morphogenesis; IEA:Ensembl. DR GO; GO:0048105; P:establishment of body hair planar orientation; IEA:Ensembl. DR GO; GO:0001942; P:hair follicle development; IEA:Ensembl. DR GO; GO:0042472; P:inner ear morphogenesis; IEA:Ensembl. DR GO; GO:1904693; P:midbrain morphogenesis; TAS:ParkinsonsUK-UCL. DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:BHF-UCL. DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:BHF-UCL. DR GO; GO:0001843; P:neural tube closure; IEA:Ensembl. DR GO; GO:0035567; P:non-canonical Wnt signaling pathway; IDA:BHF-UCL. DR GO; GO:0030168; P:platelet activation; IEA:Ensembl. DR GO; GO:0007223; P:Wnt signaling pathway, calcium modulating pathway; TAS:Reactome. DR GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; NAS:ParkinsonsUK-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; IPR026543; FZD6. DR InterPro; IPR017981; GPCR_2-like. DR PANTHER; PTHR11309; PTHR11309; 1. DR PANTHER; PTHR11309:SF75; PTHR11309:SF75; 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 Alternative splicing; Cell membrane; Complete proteome; KW Cytoplasmic vesicle; Developmental protein; Disease mutation; KW Disulfide bond; G-protein coupled receptor; Glycoprotein; Membrane; KW Phosphoprotein; Polymorphism; Receptor; Reference proteome; Signal; KW Transducer; Transmembrane; Transmembrane helix; Ubl conjugation; KW Wnt signaling pathway. FT SIGNAL 1 18 {ECO:0000255}. FT CHAIN 19 706 Frizzled-6. FT /FTId=PRO_0000012994. FT TOPO_DOM 19 201 Extracellular. {ECO:0000255}. FT TRANSMEM 202 222 Helical; Name=1. {ECO:0000255}. FT TOPO_DOM 223 233 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 234 254 Helical; Name=2. {ECO:0000255}. FT TOPO_DOM 255 284 Extracellular. {ECO:0000255}. FT TRANSMEM 285 305 Helical; Name=3. {ECO:0000255}. FT TOPO_DOM 306 324 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 325 345 Helical; Name=4. {ECO:0000255}. FT TOPO_DOM 346 370 Extracellular. {ECO:0000255}. FT TRANSMEM 371 391 Helical; Name=5. {ECO:0000255}. FT TOPO_DOM 392 416 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 417 437 Helical; Name=6. {ECO:0000255}. FT TOPO_DOM 438 473 Extracellular. {ECO:0000255}. FT TRANSMEM 474 494 Helical; Name=7. {ECO:0000255}. FT TOPO_DOM 495 706 Cytoplasmic. {ECO:0000255}. FT DOMAIN 19 132 FZ. {ECO:0000255|PROSITE- FT ProRule:PRU00090}. FT MOTIF 498 503 Lys-Thr-X-X-X-Trp motif, mediates FT interaction with the PDZ domain of Dvl FT family members. {ECO:0000250}. FT MOD_RES 653 653 Phosphoserine. FT {ECO:0000250|UniProtKB:Q61089}. FT CARBOHYD 38 38 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 352 352 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 24 85 {ECO:0000255|PROSITE-ProRule:PRU00090}. FT DISULFID 32 78 {ECO:0000255|PROSITE-ProRule:PRU00090}. FT DISULFID 69 106 {ECO:0000255|PROSITE-ProRule:PRU00090}. FT DISULFID 95 129 {ECO:0000255|PROSITE-ProRule:PRU00090}. FT DISULFID 99 123 {ECO:0000255|PROSITE-ProRule:PRU00090}. FT VAR_SEQ 1 32 Missing (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_044291. FT VARIANT 33 33 M -> V (in dbSNP:rs827528). FT {ECO:0000269|PubMed:17974005, FT ECO:0000269|PubMed:22045688}. FT /FTId=VAR_047440. FT VARIANT 140 140 H -> Y (in dbSNP:rs80216383). FT {ECO:0000269|PubMed:22045688}. FT /FTId=VAR_066963. FT VARIANT 152 152 Q -> E (in dbSNP:rs61753730). FT {ECO:0000269|PubMed:22045688}. FT /FTId=VAR_066964. FT VARIANT 345 345 M -> L (in dbSNP:rs3808553). FT {ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:22045688, FT ECO:0000269|PubMed:9480858, FT ECO:0000269|Ref.2}. FT /FTId=VAR_047441. FT VARIANT 388 388 A -> D (in dbSNP:rs142694816). FT {ECO:0000269|PubMed:22045688}. FT /FTId=VAR_066965. FT VARIANT 405 405 R -> Q (in dbSNP:rs150760762). FT {ECO:0000269|PubMed:22045688}. FT /FTId=VAR_066966. FT VARIANT 511 511 R -> C (in NDNC10; also found in a FT patient with neural tube defects; the FT mutant protein localizes to the lysosomes FT compared to wild-type; FT dbSNP:rs151339003). FT {ECO:0000269|PubMed:21665003, FT ECO:0000269|PubMed:22045688}. FT /FTId=VAR_066398. FT VARIANT 511 511 R -> H (in a patient with neural tube FT defects; dbSNP:rs767273753). FT {ECO:0000269|PubMed:22045688}. FT /FTId=VAR_066967. FT VARIANT 604 604 G -> R (in dbSNP:rs79408516). FT {ECO:0000269|PubMed:22045688}. FT /FTId=VAR_066968. FT VARIANT 620 620 S -> T (in dbSNP:rs116195528). FT {ECO:0000269|PubMed:22045688}. FT /FTId=VAR_066969. FT VARIANT 664 664 A -> E (in dbSNP:rs12549394). FT {ECO:0000269|PubMed:22045688}. FT /FTId=VAR_047442. SQ SEQUENCE 706 AA; 79292 MW; FBFF5844D6AB0223 CRC64; MEMFTFLLTC IFLPLLRGHS LFTCEPITVP RCMKMAYNMT FFPNLMGHYD QSIAAVEMEH FLPLANLECS PNIETFLCKA FVPTCIEQIH VVPPCRKLCE KVYSDCKKLI DTFGIRWPEE LECDRLQYCD ETVPVTFDPH TEFLGPQKKT EQVQRDIGFW CPRHLKTSGG QGYKFLGIDQ CAPPCPNMYF KSDELEFAKS FIGTVSIFCL CATLFTFLTF LIDVRRFRYP ERPIIYYSVC YSIVSLMYFI GFLLGDSTAC NKADEKLELG DTVVLGSQNK ACTVLFMLLY FFTMAGTVWW VILTITWFLA AGRKWSCEAI EQKAVWFHAV AWGTPGFLTV MLLAMNKVEG DNISGVCFVG LYDLDASRYF VLLPLCLCVF VGLSLLLAGI ISLNHVRQVI QHDGRNQEKL KKFMIRIGVF SGLYLVPLVT LLGCYVYEQV NRITWEITWV SDHCRQYHIP CPYQAKAKAR PELALFMIKY LMTLIVGISA VFWVGSKKTC TEWAGFFKRN RKRDPISESR RVLQESCEFF LKHNSKVKHK KKHYKPSSHK LKVISKSMGT STGATANHGT SAVAITSHDY LGQETLTEIQ TSPETSMREV KADGASTPRL REQDCGEPAS PAASISRLSG EQVDGKGQAG SVSESARSEG RISPKSDITD TGLAQSNNLQ VPSSSEPSSL KGSTSLLVHP VSGVRKEQGG GCHSDT //