ID   FZD5_MOUSE              Reviewed;         585 AA.
AC   Q9EQD0; G5E8F0; O08975; Q8BMR2; Q8CHK9;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 3.
DT   24-JAN-2024, entry version 189.
DE   RecName: Full=Frizzled-5;
DE            Short=Fz-5;
DE            Short=mFz5;
DE   Flags: Precursor;
GN   Name=Fzd5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=C57BL/6N; TISSUE=Intestine;
RX   PubMed=11092808; DOI=10.1242/dev.128.1.25;
RA   Ishikawa T., Tamai Y., Zorn A.M., Yoshida H., Seldin M.F., Nishikawa S.,
RA   Taketo M.M.;
RT   "Mouse Wnt receptor gene Fzd5 is essential for yolk sac and placental
RT   angiogenesis.";
RL   Development 128:25-33(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Ito S., Imamura T., Shiota K.;
RT   "Molecular cloning and characterization of a gene encoding for rat Frizzled
RT   5.";
RL   Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 211-300.
RC   STRAIN=C57BL/6J; TISSUE=Prostate;
RA   Johnson M.A., Greenberg N.M.;
RL   Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   TISSUE SPECIFICITY.
RX   PubMed=8626800; DOI=10.1074/jbc.271.8.4468;
RA   Wang Y., Macke J.P., Abella B.S., Andreasson K., Worley P., Gilbert D.J.,
RA   Copeland N.G., Jenkins N.A., Nathans J.;
RT   "A large family of putative transmembrane receptors homologous to the
RT   product of the Drosophila tissue polarity gene frizzled.";
RL   J. Biol. Chem. 271:4468-4476(1996).
RN   [8]
RP   INTERACTION WITH GOPC, AND SUBCELLULAR LOCATION.
RX   PubMed=11520064; DOI=10.1006/bbrc.2001.5430;
RA   Yao R., Maeda T., Takada S., Noda T.;
RT   "Identification of a PDZ domain containing Golgi protein, GOPC, as an
RT   interaction partner of frizzled.";
RL   Biochem. Biophys. Res. Commun. 286:771-778(2001).
RN   [9]
RP   INTERACTION WITH WNT7A, AND FUNCTION.
RX   PubMed=18230341; DOI=10.1016/j.bbrc.2008.01.088;
RA   Carmon K.S., Loose D.S.;
RT   "Wnt7a interaction with Fzd5 and detection of signaling activation using a
RT   split eGFP.";
RL   Biochem. Biophys. Res. Commun. 368:285-291(2008).
RN   [10]
RP   INTERACTION WITH WNT7A, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=20530549; DOI=10.1242/dev.046722;
RA   Sahores M., Gibb A., Salinas P.C.;
RT   "Frizzled-5, a receptor for the synaptic organizer Wnt7a, regulates
RT   activity-mediated synaptogenesis.";
RL   Development 137:2215-2225(2010).
CC   -!- FUNCTION: Receptor for Wnt proteins (PubMed:11092808, PubMed:18230341).
CC       Can activate WNT2, WNT10B, WNT5A, but not WNT2B or WNT4 (in vitro); the
CC       in vivo situation may be different since not all of these are known to
CC       be coexpressed (PubMed:11092808). In neurons, activation of WNT7A
CC       promotes formation of synapses (By similarity). Functions in the
CC       canonical Wnt/beta-catenin signaling pathway (PubMed:18230341). The
CC       canonical Wnt/beta-catenin signaling pathway leads to the activation of
CC       disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation
CC       of beta-catenin and activation of Wnt target genes (PubMed:18230341). A
CC       second signaling pathway involving PKC and calcium fluxes has been seen
CC       for some family members, but it is not yet clear if it represents a
CC       distinct pathway or if it can be integrated in the canonical pathway,
CC       as PKC seems to be required for Wnt-mediated inactivation of GSK-3
CC       kinase. Both pathways seem to involve interactions with G-proteins. May
CC       be involved in transduction and intercellular transmission of polarity
CC       information during tissue morphogenesis and/or in differentiated
CC       tissues (Probable). Plays a role in yolk sac angiogenesis and in
CC       placental vascularization (PubMed:11092808).
CC       {ECO:0000250|UniProtKB:Q8CHL0, ECO:0000269|PubMed:11092808,
CC       ECO:0000269|PubMed:18230341, ECO:0000305}.
CC   -!- SUBUNIT: Binding of unsaturated fatty acid molecules (via FZ domain)
CC       promotes homodimerization (via FZ domain). Interacts with WNT2B (By
CC       similarity). Interacts with WNT7A (PubMed:18230341, PubMed:20530549).
CC       Interacts with GOPC (PubMed:11520064). {ECO:0000250|UniProtKB:Q13467,
CC       ECO:0000269|PubMed:11520064, ECO:0000269|PubMed:18230341,
CC       ECO:0000269|PubMed:20530549}.
CC   -!- INTERACTION:
CC       Q9EQD0; Q8BH60: Gopc; NbExp=3; IntAct=EBI-7938232, EBI-296357;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11520064,
CC       ECO:0000269|PubMed:20530549}; Multi-pass membrane protein
CC       {ECO:0000305}. Golgi apparatus membrane {ECO:0000269|PubMed:11520064};
CC       Multi-pass membrane protein {ECO:0000305}. Synapse
CC       {ECO:0000269|PubMed:20530549}. Perikaryon
CC       {ECO:0000250|UniProtKB:Q8CHL0}. Cell projection, dendrite
CC       {ECO:0000250|UniProtKB:Q8CHL0}. Cell projection, axon
CC       {ECO:0000250|UniProtKB:Q8CHL0}. Note=Localized at the plasma membrane
CC       and also found at the Golgi. {ECO:0000269|PubMed:11520064}.
CC   -!- TISSUE SPECIFICITY: Detected in hippocampus (at protein level)
CC       (PubMed:20530549). Expressed in eye, kidney, lung, chondrocytes,
CC       epithelial cells of the small intestine and gobelet cells of the colon
CC       (PubMed:8626800). {ECO:0000269|PubMed:20530549,
CC       ECO:0000269|PubMed:8626800}.
CC   -!- DEVELOPMENTAL STAGE: Detected at low levels in neonate brain;
CC       expression levels increase steadily during the first four weeks after
CC       birth and show a further increase in adults (at protein level)
CC       (PubMed:20530549). Expressed in the yolk sac, placenta, eye and lung
CC       bud at 9.5 dpc. At 10.5 dpc, also expressed in the placental blood
CC       vessel of embryonic origin (PubMed:11092808).
CC       {ECO:0000269|PubMed:11092808, ECO:0000269|PubMed:20530549}.
CC   -!- DOMAIN: The PDZ-binding motif mediates interaction with GOPC.
CC       {ECO:0000250}.
CC   -!- DOMAIN: The FZ domain is involved in binding with Wnt ligands.
CC       {ECO:0000250}.
CC   -!- PTM: Ubiquitinated by RNF43 and ZNRF3, leading to its degradation by
CC       the proteasome. {ECO:0000250|UniProtKB:Q13467}.
CC   -!- DISRUPTION PHENOTYPE: Full embryonic lethality around 12.5 dpc, due to
CC       defects in yolk sac and placenta vascularization.
CC       {ECO:0000269|PubMed:11092808}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG39355.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF272146; AAG39355.1; ALT_FRAME; mRNA.
DR   EMBL; AB052910; BAC53981.1; -; mRNA.
DR   EMBL; AK030111; BAC26789.1; -; mRNA.
DR   EMBL; AC101915; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466548; EDL00208.1; -; Genomic_DNA.
DR   EMBL; CH466548; EDL00209.1; -; Genomic_DNA.
DR   EMBL; AF005203; AAC01953.1; -; mRNA.
DR   CCDS; CCDS15008.1; -.
DR   RefSeq; NP_001036124.1; NM_001042659.1.
DR   RefSeq; NP_073558.2; NM_022721.3.
DR   AlphaFoldDB; Q9EQD0; -.
DR   SMR; Q9EQD0; -.
DR   BioGRID; 199778; 2.
DR   DIP; DIP-41260N; -.
DR   IntAct; Q9EQD0; 7.
DR   MINT; Q9EQD0; -.
DR   STRING; 10090.ENSMUSP00000067783; -.
DR   GlyCosmos; Q9EQD0; 2 sites, No reported glycans.
DR   GlyGen; Q9EQD0; 2 sites.
DR   iPTMnet; Q9EQD0; -.
DR   PhosphoSitePlus; Q9EQD0; -.
DR   PaxDb; 10090-ENSMUSP00000067783; -.
DR   ProteomicsDB; 272926; -.
DR   Antibodypedia; 19996; 474 antibodies from 36 providers.
DR   DNASU; 14367; -.
DR   Ensembl; ENSMUST00000063982.7; ENSMUSP00000067783.6; ENSMUSG00000045005.10.
DR   Ensembl; ENSMUST00000116133.4; ENSMUSP00000111828.3; ENSMUSG00000045005.10.
DR   GeneID; 14367; -.
DR   KEGG; mmu:14367; -.
DR   UCSC; uc007bgy.1; mouse.
DR   AGR; MGI:108571; -.
DR   CTD; 7855; -.
DR   MGI; MGI:108571; Fzd5.
DR   VEuPathDB; HostDB:ENSMUSG00000045005; -.
DR   eggNOG; KOG3577; Eukaryota.
DR   GeneTree; ENSGT00940000162639; -.
DR   HOGENOM; CLU_007873_2_0_1; -.
DR   InParanoid; Q9EQD0; -.
DR   OMA; NCAIPCY; -.
DR   OrthoDB; 5483535at2759; -.
DR   PhylomeDB; Q9EQD0; -.
DR   TreeFam; TF317907; -.
DR   Reactome; R-MMU-4086398; Ca2+ pathway.
DR   Reactome; R-MMU-4608870; Asymmetric localization of PCP proteins.
DR   Reactome; R-MMU-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR   Reactome; R-MMU-4641263; Regulation of FZD by ubiquitination.
DR   Reactome; R-MMU-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
DR   BioGRID-ORCS; 14367; 2 hits in 78 CRISPR screens.
DR   ChiTaRS; Fzd5; mouse.
DR   PRO; PR:Q9EQD0; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q9EQD0; Protein.
DR   Bgee; ENSMUSG00000045005; Expressed in optic fissure and 216 other cell types or tissues.
DR   GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR   GO; GO:0005923; C:bicellular tight junction; IDA:MGI.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:BHF-UCL.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
DR   GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0045202; C:synapse; ISO:MGI.
DR   GO; GO:0001540; F:amyloid-beta binding; ISO:MGI.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR   GO; GO:0042813; F:Wnt receptor activity; ISO:MGI.
DR   GO; GO:0017147; F:Wnt-protein binding; IPI:MGI.
DR   GO; GO:0001525; P:angiogenesis; IMP:MGI.
DR   GO; GO:0008595; P:anterior/posterior axis specification, embryo; ISO:MGI.
DR   GO; GO:0060561; P:apoptotic process involved in morphogenesis; IMP:MGI.
DR   GO; GO:0060670; P:branching involved in labyrinthine layer morphogenesis; IMP:MGI.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IMP:MGI.
DR   GO; GO:0071219; P:cellular response to molecule of bacterial origin; ISO:MGI.
DR   GO; GO:0060718; P:chorionic trophoblast cell differentiation; IMP:MGI.
DR   GO; GO:0000578; P:embryonic axis specification; ISO:MGI.
DR   GO; GO:0031076; P:embryonic camera-type eye development; IMP:MGI.
DR   GO; GO:0048596; P:embryonic camera-type eye morphogenesis; IMP:CACAO.
DR   GO; GO:0002071; P:glandular epithelial cell maturation; IMP:MGI.
DR   GO; GO:0060574; P:intestinal epithelial cell maturation; IMP:MGI.
DR   GO; GO:0060716; P:labyrinthine layer blood vessel development; IMP:MGI.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:MGI.
DR   GO; GO:0035567; P:non-canonical Wnt signaling pathway; IBA:GO_Central.
DR   GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IGI:ARUK-UCL.
DR   GO; GO:0002726; P:positive regulation of T cell cytokine production; ISO:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:MGI.
DR   GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IGI:ARUK-UCL.
DR   GO; GO:0032729; P:positive regulation of type II interferon production; ISO:MGI.
DR   GO; GO:0031077; P:post-embryonic camera-type eye development; IMP:CACAO.
DR   GO; GO:0099054; P:presynapse assembly; ISO:MGI.
DR   GO; GO:2000810; P:regulation of bicellular tight junction assembly; IMP:MGI.
DR   GO; GO:1901382; P:regulation of chorionic trophoblast cell proliferation; IMP:MGI.
DR   GO; GO:0060061; P:Spemann organizer formation; ISO:MGI.
DR   GO; GO:0060715; P:syncytiotrophoblast cell differentiation involved in labyrinthine layer development; IMP:MGI.
DR   GO; GO:0033077; P:T cell differentiation in thymus; IMP:MGI.
DR   GO; GO:0001944; P:vasculature development; IMP:MGI.
DR   GO; GO:0016055; P:Wnt signaling pathway; IGI:MGI.
DR   CDD; cd07460; CRD_FZ5; 1.
DR   Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR015526; Frizzled/SFRP.
DR   InterPro; IPR000539; Frizzled/Smoothened_7TM.
DR   InterPro; IPR020067; Frizzled_dom.
DR   InterPro; IPR036790; Frizzled_dom_sf.
DR   InterPro; IPR037441; FZ5_CRD.
DR   InterPro; IPR017981; GPCR_2-like_7TM.
DR   PANTHER; PTHR11309; FRIZZLED; 1.
DR   PANTHER; PTHR11309:SF136; FRIZZLED-5; 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.
DR   Genevisible; Q9EQD0; MM.
PE   1: Evidence at protein level;
KW   Angiogenesis; Cell membrane; Cell projection; Developmental protein;
KW   Differentiation; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Golgi apparatus; Lipid-binding; Membrane; Receptor; Reference proteome;
KW   Signal; Synapse; Transducer; Transmembrane; Transmembrane helix;
KW   Ubl conjugation; Wnt signaling pathway.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..585
FT                   /note="Frizzled-5"
FT                   /id="PRO_0000243936"
FT   TOPO_DOM        27..238
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        239..259
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        260..270
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        271..291
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        292..315
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        316..336
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        337..358
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        359..379
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        380..402
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        403..423
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        424..449
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        450..470
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        471..500
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        501..521
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        522..585
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          28..150
FT                   /note="FZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   REGION          156..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           582..584
FT                   /note="PDZ-binding"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        47
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        151
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        33..94
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   DISULFID        41..87
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   DISULFID        78..116
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   DISULFID        105..147
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   DISULFID        109..133
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   CONFLICT        4
FT                   /note="P -> T (in Ref. 3; BAC26789)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        123..124
FT                   /note="YG -> S (in Ref. 2; BAC53981)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        402
FT                   /note="G -> S (in Ref. 1; AAG39355)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        419
FT                   /note="L -> H (in Ref. 2; BAC53981)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        444
FT                   /note="E -> G (in Ref. 2; BAC53981)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        477
FT                   /note="S -> T (in Ref. 1; AAG39355)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        481
FT                   /note="A -> P (in Ref. 1; AAG39355)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        489
FT                   /note="P -> T (in Ref. 1; AAG39355)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        521
FT                   /note="I -> F (in Ref. 2; BAC53981)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   585 AA;  64138 MW;  5FC03620AF087733 CRC64;
     MARPDPSAPP SLLLLLLAQL VGRAAAASKA PVCQEITVPM CRGIGYNLTH MPNQFNHDTQ
     DEAGLEVHQF WPLVEIHCSP DLRFFLCSMY TPICLPDYHK PLPPCRSVCE RAKAGCSPLM
     RQYGFAWPER MSCDRLPVLG GDAEVLCMDY NRSEATTASP KSFPAKPTLP GPPGAPSSGG
     ECPSGGPSVC TCREPFVPIL KESHPLYNKV RTGQVPNCAV PCYQPSFSPD ERTFATFWIG
     LWSVLCFIST STTVATFLID MERFRYPERP IIFLSACYLC VSLGFLVRLV VGHASVACSR
     EHSHIHYETT GPALCTVVFL LVYFFGMASS IWWVILSLTW FLAAGMKWGN EAIAGYAQYF
     HLAAWLIPSV KSITALALSS VDGDPVAGIC YVGNQNLNSL RGFVLGPLVL YLLVGTLFLL
     AGFVSLFRIR SVIKQGGTKT DKLEKLMIRI GIFTLLYTVP ASIVVACYLY EQHYRESWEA
     ALTCACPGPD AGQPRAKPEY WVLMLKYFMC LVVGITSGVW IWSGKTLESW RRFTSRCCCS
     SRRGHKSGGA MAAGDYAEAS AALTGRTGPP GPTAAYHKQV SLSHV
//