FZD5_MOUSE
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 03-AUG-2022, entry version 181.
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; 1.
DR DIP; DIP-41260N; -.
DR IntAct; Q9EQD0; 7.
DR MINT; Q9EQD0; -.
DR STRING; 10090.ENSMUSP00000067783; -.
DR GlyGen; Q9EQD0; 2 sites.
DR iPTMnet; Q9EQD0; -.
DR PhosphoSitePlus; Q9EQD0; -.
DR PaxDb; Q9EQD0; -.
DR PRIDE; Q9EQD0; -.
DR ProteomicsDB; 272926; -.
DR Antibodypedia; 19996; 427 antibodies from 36 providers.
DR DNASU; 14367; -.
DR Ensembl; ENSMUST00000063982; ENSMUSP00000067783; ENSMUSG00000045005.
DR Ensembl; ENSMUST00000116133; ENSMUSP00000111828; ENSMUSG00000045005.
DR GeneID; 14367; -.
DR KEGG; mmu:14367; -.
DR UCSC; uc007bgy.1; mouse.
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; MARPDPC; -.
DR OrthoDB; 509772at2759; -.
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 73 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 214 other tissues.
DR Genevisible; Q9EQD0; MM.
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:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
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:0032729; P:positive regulation of interferon-gamma production; ISO:MGI.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IGI:ARUK-UCL.
DR GO; GO:0043507; P:positive regulation of JUN kinase activity; IDA:MGI.
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:0031077; P:post-embryonic camera-type eye development; IMP:MGI.
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; -; 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; IPR037441; FZ5_CRD.
DR InterPro; IPR017981; GPCR_2-like.
DR PANTHER; PTHR11309; PTHR11309; 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 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
