CTND2_HUMAN
ID CTND2_HUMAN Reviewed; 1225 AA.
AC Q9UQB3; B0FTZ7; O00379; O15390; O43206; O43840; Q13589; Q9UM66; Q9UPM3;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 3.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Catenin delta-2;
DE AltName: Full=Delta-catenin;
DE AltName: Full=GT24;
DE AltName: Full=Neural plakophilin-related ARM-repeat protein;
DE Short=NPRAP;
DE AltName: Full=Neurojungin;
GN Name=CTNND2; Synonyms=NPRAP;
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] (ISOFORM 1), AND INTERACTION WITH PSEN1.
RX PubMed=9223106; DOI=10.1097/00001756-199705260-00054;
RA Zhou J., Liyanage U., Medina M., Ho C., Simmons A.D., Lovett M.,
RA Kosik K.S.;
RT "Presenilin 1 interaction in the brain with a novel member of the Armadillo
RT family.";
RL NeuroReport 8:2085-2090(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RC TISSUE=Brain;
RX PubMed=9971746; DOI=10.1083/jcb.144.3.519;
RA Lu Q., Paredes M., Medina M., Zhou J., Cavallo R., Peifer M., Orecchio L.,
RA Kosik K.S.;
RT "Delta-catenin, an adhesive junction-associated protein which promotes cell
RT scattering.";
RL J. Cell Biol. 144:519-532(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH PSEN1.
RC TISSUE=Fetal brain;
RX PubMed=10208590; DOI=10.1097/00001756-199902250-00022;
RA Tanahashi H., Tabira T.;
RT "Isolation of human delta-catenin and its binding specificity with
RT presenilin 1.";
RL NeuroReport 10:563-568(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS CYS-275; THR-482 AND
RP ARG-810.
RG NIEHS SNPs program;
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 186-1225 (ISOFORM 1), AND INTERACTION WITH
RP PSEN1.
RC TISSUE=Brain;
RX PubMed=10037471; DOI=10.1046/j.1471-4159.1999.0720999.x;
RA Levesque G., Yu G., Nishimura M., Zhang D.M., Levesque L., Yu H., Xu D.,
RA Liang Y., Rogaeva E.A., Ikeda M., Duthie M., Murgolo N., Wang L.,
RA VanderVere P., Bayne M.L., Strader C.D., Rommens J.M., Fraser P.E.,
RA St George-Hyslop P.H.;
RT "Presenilins interact with armadillo proteins including neural-specific
RT plakophilin-related protein and beta-catenin.";
RL J. Neurochem. 72:999-1008(1999).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 350-1225 (ISOFORM 1), AND ALTERNATIVE
RP SPLICING.
RC TISSUE=Fetal brain;
RX PubMed=9342840; DOI=10.1046/j.1432-0436.1997.6150293.x;
RA Paffenholz R., Franke W.W.;
RT "Identification and localization of a neurally expressed member of the
RT plakoglobin/armadillo multigene family.";
RL Differentiation 61:293-304(1997).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 689-1225 (ISOFORM 1).
RA Fraser P.E., Levesque G., Rogaeva E.A., Yu G., St George-Hyslop P.H.;
RT "A novel gene from the arm family.";
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 746-1225 (ISOFORM 1).
RC TISSUE=Brain;
RA Yu W., Sarginson J., Gibbs R.A.;
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 865-1225 (ISOFORMS 1/2).
RX PubMed=9049630; DOI=10.1101/gr.7.2.118;
RA Simmons A.D., Overhauser J., Lovett M.;
RT "Isolation of cDNAs from the Cri-du-chat critical region by direct
RT screening of a chromosome 5-specific cDNA library.";
RL Genome Res. 7:118-127(1997).
RN [12]
RP INTERACTION WITH ARHGEF28.
RX PubMed=17993462; DOI=10.1074/jbc.m707158200;
RA Kim H., Han J.-R., Park J., Oh M., James S.E., Chang S., Lu Q., Lee K.Y.,
RA Ki H., Song W.-J., Kim K.;
RT "Delta-catenin-induced dendritic morphogenesis. An essential role of
RT p190RhoGEF interaction through Akt1-mediated phosphorylation.";
RL J. Biol. Chem. 283:977-987(2008).
RN [13]
RP INTERACTION WITH GSK3A AND GSK3B, AND PHOSPHORYLATION BY GSK3B.
RX PubMed=19706605; DOI=10.1074/jbc.m109.002659;
RA Oh M., Kim H., Yang I., Park J.H., Cong W.T., Baek M.C., Bareiss S., Ki H.,
RA Lu Q., No J., Kwon I., Choi J.K., Kim K.;
RT "GSK-3 phosphorylates delta-catenin and negatively regulates its stability
RT via ubiquitination/proteosome-mediated proteolysis.";
RL J. Biol. Chem. 284:28579-28589(2009).
RN [14]
RP INTERACTION WITH FRMPD2.
RX PubMed=19706687; DOI=10.1242/jcs.046854;
RA Stenzel N., Fetzer C.P., Heumann R., Erdmann K.S.;
RT "PDZ-domain-directed basolateral targeting of the peripheral membrane
RT protein FRMPD2 in epithelial cells.";
RL J. Cell Sci. 122:3374-3384(2009).
RN [15]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH DNM2.
RX PubMed=22022388; DOI=10.1371/journal.pone.0025379;
RA Koutras C., Levesque G.;
RT "Identification of novel NPRAP/delta-catenin-interacting proteins and the
RT direct association of NPRAP with dynamin 2.";
RL PLoS ONE 6:E25379-E25379(2011).
RN [16]
RP INTERACTION WITH CCDC85B.
RX PubMed=25009281; DOI=10.1091/mbc.e13-08-0492;
RA Markham N.O., Doll C.A., Dohn M.R., Miller R.K., Yu H., Coffey R.J.,
RA McCrea P.D., Gamse J.T., Reynolds A.B.;
RT "DIPA-family coiled-coils bind conserved isoform-specific head domain of
RT p120-catenin family: potential roles in hydrocephalus and heterotopia.";
RL Mol. Biol. Cell 25:2592-2603(2014).
RN [17]
RP FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH CTNNB1, INVOLVEMENT IN
RP AUTISM, VARIANTS SER-34; LEU-189; LEU-224; CYS-275; HIS-330; HIS-454;
RP ASN-465; THR-482; PRO-507; CYS-713 AND MET-862, AND CHARACTERIZATION OF
RP VARIANTS SER-34; LEU-189; LEU-224; CYS-275; HIS-330; HIS-454; ASN-465;
RP THR-482; PRO-507; CYS-713; ARG-810 AND MET-862.
RX PubMed=25807484; DOI=10.1038/nature14186;
RA Turner T.N., Sharma K., Oh E.C., Liu Y.P., Collins R.L., Sosa M.X.,
RA Auer D.R., Brand H., Sanders S.J., Moreno-De-Luca D., Pihur V., Plona T.,
RA Pike K., Soppet D.R., Smith M.W., Cheung S.W., Martin C.L., State M.W.,
RA Talkowski M.E., Cook E., Huganir R., Katsanis N., Chakravarti A.;
RT "Loss of delta-catenin function in severe autism.";
RL Nature 520:51-56(2015).
RN [18]
RP VARIANT [LARGE SCALE ANALYSIS] SER-1159.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Has a critical role in neuronal development, particularly in
CC the formation and/or maintenance of dendritic spines and synapses
CC (PubMed:25807484). Involved in the regulation of Wnt signaling
CC (PubMed:25807484). It probably acts on beta-catenin turnover,
CC facilitating beta-catenin interaction with GSK3B, phosphorylation,
CC ubiquitination and degradation (By similarity). Functions as a
CC transcriptional activator when bound to ZBTB33 (By similarity). May be
CC involved in neuronal cell adhesion and tissue morphogenesis and
CC integrity by regulating adhesion molecules.
CC {ECO:0000250|UniProtKB:O35927, ECO:0000269|PubMed:25807484,
CC ECO:0000269|PubMed:9971746}.
CC -!- SUBUNIT: Binds to E-cadherin at a juxtamembrane site within the
CC cytoplasmic domain (By similarity). Interacts with PDZD2 (By
CC similarity). Interacts with ZBTB33 (By similarity). Binds to PSEN1
CC (PubMed:10037471) (PubMed:10208590) (PubMed:9223106). Interacts with
CC ARHGEF28 (PubMed:17993462). Interacts (via the extreme C-terminus) with
CC FRMPD2 (via the PDZ 2 domain) (PubMed:19706687). Interacts with CDK5
CC (By similarity). Interacts with CTNNB1 (PubMed:25807484). Interacts
CC with GSK3A and GSK3B (PubMed:19706605). Interacts with DNM2
CC (PubMed:22022388). Interacts with CCDC85B (PubMed:25009281).
CC {ECO:0000250|UniProtKB:O35116, ECO:0000250|UniProtKB:O35927,
CC ECO:0000269|PubMed:10037471, ECO:0000269|PubMed:10208590,
CC ECO:0000269|PubMed:17993462, ECO:0000269|PubMed:19706605,
CC ECO:0000269|PubMed:19706687, ECO:0000269|PubMed:22022388,
CC ECO:0000269|PubMed:25009281, ECO:0000269|PubMed:25807484,
CC ECO:0000269|PubMed:9223106}.
CC -!- INTERACTION:
CC Q9UQB3; Q12959: DLG1; NbExp=2; IntAct=EBI-7266482, EBI-357481;
CC Q9UQB3; Q14160: SCRIB; NbExp=2; IntAct=EBI-7266482, EBI-357345;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O35927}. Cell
CC junction, adherens junction {ECO:0000250|UniProtKB:O35927}. Cell
CC projection, dendrite {ECO:0000250|UniProtKB:O35116}. Perikaryon
CC {ECO:0000269|PubMed:22022388}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=NPRAPa;
CC IsoId=Q9UQB3-1; Sequence=Displayed;
CC Name=2; Synonyms=NPRAPc;
CC IsoId=Q9UQB3-2; Sequence=VSP_006746;
CC -!- TISSUE SPECIFICITY: Expressed in brain; highest expression is observed
CC in fetal brain (PubMed:25807484). {ECO:0000269|PubMed:25807484}.
CC -!- PTM: O-glycosylated. {ECO:0000250}.
CC -!- PTM: Phosphorylated by CDK5 (By similarity). Phosphorylated by GSK3B
CC (PubMed:19706605). {ECO:0000250|UniProtKB:O35116,
CC ECO:0000269|PubMed:19706605}.
CC -!- DISEASE: Note=Defects in CTNND2, including deleterious missense and
CC copy number variants (CNVs) are involved in autism, a complex
CC multifactorial, pervasive developmental disorder characterized by
CC impairments in reciprocal social interaction and communication,
CC restricted and stereotyped patterns of interests and activities, and
CC the presence of developmental abnormalities by 3 years of age. Most
CC individuals with autism also manifest moderate intellectual disability.
CC {ECO:0000269|PubMed:25807484}.
CC -!- SIMILARITY: Belongs to the beta-catenin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB68599.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAB88185.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/ctnnd2/";
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DR EMBL; U96136; AAC63103.1; -; mRNA.
DR EMBL; AB013805; BAA36163.1; -; mRNA.
DR EMBL; AC003089; AAB83940.1; -; Genomic_DNA.
DR EMBL; EU350953; ABY59658.1; -; Genomic_DNA.
DR EMBL; AC003954; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC004633; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC004648; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005367; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005610; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC010433; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC010626; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC113390; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC127460; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471102; EAX08053.1; -; Genomic_DNA.
DR EMBL; U81004; AAD00453.1; -; mRNA.
DR EMBL; U52351; AAB97957.1; -; mRNA.
DR EMBL; U72665; AAB68599.1; ALT_INIT; mRNA.
DR EMBL; AF035302; AAB88185.1; ALT_FRAME; mRNA.
DR EMBL; U52828; AAB96357.1; -; mRNA.
DR CCDS; CCDS3881.1; -. [Q9UQB3-1]
DR RefSeq; NP_001275644.1; NM_001288715.1.
DR RefSeq; NP_001275645.1; NM_001288716.1.
DR RefSeq; NP_001275646.1; NM_001288717.1.
DR RefSeq; NP_001323.1; NM_001332.3. [Q9UQB3-1]
DR AlphaFoldDB; Q9UQB3; -.
DR SMR; Q9UQB3; -.
DR BioGRID; 107882; 18.
DR CORUM; Q9UQB3; -.
DR DIP; DIP-1138N; -.
DR IntAct; Q9UQB3; 11.
DR MINT; Q9UQB3; -.
DR STRING; 9606.ENSP00000307134; -.
DR GlyGen; Q9UQB3; 7 sites, 1 O-linked glycan (7 sites).
DR iPTMnet; Q9UQB3; -.
DR PhosphoSitePlus; Q9UQB3; -.
DR SwissPalm; Q9UQB3; -.
DR BioMuta; CTNND2; -.
DR DMDM; 84028193; -.
DR EPD; Q9UQB3; -.
DR jPOST; Q9UQB3; -.
DR MassIVE; Q9UQB3; -.
DR MaxQB; Q9UQB3; -.
DR PaxDb; Q9UQB3; -.
DR PeptideAtlas; Q9UQB3; -.
DR PRIDE; Q9UQB3; -.
DR ProteomicsDB; 85530; -. [Q9UQB3-1]
DR ProteomicsDB; 85531; -. [Q9UQB3-2]
DR Antibodypedia; 9404; 197 antibodies from 30 providers.
DR DNASU; 1501; -.
DR Ensembl; ENST00000304623.13; ENSP00000307134.8; ENSG00000169862.20. [Q9UQB3-1]
DR GeneID; 1501; -.
DR KEGG; hsa:1501; -.
DR MANE-Select; ENST00000304623.13; ENSP00000307134.8; NM_001332.4; NP_001323.1.
DR UCSC; uc003jfa.3; human. [Q9UQB3-1]
DR CTD; 1501; -.
DR DisGeNET; 1501; -.
DR GeneCards; CTNND2; -.
DR HGNC; HGNC:2516; CTNND2.
DR HPA; ENSG00000169862; Tissue enriched (brain).
DR MalaCards; CTNND2; -.
DR MIM; 604275; gene.
DR neXtProt; NX_Q9UQB3; -.
DR OpenTargets; ENSG00000169862; -.
DR Orphanet; 86814; Benign adult familial myoclonic epilepsy.
DR Orphanet; 281; Monosomy 5p.
DR PharmGKB; PA27017; -.
DR VEuPathDB; HostDB:ENSG00000169862; -.
DR eggNOG; KOG1048; Eukaryota.
DR GeneTree; ENSGT00940000154952; -.
DR HOGENOM; CLU_007897_0_0_1; -.
DR InParanoid; Q9UQB3; -.
DR OMA; QHVGTDE; -.
DR OrthoDB; 233858at2759; -.
DR PhylomeDB; Q9UQB3; -.
DR TreeFam; TF321877; -.
DR PathwayCommons; Q9UQB3; -.
DR SignaLink; Q9UQB3; -.
DR SIGNOR; Q9UQB3; -.
DR BioGRID-ORCS; 1501; 8 hits in 1068 CRISPR screens.
DR ChiTaRS; CTNND2; human.
DR GenomeRNAi; 1501; -.
DR Pharos; Q9UQB3; Tbio.
DR PRO; PR:Q9UQB3; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9UQB3; protein.
DR Bgee; ENSG00000169862; Expressed in cortical plate and 146 other tissues.
DR ExpressionAtlas; Q9UQB3; baseline and differential.
DR Genevisible; Q9UQB3; HS.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043204; C:perikaryon; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0008013; F:beta-catenin binding; IPI:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007043; P:cell-cell junction assembly; IBA:GO_Central.
DR GO; GO:0060997; P:dendritic spine morphogenesis; IMP:UniProtKB.
DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0050808; P:synapse organization; IMP:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR028435; Plakophilin/d_Catenin.
DR PANTHER; PTHR10372; PTHR10372; 1.
DR Pfam; PF00514; Arm; 4.
DR SMART; SM00185; ARM; 7.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Autism; Autism spectrum disorder; Cell adhesion;
KW Cell junction; Cell projection; Coiled coil; Developmental protein;
KW Disease variant; Glycoprotein; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Wnt signaling pathway.
FT CHAIN 1..1225
FT /note="Catenin delta-2"
FT /id="PRO_0000064299"
FT REPEAT 394..438
FT /note="ARM 1"
FT REPEAT 540..579
FT /note="ARM 2"
FT REPEAT 582..621
FT /note="ARM 3"
FT REPEAT 626..666
FT /note="ARM 4"
FT REPEAT 682..724
FT /note="ARM 5"
FT REPEAT 728..773
FT /note="ARM 6"
FT REPEAT 835..875
FT /note="ARM 7"
FT REPEAT 882..921
FT /note="ARM 8"
FT REPEAT 975..1018
FT /note="ARM 9"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1042..1077
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 49..84
FT /evidence="ECO:0000255"
FT COMPBIAS 21..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..231
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1042..1075
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 209
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O35927"
FT MOD_RES 264
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O35927"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35927"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35927"
FT MOD_RES 282
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O35927"
FT MOD_RES 296
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O35927"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35927"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35927"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35927"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35927"
FT MOD_RES 514
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35927"
FT MOD_RES 516
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O35927"
FT MOD_RES 1065
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35927"
FT MOD_RES 1076
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35927"
FT VAR_SEQ 823..880
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_006746"
FT VARIANT 34
FT /note="G -> S (probable disease-associated variant found in
FT autism; hypomorphic variant affecting dendritic spines
FT development and maintenance; results in reduced interaction
FT with CTNNB1; dbSNP:rs151129181)"
FT /evidence="ECO:0000269|PubMed:25807484"
FT /id="VAR_073387"
FT VARIANT 189
FT /note="P -> L (probable disease-associated variant found in
FT autism; hypomorphic variant affecting Wnt signaling;
FT dbSNP:rs149573037)"
FT /evidence="ECO:0000269|PubMed:25807484"
FT /id="VAR_073388"
FT VARIANT 224
FT /note="P -> L (probable disease-associated variant found in
FT autism; hypomorphic variant affecting Wnt signaling;
FT dbSNP:rs769623284)"
FT /evidence="ECO:0000269|PubMed:25807484"
FT /id="VAR_073389"
FT VARIANT 275
FT /note="G -> C (found in patients with autism; unknown
FT pathological significance; has no effect on Wnt signaling;
FT dbSNP:rs61749844)"
FT /evidence="ECO:0000269|PubMed:25807484, ECO:0000269|Ref.4"
FT /id="VAR_062270"
FT VARIANT 330
FT /note="R -> H (has no effect on Wnt signaling;
FT dbSNP:rs199506424)"
FT /evidence="ECO:0000269|PubMed:25807484"
FT /id="VAR_073390"
FT VARIANT 454
FT /note="R -> H (probable disease-associated variant found in
FT autism; hypomorphic variant affecting Wnt signaling;
FT dbSNP:rs750266236)"
FT /evidence="ECO:0000269|PubMed:25807484"
FT /id="VAR_073391"
FT VARIANT 465
FT /note="D -> N (has no effect on Wnt signaling;
FT dbSNP:rs200377770)"
FT /evidence="ECO:0000269|PubMed:25807484"
FT /id="VAR_073392"
FT VARIANT 482
FT /note="A -> T (has no effect on Wnt signaling;
FT dbSNP:rs61750706)"
FT /evidence="ECO:0000269|PubMed:25807484, ECO:0000269|Ref.4"
FT /id="VAR_062271"
FT VARIANT 507
FT /note="Q -> P (probable disease-associated variant found in
FT autism; hypomorphic variant affecting Wnt signaling;
FT dbSNP:rs142843736)"
FT /evidence="ECO:0000269|PubMed:25807484"
FT /id="VAR_073393"
FT VARIANT 713
FT /note="R -> C (probable disease-associated variant found in
FT autism; loss-of-function variant affecting dendritic spines
FT development and maintenance; results in reduced interaction
FT with CTNNB1; dbSNP:rs768575356)"
FT /evidence="ECO:0000269|PubMed:25807484"
FT /id="VAR_073394"
FT VARIANT 810
FT /note="G -> R (has no effect on Wnt signaling;
FT dbSNP:rs61754599)"
FT /evidence="ECO:0000269|PubMed:25807484, ECO:0000269|Ref.4"
FT /id="VAR_062272"
FT VARIANT 862
FT /note="T -> M (found in patients with autism; unknown
FT pathological significance; has no effect on Wnt signaling;
FT dbSNP:rs773517967)"
FT /evidence="ECO:0000269|PubMed:25807484"
FT /id="VAR_073395"
FT VARIANT 1159
FT /note="P -> S (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036162"
FT CONFLICT 426
FT /note="D -> V (in Ref. 1; AAC63103)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="D -> V (in Ref. 1; AAC63103)"
FT /evidence="ECO:0000305"
FT CONFLICT 725
FT /note="A -> P (in Ref. 1; AAC63103)"
FT /evidence="ECO:0000305"
FT CONFLICT 894
FT /note="L -> R (in Ref. 1; AAC63103 and 11; AAB96357)"
FT /evidence="ECO:0000305"
FT CONFLICT 909
FT /note="V -> A (in Ref. 1; AAC63103 and 11; AAB96357)"
FT /evidence="ECO:0000305"
FT CONFLICT 980
FT /note="A -> G (in Ref. 8; AAB97957)"
FT /evidence="ECO:0000305"
FT CONFLICT 1102
FT /note="A -> G (in Ref. 7; AAD00453 and 9; AAB68599)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1225 AA; 132656 MW; 4A24ACC3E22BFE83 CRC64;
MFARKPPGAA PLGAMPVPDQ PSSASEKTSS LSPGLNTSNG DGSETETTSA ILASVKEQEL
QFERLTRELE AERQIVASQL ERCKLGSETG SMSSMSSAEE QFQWQSQDGQ KDIEDELTTG
LELVDSCIRS LQESGILDPQ DYSTGERPSL LSQSALQLNS KPEGSFQYPA SYHSNQTLAL
GETTPSQLPA RGTQARATGQ SFSQGTTSRA GHLAGPEPAP PPPPPPREPF APSLGSAFHL
PDAPPAAAAA ALYYSSSTLP APPRGGSPLA APQGGSPTKL QRGGSAPEGA TYAAPRGSSP
KQSPSRLAKS YSTSSPINIV VSSAGLSPIR VTSPPTVQST ISSSPIHQLS STIGTYATLS
PTKRLVHASE QYSKHSQELY ATATLQRPGS LAAGSRASYS SQHGHLGPEL RALQSPEHHI
DPIYEDRVYQ KPPMRSLSQS QGDPLPPAHT GTYRTSTAPS SPGVDSVPLQ RTGSQHGPQN
AAAATFQRAS YAAGPASNYA DPYRQLQYCP SVESPYSKSG PALPPEGTLA RSPSIDSIQK
DPREFGWRDP ELPEVIQMLQ HQFPSVQSNA AAYLQHLCFG DNKIKAEIRR QGGIQLLVDL
LDHRMTEVHR SACGALRNLV YGKANDDNKI ALKNCGGIPA LVRLLRKTTD LEIRELVTGV
LWNLSSCDAL KMPIIQDALA VLTNAVIIPH SGWENSPLQD DRKIQLHSSQ VLRNATGCLR
NVSSAGEEAR RRMRECDGLT DALLYVIQSA LGSSEIDSKT VENCVCILRN LSYRLAAETS
QGQHMGTDEL DGLLCGEANG KDAESSGCWG KKKKKKKSQD QWDGVGPLPD CAEPPKGIQM
LWHPSIVKPY LTLLSECSNP DTLEGAAGAL QNLAAGSWKW SVYIRAAVRK EKGLPILVEL
LRIDNDRVVC AVATALRNMA LDVRNKELIG KYAMRDLVHR LPGGNNSNNT ASKAMSDDTV
TAVCCTLHEV ITKNMENAKA LRDAGGIEKL VGISKSKGDK HSPKVVKAAS QVLNSMWQYR
DLRSLYKKDG WSQYHFVASS STIERDRQRP YSSSRTPSIS PVRVSPNNRS ASAPASPREM
ISLKERKTDY ECTGSNATYH GAKGEHTSRK DAMTAQNTGI STLYRNSYGA PAEDIKHNQV
SAQPVPQEPS RKDYETYQPF QNSTRNYDES FFEDQVHHRP PASEYTMHLG LKSTGNYVDF
YSAARPYSEL NYETSHYPAS PDSWV
