CTNA3_HUMAN
ID CTNA3_HUMAN Reviewed; 895 AA.
AC Q9UI47; Q5VSR2; Q6P056;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Catenin alpha-3;
DE AltName: Full=Alpha T-catenin;
DE AltName: Full=Cadherin-associated protein;
GN Name=CTNNA3 {ECO:0000312|EMBL:AAF21801.1, ECO:0000312|HGNC:HGNC:2511};
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] {ECO:0000305, ECO:0000312|EMBL:AAF21801.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH CTNNB1,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Testis {ECO:0000269|PubMed:11590244};
RX PubMed=11590244; DOI=10.1242/jcs.114.17.3177;
RA Janssens B., Goossens S., Staes K., Gilbert B., van Hengel J., Colpaert C.,
RA Bruyneel E., Mareel M., van Roy F.;
RT "AlphaT-catenin: a novel tissue-specific beta-catenin-binding protein
RT mediating strong cell-cell adhesion.";
RL J. Cell Sci. 114:3177-3188(2001).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAQ14328.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=12596047; DOI=10.1007/s00439-002-0857-5;
RA Janssens B., Mohapatra B., Vatta M., Goossens S., Vanpoucke G., Kools P.,
RA Montoye T., van Hengel J., Bowles N.E., van Roy F., Towbin J.A.;
RT "Assessment of the CTNNA3 gene encoding human alpha T-catenin regarding its
RT involvement in dilated cardiomyopathy.";
RL Hum. Genet. 112:227-236(2003).
RN [3] {ECO:0000312|EMBL:AL731549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAH65819.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=PNS {ECO:0000312|EMBL:AAH65819.1};
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-637, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56 AND SER-637, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [7]
RP VARIANT ARVD13 ASP-94.
RX PubMed=23136403; DOI=10.1093/eurheartj/ehs373;
RA van Hengel J., Calore M., Bauce B., Dazzo E., Mazzotti E., De Bortoli M.,
RA Lorenzon A., Li Mura I.E., Beffagna G., Rigato I., Vleeschouwers M.,
RA Tyberghein K., Hulpiau P., van Hamme E., Zaglia T., Corrado D., Basso C.,
RA Thiene G., Daliento L., Nava A., van Roy F., Rampazzo A.;
RT "Mutations in the area composita protein alphaT-catenin are associated with
RT arrhythmogenic right ventricular cardiomyopathy.";
RL Eur. Heart J. 34:201-210(2013).
CC -!- FUNCTION: May be involved in formation of stretch-resistant cell-cell
CC adhesion complexes. {ECO:0000303|PubMed:11590244}.
CC -!- SUBUNIT: Interacts with CTNNB1. {ECO:0000269|PubMed:11590244}.
CC -!- INTERACTION:
CC Q9UI47; PRO_0000038596 [P04591]: gag; Xeno; NbExp=2; IntAct=EBI-3937546, EBI-6179727;
CC Q9UI47-1; P35222: CTNNB1; NbExp=4; IntAct=EBI-21980640, EBI-491549;
CC Q9UI47-2; Q6PJH3: AKAP9; NbExp=3; IntAct=EBI-11962928, EBI-11745576;
CC Q9UI47-2; Q86SG2: ANKRD23; NbExp=3; IntAct=EBI-11962928, EBI-5661893;
CC Q9UI47-2; Q9BQD7: ANTKMT; NbExp=3; IntAct=EBI-11962928, EBI-713602;
CC Q9UI47-2; Q9Y6H3: ATP23; NbExp=3; IntAct=EBI-11962928, EBI-12811889;
CC Q9UI47-2; Q6QNY1: BLOC1S2; NbExp=3; IntAct=EBI-11962928, EBI-465872;
CC Q9UI47-2; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-11962928, EBI-2548012;
CC Q9UI47-2; Q8WW18: C17orf50; NbExp=3; IntAct=EBI-11962928, EBI-12877892;
CC Q9UI47-2; G5E9W6: CCDC183; NbExp=3; IntAct=EBI-11962928, EBI-17212717;
CC Q9UI47-2; Q8N2Z9: CENPS; NbExp=3; IntAct=EBI-11962928, EBI-5529649;
CC Q9UI47-2; P12532: CKMT1B; NbExp=3; IntAct=EBI-11962928, EBI-1050662;
CC Q9UI47-2; Q9NRP2: CMC2; NbExp=3; IntAct=EBI-11962928, EBI-16780661;
CC Q9UI47-2; Q9H9E3: COG4; NbExp=3; IntAct=EBI-11962928, EBI-368382;
CC Q9UI47-2; O43186: CRX; NbExp=3; IntAct=EBI-11962928, EBI-748171;
CC Q9UI47-2; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-11962928, EBI-742054;
CC Q9UI47-2; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-11962928, EBI-11988027;
CC Q9UI47-2; Q9BQ95: ECSIT; NbExp=3; IntAct=EBI-11962928, EBI-712452;
CC Q9UI47-2; Q96D98: EID2B; NbExp=3; IntAct=EBI-11962928, EBI-724968;
CC Q9UI47-2; Q96A65-2: EXOC4; NbExp=3; IntAct=EBI-11962928, EBI-17869840;
CC Q9UI47-2; Q9BQ89: FAM110A; NbExp=3; IntAct=EBI-11962928, EBI-1752811;
CC Q9UI47-2; Q3B820: FAM161A; NbExp=3; IntAct=EBI-11962928, EBI-719941;
CC Q9UI47-2; Q96MY7: FAM161B; NbExp=3; IntAct=EBI-11962928, EBI-7225287;
CC Q9UI47-2; Q8IZU1: FAM9A; NbExp=3; IntAct=EBI-11962928, EBI-8468186;
CC Q9UI47-2; Q9NVF7: FBXO28; NbExp=3; IntAct=EBI-11962928, EBI-740282;
CC Q9UI47-2; Q9BRX5: GINS3; NbExp=3; IntAct=EBI-11962928, EBI-2857315;
CC Q9UI47-2; P62873: GNB1; NbExp=3; IntAct=EBI-11962928, EBI-357130;
CC Q9UI47-2; Q7Z353: HDX; NbExp=3; IntAct=EBI-11962928, EBI-1052734;
CC Q9UI47-2; P14923: JUP; NbExp=3; IntAct=EBI-11962928, EBI-702484;
CC Q9UI47-2; Q9BW62: KATNAL1; NbExp=3; IntAct=EBI-11962928, EBI-743591;
CC Q9UI47-2; Q14847-2: LASP1; NbExp=3; IntAct=EBI-11962928, EBI-9088686;
CC Q9UI47-2; Q9H992: MARCHF7; NbExp=3; IntAct=EBI-11962928, EBI-949983;
CC Q9UI47-2; Q8WWY6: MBD3L1; NbExp=3; IntAct=EBI-11962928, EBI-12516603;
CC Q9UI47-2; P59942: MCCD1; NbExp=3; IntAct=EBI-11962928, EBI-11987923;
CC Q9UI47-2; O00566: MPHOSPH10; NbExp=3; IntAct=EBI-11962928, EBI-5235884;
CC Q9UI47-2; Q9UJ68: MSRA; NbExp=3; IntAct=EBI-11962928, EBI-19157918;
CC Q9UI47-2; P15173: MYOG; NbExp=3; IntAct=EBI-11962928, EBI-3906629;
CC Q9UI47-2; Q15742: NAB2; NbExp=3; IntAct=EBI-11962928, EBI-8641936;
CC Q9UI47-2; P17568: NDUFB7; NbExp=3; IntAct=EBI-11962928, EBI-1246238;
CC Q9UI47-2; O43482: OIP5; NbExp=3; IntAct=EBI-11962928, EBI-536879;
CC Q9UI47-2; Q13416: ORC2; NbExp=3; IntAct=EBI-11962928, EBI-374957;
CC Q9UI47-2; P26367: PAX6; NbExp=3; IntAct=EBI-11962928, EBI-747278;
CC Q9UI47-2; Q9UPG8: PLAGL2; NbExp=3; IntAct=EBI-11962928, EBI-2876622;
CC Q9UI47-2; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-11962928, EBI-302345;
CC Q9UI47-2; Q96PV4: PNMA5; NbExp=3; IntAct=EBI-11962928, EBI-10171633;
CC Q9UI47-2; P78424: POU6F2; NbExp=3; IntAct=EBI-11962928, EBI-12029004;
CC Q9UI47-2; P85299-2: PRR5; NbExp=3; IntAct=EBI-11962928, EBI-12944296;
CC Q9UI47-2; Q04864-2: REL; NbExp=3; IntAct=EBI-11962928, EBI-10829018;
CC Q9UI47-2; Q0D2K3: RIPPLY1; NbExp=3; IntAct=EBI-11962928, EBI-10226430;
CC Q9UI47-2; P32969: RPL9P9; NbExp=3; IntAct=EBI-11962928, EBI-358122;
CC Q9UI47-2; O75582: RPS6KA5; NbExp=3; IntAct=EBI-11962928, EBI-73869;
CC Q9UI47-2; Q14140: SERTAD2; NbExp=3; IntAct=EBI-11962928, EBI-2822051;
CC Q9UI47-2; Q9UJW9: SERTAD3; NbExp=3; IntAct=EBI-11962928, EBI-748621;
CC Q9UI47-2; Q496A3: SPATS1; NbExp=3; IntAct=EBI-11962928, EBI-3923692;
CC Q9UI47-2; Q93045: STMN2; NbExp=3; IntAct=EBI-11962928, EBI-714194;
CC Q9UI47-2; Q9NZ72: STMN3; NbExp=3; IntAct=EBI-11962928, EBI-725557;
CC Q9UI47-2; Q5VWN6: TASOR2; NbExp=3; IntAct=EBI-11962928, EBI-745958;
CC Q9UI47-2; O43711: TLX3; NbExp=3; IntAct=EBI-11962928, EBI-3939165;
CC Q9UI47-2; P19237: TNNI1; NbExp=3; IntAct=EBI-11962928, EBI-746692;
CC Q9UI47-2; P48788: TNNI2; NbExp=3; IntAct=EBI-11962928, EBI-7746394;
CC Q9UI47-2; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-11962928, EBI-2130429;
CC Q9UI47-2; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-11962928, EBI-9090990;
CC Q9UI47-2; Q6F5E7: TXNRD3NB; NbExp=3; IntAct=EBI-11962928, EBI-18122152;
CC Q9UI47-2; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-11962928, EBI-739895;
CC Q9UI47-2; P01282-2: VIP; NbExp=3; IntAct=EBI-11962928, EBI-12320391;
CC Q9UI47-2; O60844: ZG16; NbExp=3; IntAct=EBI-11962928, EBI-746479;
CC Q9UI47-2; Q8N5A5-2: ZGPAT; NbExp=3; IntAct=EBI-11962928, EBI-10183064;
CC Q9UI47-2; P17023: ZNF19; NbExp=3; IntAct=EBI-11962928, EBI-12884200;
CC Q9UI47-2; Q9BUY5: ZNF426; NbExp=3; IntAct=EBI-11962928, EBI-743265;
CC Q9UI47-2; Q6S9Z5: ZNF474; NbExp=3; IntAct=EBI-11962928, EBI-17269964;
CC Q9UI47-2; Q9H707: ZNF552; NbExp=3; IntAct=EBI-11962928, EBI-2555731;
CC Q9UI47-2; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-11962928, EBI-4395669;
CC Q9UI47-2; Q6ZS27-3: ZNF662; NbExp=3; IntAct=EBI-11962928, EBI-10255155;
CC Q9UI47-2; A0A1U9X8X8; NbExp=3; IntAct=EBI-11962928, EBI-17234977;
CC Q9UI47-2; Q6ZN96; NbExp=3; IntAct=EBI-11962928, EBI-10255097;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC Note=Localizes to intercalated disks of cardiomyocytes and in
CC peritubular myoid cells of testis, and colocalizes with CTNNA1 and
CC CTNNA2. {ECO:0000269|PubMed:11590244}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:11590244};
CC IsoId=Q9UI47-1; Sequence=Displayed;
CC Name=2 {ECO:0000305};
CC IsoId=Q9UI47-2; Sequence=VSP_051852, VSP_051853;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in heart and testis.
CC Expressed at lower levels in brain, kidney, liver and skeletal muscle.
CC {ECO:0000269|PubMed:11590244}.
CC -!- DISEASE: Arrhythmogenic right ventricular dysplasia, familial, 13
CC (ARVD13) [MIM:615616]: A congenital heart disease characterized by
CC infiltration of adipose and fibrous tissue into the right ventricle and
CC loss of myocardial cells, resulting in ventricular and supraventricular
CC arrhythmias. {ECO:0000269|PubMed:23136403}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the vinculin/alpha-catenin family.
CC {ECO:0000255}.
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DR EMBL; AF091606; AAF21801.1; -; mRNA.
DR EMBL; AF282692; AAQ14328.1; -; Genomic_DNA.
DR EMBL; AF282679; AAQ14328.1; JOINED; Genomic_DNA.
DR EMBL; AF282680; AAQ14328.1; JOINED; Genomic_DNA.
DR EMBL; AF282681; AAQ14328.1; JOINED; Genomic_DNA.
DR EMBL; AF282683; AAQ14328.1; JOINED; Genomic_DNA.
DR EMBL; AF282685; AAQ14328.1; JOINED; Genomic_DNA.
DR EMBL; AF282689; AAQ14328.1; JOINED; Genomic_DNA.
DR EMBL; AF391793; AAQ14328.1; JOINED; Genomic_DNA.
DR EMBL; AF282686; AAQ14328.1; JOINED; Genomic_DNA.
DR EMBL; AF282688; AAQ14328.1; JOINED; Genomic_DNA.
DR EMBL; AF282690; AAQ14328.1; JOINED; Genomic_DNA.
DR EMBL; AF282691; AAQ14328.1; JOINED; Genomic_DNA.
DR EMBL; AF391792; AAQ14328.1; JOINED; Genomic_DNA.
DR EMBL; AF391794; AAQ14328.1; JOINED; Genomic_DNA.
DR EMBL; AF282687; AAQ14328.1; JOINED; Genomic_DNA.
DR EMBL; AF282682; AAQ14328.1; JOINED; Genomic_DNA.
DR EMBL; AF282684; AAQ14328.1; JOINED; Genomic_DNA.
DR EMBL; AC016819; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC018979; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC020642; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC022017; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC022401; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC026394; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL607022; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL607023; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL731538; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL731549; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC065819; AAH65819.1; -; mRNA.
DR CCDS; CCDS7269.1; -. [Q9UI47-1]
DR RefSeq; NP_001120856.1; NM_001127384.2. [Q9UI47-1]
DR RefSeq; NP_037398.2; NM_013266.3. [Q9UI47-1]
DR AlphaFoldDB; Q9UI47; -.
DR SMR; Q9UI47; -.
DR BioGRID; 118885; 116.
DR IntAct; Q9UI47; 102.
DR STRING; 9606.ENSP00000389714; -.
DR iPTMnet; Q9UI47; -.
DR PhosphoSitePlus; Q9UI47; -.
DR SwissPalm; Q9UI47; -.
DR BioMuta; CTNNA3; -.
DR DMDM; 78099215; -.
DR EPD; Q9UI47; -.
DR jPOST; Q9UI47; -.
DR MassIVE; Q9UI47; -.
DR MaxQB; Q9UI47; -.
DR PaxDb; Q9UI47; -.
DR PeptideAtlas; Q9UI47; -.
DR PRIDE; Q9UI47; -.
DR ProteomicsDB; 84475; -. [Q9UI47-1]
DR ProteomicsDB; 84476; -. [Q9UI47-2]
DR Antibodypedia; 2926; 182 antibodies from 29 providers.
DR DNASU; 29119; -.
DR Ensembl; ENST00000433211.7; ENSP00000389714.1; ENSG00000183230.18. [Q9UI47-1]
DR Ensembl; ENST00000682758.1; ENSP00000508047.1; ENSG00000183230.18. [Q9UI47-1]
DR Ensembl; ENST00000684154.1; ENSP00000508371.1; ENSG00000183230.18. [Q9UI47-1]
DR GeneID; 29119; -.
DR KEGG; hsa:29119; -.
DR MANE-Select; ENST00000433211.7; ENSP00000389714.1; NM_013266.4; NP_037398.2.
DR UCSC; uc001jmw.3; human. [Q9UI47-1]
DR CTD; 29119; -.
DR DisGeNET; 29119; -.
DR GeneCards; CTNNA3; -.
DR HGNC; HGNC:2511; CTNNA3.
DR HPA; ENSG00000183230; Tissue enriched (brain).
DR MalaCards; CTNNA3; -.
DR MIM; 607667; gene.
DR MIM; 615616; phenotype.
DR neXtProt; NX_Q9UI47; -.
DR OpenTargets; ENSG00000183230; -.
DR Orphanet; 293899; Familial isolated arrhythmogenic ventricular dysplasia, biventricular form.
DR Orphanet; 293888; Familial isolated arrhythmogenic ventricular dysplasia, left dominant form.
DR Orphanet; 293910; Familial isolated arrhythmogenic ventricular dysplasia, right dominant form.
DR PharmGKB; PA27010; -.
DR VEuPathDB; HostDB:ENSG00000183230; -.
DR eggNOG; KOG3681; Eukaryota.
DR GeneTree; ENSGT01030000234543; -.
DR HOGENOM; CLU_015314_2_0_1; -.
DR InParanoid; Q9UI47; -.
DR OMA; SAXDLKS; -.
DR OrthoDB; 953344at2759; -.
DR PhylomeDB; Q9UI47; -.
DR TreeFam; TF313686; -.
DR PathwayCommons; Q9UI47; -.
DR SignaLink; Q9UI47; -.
DR SIGNOR; Q9UI47; -.
DR BioGRID-ORCS; 29119; 8 hits in 1065 CRISPR screens.
DR ChiTaRS; CTNNA3; human.
DR GenomeRNAi; 29119; -.
DR Pharos; Q9UI47; Tbio.
DR PRO; PR:Q9UI47; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9UI47; protein.
DR Bgee; ENSG00000183230; Expressed in corpus callosum and 151 other tissues.
DR ExpressionAtlas; Q9UI47; baseline and differential.
DR Genevisible; Q9UI47; HS.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:InterPro.
DR GO; GO:0005916; C:fascia adherens; IDA:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0008013; F:beta-catenin binding; IPI:BHF-UCL.
DR GO; GO:0045296; F:cadherin binding; TAS:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; IEA:InterPro.
DR GO; GO:0086073; P:bundle of His cell-Purkinje myocyte adhesion involved in cell communication; IMP:BHF-UCL.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IPI:UniProtKB.
DR GO; GO:0090136; P:epithelial cell-cell adhesion; IEA:InterPro.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IMP:BHF-UCL.
DR GO; GO:0098911; P:regulation of ventricular cardiac muscle cell action potential; IMP:BHF-UCL.
DR InterPro; IPR036723; Alpha-catenin/vinculin-like_sf.
DR InterPro; IPR001033; Alpha_catenin.
DR InterPro; IPR030047; CTNNA1/CTNNA3.
DR InterPro; IPR006077; Vinculin/catenin.
DR PANTHER; PTHR18914:SF24; PTHR18914:SF24; 1.
DR Pfam; PF01044; Vinculin; 2.
DR PRINTS; PR00805; ALPHACATENIN.
DR SUPFAM; SSF47220; SSF47220; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Cardiomyopathy; Cell adhesion; Coiled coil;
KW Cytoplasm; Cytoskeleton; Disease variant; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..895
FT /note="Catenin alpha-3"
FT /id="PRO_0000064266"
FT COILED 74..111
FT /evidence="ECO:0000255"
FT COILED 325..379
FT /evidence="ECO:0000255"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q65CL1"
FT MOD_RES 637
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 647
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q65CL1"
FT MOD_RES 649
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q65CL1"
FT VAR_SEQ 511..516
FT /note="ESHILE -> GMFLFF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_051852"
FT VAR_SEQ 517..895
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_051853"
FT VARIANT 94
FT /note="V -> D (in ARVD13; dbSNP:rs587777134)"
FT /evidence="ECO:0000269|PubMed:23136403"
FT /id="VAR_070998"
FT VARIANT 535
FT /note="R -> C (in dbSNP:rs41274090)"
FT /id="VAR_062093"
FT VARIANT 596
FT /note="S -> N (in dbSNP:rs4548513)"
FT /id="VAR_053369"
FT CONFLICT 160
FT /note="S -> T (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 895 AA; 99809 MW; 269E6DFB4956BDFE CRC64;
MSAETPITLN IDPQDLQVQT FTVEKLLEPL IIQVTTLVNC PQNPSSRKKG RSKRASVLLA
SVEEATWNLL DKGEKIAQEA TVLKDELTAS LEEVRKESEA LKVSAERFTD DPCFLPKREA
VVQAARALLA AVTRLLILAD MIDVMCLLQH VSAFQRTFES LKNVANKSDL QKTYQKLGKE
LENLDYLAFK RQQDLKSPNQ RDEIAGARAS LKENSPLLHS ICSACLEHSD VASLKASKDT
VCEEIQNALN VISNASQGIQ NMTTPPEPQA ATLGSALDEL ENLIVLNPLT VTEEEIRPSL
EKRLEAIISG AALLADSSCT RDLHRERIIA ECNAIRQALQ DLLSEYMNNA GKKERSNTLN
IALDNMCKKT RDLRRQLRKA IIDHVSDSFL DTTVPLLVLI EAAKNGREKE IKEYAAIFHE
HTSRLVEVAN LACSMSTNED GIKIVKIAAN HLETLCPQII NAALALAARP KSQAVKNTME
MYKRTWENHI HVLTEAVDDI TSIDDFLAVS ESHILEDVNK CIIALRDQDA DNLDRAAGAI
RGRAARVAHI VTGEMDSYEP GAYTEGVMRN VNFLTSTVIP EFVTQVNVAL EALSKSSLNV
LDDNQFVDIS KKIYDTIHDI RCSVMMIRTP EELEDVSDLE EEHEVRSHTS IQTEGKTDRA
KMTQLPEAEK EKIAEQVADF KKVKSKLDAE IEIWDDTSND IIVLAKNMCM IMMEMTDFTR
GKGPLKHTTD VIYAAKMISE SGSRMDVLAR QIANQCPDPS CKQDLLAYLE QIKFYSHQLK
ICSQVKAEIQ NLGGELIMSA LDSVTSLIQA AKNLMNAVVQ TVKMSYIAST KIIRIQSPAG
PRHPVVMWRM KAPAKKPLIK REKPEETCAA VRRGSAKKKI HPLQVMSEFR GRQIY
