CTNA3_MOUSE
ID CTNA3_MOUSE Reviewed; 895 AA.
AC Q65CL1; Q3UQ61; Q8C0N3;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Catenin alpha-3;
DE AltName: Full=Alpha T-catenin;
DE AltName: Full=Cadherin-associated protein;
GN Name=Ctnna3 {ECO:0000312|MGI:MGI:2661445};
GN Synonyms=Catna3 {ECO:0000312|MGI:MGI:2661445};
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] {ECO:0000312|EMBL:AAQ14965.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart {ECO:0000269|PubMed:12596047};
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 [2] {ECO:0000312|EMBL:BAC26817.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC26817.1};
RC TISSUE=Heart, and Testis {ECO:0000312|EMBL:BAC26817.1};
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 [3] {ECO:0000305}
RP INTERACTION WITH CTNNB1.
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-637, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160; THR-361; SER-637;
RP SER-647 AND THR-649, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Heart, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May be involved in formation of stretch-resistant cell-cell
CC adhesion complexes. {ECO:0000250|UniProtKB:Q9UI47}.
CC -!- SUBUNIT: Interacts with CTNNB1. {ECO:0000269|PubMed:11590244}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC Note=Localizes to intercalated disks of cardiomyocytes and in
CC peritubular myoid cells of testis, and colocalizes with CTNNA1 and
CC CTNNA2. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the vinculin/alpha-catenin family.
CC {ECO:0000255}.
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DR EMBL; AF344871; AAQ14965.1; -; mRNA.
DR EMBL; AK030166; BAC26817.1; -; mRNA.
DR EMBL; AK142745; BAE25182.1; -; mRNA.
DR CCDS; CCDS23901.1; -.
DR RefSeq; NP_001157848.1; NM_001164376.1.
DR RefSeq; NP_808280.2; NM_177612.3.
DR RefSeq; XP_006513538.1; XM_006513475.2.
DR AlphaFoldDB; Q65CL1; -.
DR SMR; Q65CL1; -.
DR BioGRID; 229691; 3.
DR STRING; 10090.ENSMUSP00000101080; -.
DR iPTMnet; Q65CL1; -.
DR PhosphoSitePlus; Q65CL1; -.
DR jPOST; Q65CL1; -.
DR MaxQB; Q65CL1; -.
DR PaxDb; Q65CL1; -.
DR PRIDE; Q65CL1; -.
DR ProteomicsDB; 284056; -.
DR Antibodypedia; 2926; 182 antibodies from 29 providers.
DR DNASU; 216033; -.
DR Ensembl; ENSMUST00000075099; ENSMUSP00000074606; ENSMUSG00000060843.
DR Ensembl; ENSMUST00000105440; ENSMUSP00000101080; ENSMUSG00000060843.
DR Ensembl; ENSMUST00000105441; ENSMUSP00000101081; ENSMUSG00000060843.
DR GeneID; 216033; -.
DR KEGG; mmu:216033; -.
DR UCSC; uc007fkh.2; mouse.
DR CTD; 29119; -.
DR MGI; MGI:2661445; Ctnna3.
DR VEuPathDB; HostDB:ENSMUSG00000060843; -.
DR eggNOG; KOG3681; Eukaryota.
DR GeneTree; ENSGT01030000234543; -.
DR HOGENOM; CLU_015314_2_0_1; -.
DR InParanoid; Q65CL1; -.
DR OMA; SAXDLKS; -.
DR OrthoDB; 953344at2759; -.
DR PhylomeDB; Q65CL1; -.
DR TreeFam; TF313686; -.
DR BioGRID-ORCS; 216033; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Ctnna3; mouse.
DR PRO; PR:Q65CL1; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q65CL1; protein.
DR Bgee; ENSMUSG00000060843; Expressed in interventricular septum and 60 other tissues.
DR Genevisible; Q65CL1; MM.
DR GO; GO:0005912; C:adherens junction; IDA:MGI.
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:MGI.
DR GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IDA:UniProtKB.
DR GO; GO:0090136; P:epithelial cell-cell adhesion; IEA:InterPro.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; ISO:MGI.
DR GO; GO:0098911; P:regulation of ventricular cardiac muscle cell action potential; ISO:MGI.
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; 1.
DR PRINTS; PR00805; ALPHACATENIN.
DR SUPFAM; SSF47220; SSF47220; 4.
PE 1: Evidence at protein level;
KW Cell adhesion; Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..895
FT /note="Catenin alpha-3"
FT /id="PRO_0000064267"
FT REGION 635..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 74..107
FT /evidence="ECO:0000255"
FT COILED 325..379
FT /evidence="ECO:0000255"
FT COMPBIAS 640..660
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 361
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 637
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 647
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 649
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 439
FT /note="E -> K (in Ref. 2; BAC26817)"
FT /evidence="ECO:0000305"
FT CONFLICT 838
FT /note="S -> C (in Ref. 2; BAC26817)"
FT /evidence="ECO:0000305"
FT CONFLICT 869
FT /note="A -> V (in Ref. 2; BAC26817)"
FT /evidence="ECO:0000305"
FT CONFLICT 871
FT /note="V -> A (in Ref. 1; AAQ14965)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 895 AA; 99803 MW; 82355DA239D17A6A CRC64;
MSAETPITLN MDTQDLQIQT FTVEKLLEPL IIQVTTLVNC PQNPSNRKKG RSKRARVLLA
SVEEATWNLL DKGEMIAKEA TVLKEELAAA LQEVRKESKA LKVSAERFTD DPCYLPKREA
VVQAARALLA AVTRLLVLAD MIDVMCLLQH VSSFQRTFES LKNVSNKSDL QRTYQKLGKE
LESLDYLAFK RQQDLKSPSQ RDEIAGARAT LKENSPLLHS ICSACLEHSD VASLKASKDT
VCEEIQNALD VISNASQGIQ NAPAPPEPQA ATLGSAFDEL ENLIVLNPLT VTEEDVRPSL
EKRLEAIISG AALLADSSCT RDLHRERIIA ECNAIRQALQ DLLTEYMSNT GKTERSNTLN
TAIVNMSKKT RDLRRQLRKA IIDHISDSFL DTTVPLLVLI EAAKNGRVKE IKDYAAIFHE
HTGRLVEVAN LACSMSTNED GIKIVRIAAN HLETLCPQII NAALALASRP KSQVVKNTME
MYKRTWEHYI HVLTEAVDDI TSIDDFLAVS ESHILEDVNK CIIALRDQDA DNLDRAAGAI
RGRAARVAHI VAGEMDSYEP GAYTEGVMRN VNFLTSTVIP EFVTQVNVAL DALSKNSLTA
LDDNQFVDIS KKIYDTIHDI RCSVMMIRTP EELEDVSDLE DDHEVRSHTS IQTEGKTDRA
KMTQLPEAEK EKIAEQVADF KKVKSKLDAE IEIWDDTSND IIVLAKKMCM IMMEMTDFTR
GKGPLKHTTD VIYAAKMISE SGSRMDVLAR QIANQCPDPP CKQDLLAYLE QIKFYSHQLK
ICSQVKAEIQ NLGGELIVSA LDSVTSLIQA AKNLMNAVVQ TVKMSYIAST KIIRIQSSAG
PRHPVVMWRM KAPAKKPLIK REKPEETWAA VRRGSAKKKI HPVQVMSEFR GRQVY
