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Protein

Catenin alpha-3

Gene

Ctnna3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May be involved in formation of stretch-resistant cell-cell adhesion complexes.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Names & Taxonomyi

Protein namesi
Recommended name:
Catenin alpha-3
Alternative name(s):
Alpha T-catenin
Cadherin-associated protein
Gene namesi
Name:Ctnna3Imported
Synonyms:Catna3Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:2661445. Ctnna3.

Subcellular locationi

  • Cytoplasmcytoskeleton By similarity

  • Note: Localizes to intercalated disks of cardiomyocytes and in peritubular myoid cells of testis, and colocalizes with CTNNA1 and CTNNA2.By similarity

GO - Cellular componenti

  • adherens junction Source: MGI
  • cytoplasm Source: UniProtKB-KW
  • cytoskeleton Source: UniProtKB-SubCell
  • fascia adherens Source: UniProtKB
  • lamellipodium Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 895895Catenin alpha-3PRO_0000064267Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei160 – 1601PhosphoserineCombined sources
Modified residuei361 – 3611PhosphothreonineCombined sources
Modified residuei637 – 6371PhosphoserineCombined sources
Modified residuei647 – 6471PhosphoserineCombined sources
Modified residuei649 – 6491PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ65CL1.
MaxQBiQ65CL1.
PaxDbiQ65CL1.
PRIDEiQ65CL1.

PTM databases

iPTMnetiQ65CL1.
PhosphoSiteiQ65CL1.

Expressioni

Gene expression databases

BgeeiQ65CL1.
CleanExiMM_CTNNA3.
GenevisibleiQ65CL1. MM.

Interactioni

Subunit structurei

Interacts with CTNNB1.1 Publication

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000074606.

Structurei

3D structure databases

ProteinModelPortaliQ65CL1.
SMRiQ65CL1. Positions 17-867.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili74 – 10734Sequence analysisAdd
BLAST
Coiled coili325 – 37955Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the vinculin/alpha-catenin family.Sequence analysis

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG3681. Eukaryota.
ENOG410XSRU. LUCA.
GeneTreeiENSGT00550000074411.
HOGENOMiHOG000280724.
HOVERGENiHBG000069.
InParanoidiQ65CL1.
KOiK05691.
OMAiAFKRQQD.
OrthoDBiEOG7HQN7B.
PhylomeDBiQ65CL1.
TreeFamiTF313686.

Family and domain databases

InterProiIPR001033. Alpha_catenin.
IPR030044. CTNNA3.
IPR006077. Vinculin/catenin.
[Graphical view]
PANTHERiPTHR18914. PTHR18914. 1 hit.
PTHR18914:SF21. PTHR18914:SF21. 1 hit.
PfamiPF01044. Vinculin. 2 hits.
[Graphical view]
PRINTSiPR00805. ALPHACATENIN.
SUPFAMiSSF47220. SSF47220. 4 hits.

Sequencei

Sequence statusi: Complete.

Q65CL1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAETPITLN MDTQDLQIQT FTVEKLLEPL IIQVTTLVNC PQNPSNRKKG
60 70 80 90 100
RSKRARVLLA SVEEATWNLL DKGEMIAKEA TVLKEELAAA LQEVRKESKA
110 120 130 140 150
LKVSAERFTD DPCYLPKREA VVQAARALLA AVTRLLVLAD MIDVMCLLQH
160 170 180 190 200
VSSFQRTFES LKNVSNKSDL QRTYQKLGKE LESLDYLAFK RQQDLKSPSQ
210 220 230 240 250
RDEIAGARAT LKENSPLLHS ICSACLEHSD VASLKASKDT VCEEIQNALD
260 270 280 290 300
VISNASQGIQ NAPAPPEPQA ATLGSAFDEL ENLIVLNPLT VTEEDVRPSL
310 320 330 340 350
EKRLEAIISG AALLADSSCT RDLHRERIIA ECNAIRQALQ DLLTEYMSNT
360 370 380 390 400
GKTERSNTLN TAIVNMSKKT RDLRRQLRKA IIDHISDSFL DTTVPLLVLI
410 420 430 440 450
EAAKNGRVKE IKDYAAIFHE HTGRLVEVAN LACSMSTNED GIKIVRIAAN
460 470 480 490 500
HLETLCPQII NAALALASRP KSQVVKNTME MYKRTWEHYI HVLTEAVDDI
510 520 530 540 550
TSIDDFLAVS ESHILEDVNK CIIALRDQDA DNLDRAAGAI RGRAARVAHI
560 570 580 590 600
VAGEMDSYEP GAYTEGVMRN VNFLTSTVIP EFVTQVNVAL DALSKNSLTA
610 620 630 640 650
LDDNQFVDIS KKIYDTIHDI RCSVMMIRTP EELEDVSDLE DDHEVRSHTS
660 670 680 690 700
IQTEGKTDRA KMTQLPEAEK EKIAEQVADF KKVKSKLDAE IEIWDDTSND
710 720 730 740 750
IIVLAKKMCM IMMEMTDFTR GKGPLKHTTD VIYAAKMISE SGSRMDVLAR
760 770 780 790 800
QIANQCPDPP CKQDLLAYLE QIKFYSHQLK ICSQVKAEIQ NLGGELIVSA
810 820 830 840 850
LDSVTSLIQA AKNLMNAVVQ TVKMSYIAST KIIRIQSSAG PRHPVVMWRM
860 870 880 890
KAPAKKPLIK REKPEETWAA VRRGSAKKKI HPVQVMSEFR GRQVY
Length:895
Mass (Da):99,803
Last modified:October 25, 2005 - v2
Checksum:i82355DA239D17A6A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti439 – 4391E → K in BAC26817 (PubMed:16141072).Curated
Sequence conflicti838 – 8381S → C in BAC26817 (PubMed:16141072).Curated
Sequence conflicti869 – 8691A → V in BAC26817 (PubMed:16141072).Curated
Sequence conflicti871 – 8711V → A in AAQ14965 (PubMed:12596047).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF344871 mRNA. Translation: AAQ14965.1.
AK030166 mRNA. Translation: BAC26817.1.
AK142745 mRNA. Translation: BAE25182.1.
CCDSiCCDS23901.1.
RefSeqiNP_001157848.1. NM_001164376.1.
NP_808280.2. NM_177612.3.
XP_006513538.1. XM_006513475.1.
XP_006513539.1. XM_006513476.2.
UniGeneiMm.444692.
Mm.483238.

Genome annotation databases

EnsembliENSMUST00000075099; ENSMUSP00000074606; ENSMUSG00000060843.
ENSMUST00000105440; ENSMUSP00000101080; ENSMUSG00000060843.
ENSMUST00000105441; ENSMUSP00000101081; ENSMUSG00000060843.
GeneIDi216033.
KEGGimmu:216033.
UCSCiuc007fkh.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF344871 mRNA. Translation: AAQ14965.1.
AK030166 mRNA. Translation: BAC26817.1.
AK142745 mRNA. Translation: BAE25182.1.
CCDSiCCDS23901.1.
RefSeqiNP_001157848.1. NM_001164376.1.
NP_808280.2. NM_177612.3.
XP_006513538.1. XM_006513475.1.
XP_006513539.1. XM_006513476.2.
UniGeneiMm.444692.
Mm.483238.

3D structure databases

ProteinModelPortaliQ65CL1.
SMRiQ65CL1. Positions 17-867.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000074606.

PTM databases

iPTMnetiQ65CL1.
PhosphoSiteiQ65CL1.

Proteomic databases

EPDiQ65CL1.
MaxQBiQ65CL1.
PaxDbiQ65CL1.
PRIDEiQ65CL1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000075099; ENSMUSP00000074606; ENSMUSG00000060843.
ENSMUST00000105440; ENSMUSP00000101080; ENSMUSG00000060843.
ENSMUST00000105441; ENSMUSP00000101081; ENSMUSG00000060843.
GeneIDi216033.
KEGGimmu:216033.
UCSCiuc007fkh.2. mouse.

Organism-specific databases

CTDi29119.
MGIiMGI:2661445. Ctnna3.

Phylogenomic databases

eggNOGiKOG3681. Eukaryota.
ENOG410XSRU. LUCA.
GeneTreeiENSGT00550000074411.
HOGENOMiHOG000280724.
HOVERGENiHBG000069.
InParanoidiQ65CL1.
KOiK05691.
OMAiAFKRQQD.
OrthoDBiEOG7HQN7B.
PhylomeDBiQ65CL1.
TreeFamiTF313686.

Miscellaneous databases

ChiTaRSiCtnna3. mouse.
PROiQ65CL1.
SOURCEiSearch...

Gene expression databases

BgeeiQ65CL1.
CleanExiMM_CTNNA3.
GenevisibleiQ65CL1. MM.

Family and domain databases

InterProiIPR001033. Alpha_catenin.
IPR030044. CTNNA3.
IPR006077. Vinculin/catenin.
[Graphical view]
PANTHERiPTHR18914. PTHR18914. 1 hit.
PTHR18914:SF21. PTHR18914:SF21. 1 hit.
PfamiPF01044. Vinculin. 2 hits.
[Graphical view]
PRINTSiPR00805. ALPHACATENIN.
SUPFAMiSSF47220. SSF47220. 4 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Assessment of the CTNNA3 gene encoding human alpha T-catenin regarding its involvement in dilated cardiomyopathy."
    Janssens B., Mohapatra B., Vatta M., Goossens S., Vanpoucke G., Kools P., Montoye T., van Hengel J., Bowles N.E., van Roy F., Towbin J.A.
    Hum. Genet. 112:227-236(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Heart1 Publication.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6JImported.
    Tissue: Heart and TestisImported.
  3. "AlphaT-catenin: a novel tissue-specific beta-catenin-binding protein mediating strong cell-cell adhesion."
    Janssens B., Goossens S., Staes K., Gilbert B., van Hengel J., Colpaert C., Bruyneel E., Mareel M., van Roy F.
    J. Cell Sci. 114:3177-3188(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CTNNB1.
  4. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-637, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160; THR-361; SER-637; SER-647 AND THR-649, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Lung, Spleen and Testis.

Entry informationi

Entry nameiCTNA3_MOUSE
AccessioniPrimary (citable) accession number: Q65CL1
Secondary accession number(s): Q3UQ61, Q8C0N3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 25, 2005
Last modified: June 8, 2016
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.