CTNA2_HUMAN
ID CTNA2_HUMAN Reviewed; 953 AA.
AC P26232; B3KXE5; B7Z2W7; B7Z352; B7Z898; Q4ZFW1; Q53R26; Q53R33; Q53T67;
AC Q53T71; Q53TM8; Q7Z3L1; Q7Z3Y0;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 5.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Catenin alpha-2;
DE AltName: Full=Alpha N-catenin;
DE AltName: Full=Alpha-catenin-related protein;
GN Name=CTNNA2; Synonyms=CAPR;
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).
RC TISSUE=Brain;
RX PubMed=8432524; DOI=10.1006/geno.1993.1004;
RA Claverie J.-M., Hardelin J.-P., Legouis R., Levilliers J., Bougueleret L.,
RA Mattei M.-G., Petit C.;
RT "Characterization and chromosomal assignment of a human cDNA encoding a
RT protein related to the murine 102-kDa cadherin-associated protein (alpha-
RT catenin).";
RL Genomics 15:13-20(1993).
RN [2]
RP SEQUENCE REVISION TO C-TERMINUS.
RA Hardelin J.-P.;
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4 AND 5).
RC TISSUE=Brain, Hippocampus, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC TISSUE=Hippocampus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=PNS;
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 [8]
RP INTERACTION WITH ZNF639, AND SUBCELLULAR LOCATION.
RX PubMed=16182284; DOI=10.1016/j.yexcr.2005.06.018;
RA Bogaerts S., Vanlandschoot A., van Hengel J., van Roy F.;
RT "Nuclear translocation of alphaN-catenin by the novel zinc finger
RT transcriptional repressor ZASC1.";
RL Exp. Cell Res. 311:1-13(2005).
RN [9]
RP ALTERNATIVE SPLICING (ISOFORM 6).
RX PubMed=18163523; DOI=10.1002/ajmg.b.30679;
RA Mexal S., Berger R., Pearce L., Barton A., Logel J., Adams C.E., Ross R.G.,
RA Freedman R., Leonard S.;
RT "Regulation of a novel alphaN-catenin splice variant in schizophrenic
RT smokers.";
RL Am. J. Med. Genet. B Neuropsychiatr. Genet. 147:759-768(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-640, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP FUNCTION, INTERACTION WITH F-ACTIN, TISSUE SPECIFICITY, INVOLVEMENT IN
RP CDCBM9, VARIANTS CDCBM9 494-ARG--PHE-953 DEL; 781-ARG--PHE-953 DEL AND
RP 930-ARG--PHE-953 DEL, AND CHARACTERIZATION OF VARIANT CDCBM9
RP 781-ARG--PHE-953 DEL.
RX PubMed=30013181; DOI=10.1038/s41588-018-0166-0;
RA Schaffer A.E., Breuss M.W., Caglayan A.O., Al-Sanaa N., Al-Abdulwahed H.Y.,
RA Kaymakcalan H., Yilmaz C., Zaki M.S., Rosti R.O., Copeland B., Baek S.T.,
RA Musaev D., Scott E.C., Ben-Omran T., Kariminejad A., Kayserili H.,
RA Mojahedi F., Kara M., Cai N., Silhavy J.L., Elsharif S., Fenercioglu E.,
RA Barshop B.A., Kara B., Wang R., Stanley V., James K.N., Nachnani R.,
RA Kalur A., Megahed H., Incecik F., Danda S., Alanay Y., Faqeih E.,
RA Melikishvili G., Mansour L., Miller I., Sukhudyan B., Chelly J.,
RA Dobyns W.B., Bilguvar K., Jamra R.A., Gunel M., Gleeson J.G.;
RT "Biallelic loss of human CTNNA2, encoding alphaN-catenin, leads to ARP2/3
RT complex overactivity and disordered cortical neuronal migration.";
RL Nat. Genet. 50:1093-1101(2018).
CC -!- FUNCTION: May function as a linker between cadherin adhesion receptors
CC and the cytoskeleton to regulate cell-cell adhesion and differentiation
CC in the nervous system (By similarity). Required for proper regulation
CC of cortical neuronal migration and neurite growth (PubMed:30013181). It
CC acts as negative regulator of Arp2/3 complex activity and Arp2/3-
CC mediated actin polymerization (PubMed:30013181). It thereby suppresses
CC excessive actin branching which would impair neurite growth and
CC stability (PubMed:30013181). Regulates morphological plasticity of
CC synapses and cerebellar and hippocampal lamination during development.
CC Functions in the control of startle modulation (By similarity).
CC {ECO:0000250|UniProtKB:Q61301, ECO:0000269|PubMed:30013181}.
CC -!- SUBUNIT: Interacts with CDH1 and CDH2 (By similarity). Interacts with
CC ZNF639; recruits CTNNA2 to the nucleus (PubMed:16182284). Interacts
CC with F-actin (PubMed:30013181). {ECO:0000250|UniProtKB:P30997,
CC ECO:0000269|PubMed:16182284, ECO:0000269|PubMed:30013181}.
CC -!- INTERACTION:
CC P26232; Q9UID6: ZNF639; NbExp=7; IntAct=EBI-3953920, EBI-947476;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q61301};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q61301}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:Q61301}. Cytoplasm
CC {ECO:0000269|PubMed:16182284}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q61301}. Cell junction, adherens junction
CC {ECO:0000250|UniProtKB:Q61301}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q61301}. Nucleus {ECO:0000269|PubMed:16182284}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=AlphaN-catenin II;
CC IsoId=P26232-1; Sequence=Displayed;
CC Name=2; Synonyms=AlphaN-catenin I;
CC IsoId=P26232-2; Sequence=VSP_020337;
CC Name=3;
CC IsoId=P26232-3; Sequence=VSP_038009;
CC Name=4;
CC IsoId=P26232-4; Sequence=VSP_038008, VSP_020337;
CC Name=5;
CC IsoId=P26232-5; Sequence=VSP_038007, VSP_020337;
CC Name=6; Synonyms=AlphaN-catenin III;
CC IsoId=P26232-6; Sequence=VSP_038005, VSP_038006, VSP_020337;
CC -!- TISSUE SPECIFICITY: Expressed in neural tissues, with strongest
CC expression in fetal and adult brain. Expressed in the developing
CC cortical plate and marginal zone of 20-week-old human fetal brain.
CC {ECO:0000269|PubMed:30013181}.
CC -!- DISEASE: Cortical dysplasia, complex, with other brain malformations 9
CC (CDCBM9) [MIM:618174]: An autosomal recessive disorder characterized by
CC neurodevelopmental delay apparent from early infancy, acquired
CC microcephaly, hypotonic cerebral palsy, inability to ambulate or speak,
CC and intractable seizures. Brain imaging shows pachygyria with severe
CC cortical gray matter thickening, paucity of gyri without an obvious
CC posterior-anterior gradient or focal dysplasias, hypogenesis of the
CC corpus callosum, and cerebellar hypoplasia.
CC {ECO:0000269|PubMed:30013181}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the vinculin/alpha-catenin family.
CC {ECO:0000305}.
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DR EMBL; M94151; AAA58407.2; -; mRNA.
DR EMBL; AK127226; BAG54457.1; -; mRNA.
DR EMBL; AK295181; BAH12003.1; -; mRNA.
DR EMBL; AK295493; BAH12088.1; -; mRNA.
DR EMBL; AK303035; BAH13884.1; -; mRNA.
DR EMBL; BX537769; CAD97832.1; -; mRNA.
DR EMBL; AC008067; AAY15073.1; -; Genomic_DNA.
DR EMBL; AC010975; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011741; AAX93241.1; -; Genomic_DNA.
DR EMBL; AC011746; AAY15008.1; -; Genomic_DNA.
DR EMBL; AC016670; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC016716; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093322; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC096573; AAY14758.1; -; Genomic_DNA.
DR EMBL; AC096753; AAY14763.1; -; Genomic_DNA.
DR EMBL; AC104780; AAX88946.1; -; Genomic_DNA.
DR EMBL; FJ695201; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471053; EAW99564.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99565.1; -; Genomic_DNA.
DR EMBL; BC052996; AAH52996.1; -; mRNA.
DR CCDS; CCDS42703.2; -. [P26232-2]
DR CCDS; CCDS54371.1; -. [P26232-3]
DR CCDS; CCDS62944.1; -. [P26232-1]
DR CCDS; CCDS62945.1; -. [P26232-6]
DR CCDS; CCDS74531.1; -. [P26232-4]
DR PIR; A45011; A45011.
DR RefSeq; NP_001158355.1; NM_001164883.1. [P26232-3]
DR RefSeq; NP_001269526.1; NM_001282597.2. [P26232-1]
DR RefSeq; NP_001269527.1; NM_001282598.1. [P26232-5]
DR RefSeq; NP_001269528.1; NM_001282599.1. [P26232-6]
DR RefSeq; NP_001269529.1; NM_001282600.1. [P26232-4]
DR RefSeq; NP_001307739.1; NM_001320810.1.
DR RefSeq; NP_004380.2; NM_004389.3. [P26232-2]
DR RefSeq; XP_011530857.1; XM_011532555.2. [P26232-1]
DR RefSeq; XP_011530858.1; XM_011532556.2. [P26232-1]
DR RefSeq; XP_016858892.1; XM_017003403.1. [P26232-2]
DR PDB; 6DUW; X-ray; 2.20 A; A=651-953.
DR PDBsum; 6DUW; -.
DR AlphaFoldDB; P26232; -.
DR SMR; P26232; -.
DR BioGRID; 107877; 75.
DR DIP; DIP-60979N; -.
DR IntAct; P26232; 23.
DR MINT; P26232; -.
DR STRING; 9606.ENSP00000384638; -.
DR iPTMnet; P26232; -.
DR PhosphoSitePlus; P26232; -.
DR SwissPalm; P26232; -.
DR BioMuta; CTNNA2; -.
DR DMDM; 114152793; -.
DR CPTAC; CPTAC-1756; -.
DR EPD; P26232; -.
DR jPOST; P26232; -.
DR MassIVE; P26232; -.
DR MaxQB; P26232; -.
DR PeptideAtlas; P26232; -.
DR PRIDE; P26232; -.
DR ProteomicsDB; 54314; -. [P26232-1]
DR ProteomicsDB; 54315; -. [P26232-2]
DR ProteomicsDB; 54316; -. [P26232-3]
DR ProteomicsDB; 54317; -. [P26232-4]
DR ProteomicsDB; 54318; -. [P26232-5]
DR ProteomicsDB; 54319; -. [P26232-6]
DR TopDownProteomics; P26232-6; -. [P26232-6]
DR Antibodypedia; 8335; 143 antibodies from 28 providers.
DR DNASU; 1496; -.
DR Ensembl; ENST00000343114.7; ENSP00000341500.3; ENSG00000066032.19. [P26232-6]
DR Ensembl; ENST00000402739.9; ENSP00000384638.4; ENSG00000066032.19. [P26232-1]
DR Ensembl; ENST00000466387.5; ENSP00000418191.1; ENSG00000066032.19. [P26232-2]
DR Ensembl; ENST00000496558.5; ENSP00000419295.1; ENSG00000066032.19. [P26232-2]
DR Ensembl; ENST00000541047.5; ENSP00000444675.2; ENSG00000066032.19. [P26232-4]
DR Ensembl; ENST00000629316.2; ENSP00000486160.1; ENSG00000066032.19. [P26232-3]
DR GeneID; 1496; -.
DR KEGG; hsa:1496; -.
DR MANE-Select; ENST00000402739.9; ENSP00000384638.4; NM_001282597.3; NP_001269526.1.
DR UCSC; uc010yse.3; human. [P26232-1]
DR CTD; 1496; -.
DR DisGeNET; 1496; -.
DR GeneCards; CTNNA2; -.
DR HGNC; HGNC:2510; CTNNA2.
DR HPA; ENSG00000066032; Tissue enhanced (brain, epididymis, retina).
DR MalaCards; CTNNA2; -.
DR MIM; 114025; gene.
DR MIM; 618174; phenotype.
DR neXtProt; NX_P26232; -.
DR OpenTargets; ENSG00000066032; -.
DR PharmGKB; PA27013; -.
DR VEuPathDB; HostDB:ENSG00000066032; -.
DR eggNOG; KOG3681; Eukaryota.
DR GeneTree; ENSGT01030000234543; -.
DR HOGENOM; CLU_015314_2_0_1; -.
DR InParanoid; P26232; -.
DR OMA; QDELMNN; -.
DR OrthoDB; 953344at2759; -.
DR PhylomeDB; P26232; -.
DR TreeFam; TF313686; -.
DR PathwayCommons; P26232; -.
DR Reactome; R-HSA-525793; Myogenesis.
DR SignaLink; P26232; -.
DR SIGNOR; P26232; -.
DR BioGRID-ORCS; 1496; 15 hits in 1071 CRISPR screens.
DR ChiTaRS; CTNNA2; human.
DR GenomeRNAi; 1496; -.
DR Pharos; P26232; Tbio.
DR PRO; PR:P26232; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P26232; protein.
DR Bgee; ENSG00000066032; Expressed in frontal pole and 148 other tissues.
DR ExpressionAtlas; P26232; baseline and differential.
DR Genevisible; P26232; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
DR GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0008013; F:beta-catenin binding; IBA:GO_Central.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; NAS:UniProtKB.
DR GO; GO:0007409; P:axonogenesis; ISS:UniProtKB.
DR GO; GO:0048854; P:brain morphogenesis; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0048813; P:dendrite morphogenesis; ISS:UniProtKB.
DR GO; GO:0034316; P:negative regulation of Arp2/3 complex-mediated actin nucleation; IMP:UniProtKB.
DR GO; GO:0060134; P:prepulse inhibition; ISS:UniProtKB.
DR GO; GO:0021942; P:radial glia guided migration of Purkinje cell; ISS:UniProtKB.
DR GO; GO:2001222; P:regulation of neuron migration; IMP:UniProtKB.
DR GO; GO:0010975; P:regulation of neuron projection development; IMP:UniProtKB.
DR GO; GO:0051823; P:regulation of synapse structural plasticity; ISS:UniProtKB.
DR InterPro; IPR036723; Alpha-catenin/vinculin-like_sf.
DR InterPro; IPR001033; Alpha_catenin.
DR InterPro; IPR030046; CTNNA2.
DR InterPro; IPR006077; Vinculin/catenin.
DR InterPro; IPR000633; Vinculin_CS.
DR PANTHER; PTHR18914:SF23; PTHR18914:SF23; 1.
DR Pfam; PF01044; Vinculin; 2.
DR PRINTS; PR00805; ALPHACATENIN.
DR SUPFAM; SSF47220; SSF47220; 4.
DR PROSITE; PS00663; VINCULIN_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell junction;
KW Cell membrane; Cell projection; Cytoplasm; Cytoskeleton;
KW Developmental protein; Differentiation; Disease variant; Lissencephaly;
KW Membrane; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..953
FT /note="Catenin alpha-2"
FT /id="PRO_0000064263"
FT REGION 912..939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..931
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 632
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q61301"
FT MOD_RES 640
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 651
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61301"
FT MOD_RES 901
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61301"
FT MOD_RES 939
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61301"
FT VAR_SEQ 1..368
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038008"
FT VAR_SEQ 1..351
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_038005"
FT VAR_SEQ 1
FT /note="M -> MSGLICLQYGLWHGQKIDFGGPRRLLQRNRGEGSM (in isoform
FT 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038007"
FT VAR_SEQ 352
FT /note="N -> MDGWRRPLQSVGKVCEKNMKTSEMHTMSGAQ (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_038006"
FT VAR_SEQ 766..858
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038009"
FT VAR_SEQ 811..858
FT /note="Missing (in isoform 2, isoform 4, isoform 5 and
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT /id="VSP_020337"
FT VARIANT 494..953
FT /note="Missing (in CDCBM9)"
FT /evidence="ECO:0000269|PubMed:30013181"
FT /id="VAR_081335"
FT VARIANT 781..953
FT /note="Missing (in CDCBM9; loss-of-function variant
FT resulting in decreased neurite length and impaired neuronal
FT migration in patient-derived nerve cells; no protein
FT detected in patient cells)"
FT /evidence="ECO:0000269|PubMed:30013181"
FT /id="VAR_081336"
FT VARIANT 930..953
FT /note="Missing (in CDCBM9; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30013181"
FT /id="VAR_081337"
FT CONFLICT 122
FT /note="T -> A (in Ref. 3; BAH12003)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="E -> K (in Ref. 1; AAA58407)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="S -> SS (in Ref. 5; AAY15008)"
FT /evidence="ECO:0000305"
FT CONFLICT 651..652
FT /note="SR -> RG (in Ref. 1; AAA58407)"
FT /evidence="ECO:0000305"
FT HELIX 677..702
FT /evidence="ECO:0007829|PDB:6DUW"
FT HELIX 710..729
FT /evidence="ECO:0007829|PDB:6DUW"
FT HELIX 738..765
FT /evidence="ECO:0007829|PDB:6DUW"
FT HELIX 769..792
FT /evidence="ECO:0007829|PDB:6DUW"
FT STRAND 798..802
FT /evidence="ECO:0007829|PDB:6DUW"
FT STRAND 805..809
FT /evidence="ECO:0007829|PDB:6DUW"
FT HELIX 861..894
FT /evidence="ECO:0007829|PDB:6DUW"
SQ SEQUENCE 953 AA; 105313 MW; 5FC88907B37E8A6C CRC64;
MTSATSPIIL KWDPKSLEIR TLTVERLLEP LVTQVTTLVN TSNKGPSGKK KGRSKKAHVL
AASVEQATQN FLEKGEQIAK ESQDLKEELV AAVEDVRKQG ETMRIASSEF ADDPCSSVKR
GTMVRAARAL LSAVTRLLIL ADMADVMRLL SHLKIVEEAL EAVKNATNEQ DLANRFKEFG
KEMVKLNYVA ARRQQELKDP HCRDEMAAAR GALKKNATML YTASQAFLRH PDVAATRANR
DYVFKQVQEA IAGISNAAQA TSPTDEAKGH TGIGELAAAL NEFDNKIILD PMTFSEARFR
PSLEERLESI ISGAALMADS SCTRDDRRER IVAECNAVRQ ALQDLLSEYM NNTGRKEKGD
PLNIAIDKMT KKTRDLRRQL RKAVMDHISD SFLETNVPLL VLIEAAKSGN EKEVKEYAQV
FREHANKLVE VANLACSISN NEEGVKLVRM AATQIDSLCP QVINAALTLA ARPQSKVAQD
NMDVFKDQWE KQVRVLTEAV DDITSVDDFL SVSENHILED VNKCVIALQE GDVDTLDRTA
GAIRGRAARV IHIINAEMEN YEAGVYTEKV LEATKLLSET VMPRFAEQVE VAIEALSANV
PQPFEENEFI DASRLVYDGV RDIRKAVLMI RTPEELEDDS DFEQEDYDVR SRTSVQTEDD
QLIAGQSARA IMAQLPQEEK AKIAEQVEIF HQEKSKLDAE VAKWDDSGND IIVLAKQMCM
IMMEMTDFTR GKGPLKNTSD VINAAKKIAE AGSRMDKLAR AVADQCPDSA CKQDLLAYLQ
RIALYCHQLN ICSKVKAEVQ NLGGELIVSG TGVQSTFTTF YEVDCDVIDG GRASQLSTHL
PTCAEGAPIG SGSSDSSMLD SATSLIQAAK NLMNAVVLTV KASYVASTKY QKVYGTAAVN
SPVVSWKMKA PEKKPLVKRE KPEEFQTRVR RGSQKKHISP VQALSEFKAM DSF
