CTNA2_DANRE
ID CTNA2_DANRE Reviewed; 865 AA.
AC B7ZC77;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Catenin alpha-2;
DE AltName: Full=Alpha N-catenin;
GN Name=Ctnna2; ORFNames=si:dkeyp-13b9.1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
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. {ECO:0000250|UniProtKB:P30997}.
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:0000250|UniProtKB:Q61301}. 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:0000250|UniProtKB:P26232}.
CC -!- SIMILARITY: Belongs to the vinculin/alpha-catenin family.
CC {ECO:0000305}.
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DR EMBL; CT997814; CAX12136.1; -; Genomic_DNA.
DR EMBL; AL626804; CAX12136.1; JOINED; Genomic_DNA.
DR EMBL; BX927206; CAX12136.1; JOINED; Genomic_DNA.
DR EMBL; CR925858; CAX12136.1; JOINED; Genomic_DNA.
DR EMBL; CT998561; CAX12136.1; JOINED; Genomic_DNA.
DR EMBL; CU076051; CAX12136.1; JOINED; Genomic_DNA.
DR EMBL; AL626804; CAX12850.1; -; Genomic_DNA.
DR EMBL; BX927206; CAX12850.1; JOINED; Genomic_DNA.
DR EMBL; CR925858; CAX12850.1; JOINED; Genomic_DNA.
DR EMBL; CT997814; CAX12850.1; JOINED; Genomic_DNA.
DR EMBL; CT998561; CAX12850.1; JOINED; Genomic_DNA.
DR EMBL; CU076051; CAX12850.1; JOINED; Genomic_DNA.
DR EMBL; CT998561; CAX13235.1; -; Genomic_DNA.
DR EMBL; AL626804; CAX13235.1; JOINED; Genomic_DNA.
DR EMBL; BX927206; CAX13235.1; JOINED; Genomic_DNA.
DR EMBL; CR925858; CAX13235.1; JOINED; Genomic_DNA.
DR EMBL; CT997814; CAX13235.1; JOINED; Genomic_DNA.
DR EMBL; CU076051; CAX13235.1; JOINED; Genomic_DNA.
DR EMBL; BX927206; CAX13660.1; -; Genomic_DNA.
DR EMBL; AL626804; CAX13660.1; JOINED; Genomic_DNA.
DR EMBL; CR925858; CAX13660.1; JOINED; Genomic_DNA.
DR EMBL; CT997814; CAX13660.1; JOINED; Genomic_DNA.
DR EMBL; CT998561; CAX13660.1; JOINED; Genomic_DNA.
DR EMBL; CU076051; CAX13660.1; JOINED; Genomic_DNA.
DR EMBL; CR925858; CAX13953.1; -; Genomic_DNA.
DR EMBL; AL626804; CAX13953.1; JOINED; Genomic_DNA.
DR EMBL; BX927206; CAX13953.1; JOINED; Genomic_DNA.
DR EMBL; CT997814; CAX13953.1; JOINED; Genomic_DNA.
DR EMBL; CT998561; CAX13953.1; JOINED; Genomic_DNA.
DR EMBL; CU076051; CAX13953.1; JOINED; Genomic_DNA.
DR EMBL; CU076051; CAX14820.1; -; Genomic_DNA.
DR EMBL; AL626804; CAX14820.1; JOINED; Genomic_DNA.
DR EMBL; BX927206; CAX14820.1; JOINED; Genomic_DNA.
DR EMBL; CR925858; CAX14820.1; JOINED; Genomic_DNA.
DR EMBL; CT997814; CAX14820.1; JOINED; Genomic_DNA.
DR EMBL; CT998561; CAX14820.1; JOINED; Genomic_DNA.
DR RefSeq; NP_001152844.1; NM_001159372.1.
DR AlphaFoldDB; B7ZC77; -.
DR SMR; B7ZC77; -.
DR STRING; 7955.ENSDARP00000092080; -.
DR PaxDb; B7ZC77; -.
DR PeptideAtlas; B7ZC77; -.
DR PRIDE; B7ZC77; -.
DR Ensembl; ENSDART00000101306; ENSDARP00000092080; ENSDARG00000024785.
DR GeneID; 567500; -.
DR KEGG; dre:567500; -.
DR CTD; 1496; -.
DR ZFIN; ZDB-GENE-060815-3; ctnna2.
DR eggNOG; KOG3681; Eukaryota.
DR GeneTree; ENSGT01030000234543; -.
DR HOGENOM; CLU_015314_2_0_1; -.
DR InParanoid; B7ZC77; -.
DR OMA; QDELMNN; -.
DR OrthoDB; 953344at2759; -.
DR PhylomeDB; B7ZC77; -.
DR TreeFam; TF313686; -.
DR Reactome; R-DRE-525793; Myogenesis.
DR PRO; PR:B7ZC77; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 1.
DR Bgee; ENSDARG00000024785; Expressed in brain and 22 other tissues.
DR ExpressionAtlas; B7ZC77; baseline.
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; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0008013; F:beta-catenin binding; IBA:GO_Central.
DR GO; GO:0045296; F:cadherin binding; IEA:InterPro.
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: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 PANTHER; PTHR18914:SF23; PTHR18914:SF23; 2.
DR Pfam; PF01044; Vinculin; 3.
DR PRINTS; PR00805; ALPHACATENIN.
DR SUPFAM; SSF47220; SSF47220; 4.
PE 3: Inferred from homology;
KW Cell adhesion; Cell junction; Cell membrane; Cell projection; Cytoplasm;
KW Cytoskeleton; Developmental protein; Differentiation; Membrane; Nucleus;
KW Reference proteome.
FT CHAIN 1..865
FT /note="Catenin alpha-2"
FT /id="PRO_0000383569"
FT REGION 823..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..843
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 865 AA; 95856 MW; 49F906AD1ACA0AF5 CRC64;
MTSATSPILL KWDPKSLEIR TLTVERLLEP LVTQVTTLVN TSNKGPSSKK KGRSKKAHVL
AVSVEQATQN FLEKGEQIAK DSQDLKEELI AAVEDVRKQG DTMRVASSEF ADDPCSSVKR
GTMVRAARAL LSAVTRLLIL ADMADVMRLL AHLKIELKDP QCRDEMAAAR GALKKNATML
YTASQAFLRH PDVAATRANR DYVFKQVQEA IGGISSSAQA TSPTDEKHGH AGIGELAAAL
NEFDNKIILD PLTFSEARFR PSLEERLESI ISGAALMADS SCTRDDRRER IVAECNAVRQ
ALQDLLSEYM NNTGRKEKGD PLNSAIDKMT KKTRDLRRQL RKAVMDHISD SFLETNVPLL
VLIEAAKSGN EKEVKEYAQV FREHANKLVE VANLACSISN NEEGVKLVRM AATQIDSLCP
QVINAALTLA ARPQSKVAQD NMDVFKDQWE KQVRILTEAV DDITSVDDFL SVSENHILED
VNKCVIALQE GDVDTLDRTA GAIRGRAARV VHIINAEMEN YEPGVYTERV LESIKLLSET
VMPRFAEQVE VAIEALSTSP PQPFEENEFI DASRLVYDGV RDIRKAVLMI RTPEELEDDS
DFEQEDYDAR SRTSIQTEDD QLIAGQSARA IMAQLPQEEK AKIAEQVESF RQEKSKLDAE
VAKWDDNGND IIVLAKQMCM IMMEMTDFTR GKGPLKNSSD VINAAKKIAE AGSRMDKLAR
AVADQCPDSA CKQDLLAYLQ RIALYCHQLN ICSKVKAEVQ NLGGELIVSG LDSATSLIQA
AKNLMNAVVL TVKASYVAST KYQKVYGTAA VNSPVVSWRM KAPEKKPLVK REKPEECQTR
VRRGSQKKHI SPVQALSEFK AMDSF
