ID   CTNA2_XENLA             Reviewed;         966 AA.
AC   Q6GLP0;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Catenin alpha-2;
DE   AltName: Full=Alpha N-catenin;
GN   Name=ctnna2;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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; BC074420; AAH74420.1; -; mRNA.
DR   RefSeq; NP_001086281.1; NM_001092812.1.
DR   AlphaFoldDB; Q6GLP0; -.
DR   SMR; Q6GLP0; -.
DR   DNASU; 444710; -.
DR   GeneID; 444710; -.
DR   KEGG; xla:444710; -.
DR   CTD; 444710; -.
DR   Xenbase; XB-GENE-5955229; ctnna2.L.
DR   OrthoDB; 953344at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 444710; Expressed in brain and 2 other tissues.
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:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR   GO; GO:0045296; F:cadherin binding; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0007409; P:axonogenesis; ISS:UniProtKB.
DR   GO; GO:0048854; P:brain morphogenesis; ISS:UniProtKB.
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   InterPro; IPR000633; Vinculin_CS.
DR   PANTHER; PTHR18914:SF23; PTHR18914:SF23; 1.
DR   Pfam; PF01044; Vinculin; 1.
DR   PRINTS; PR00805; ALPHACATENIN.
DR   SUPFAM; SSF47220; SSF47220; 4.
DR   PROSITE; PS00663; VINCULIN_1; 1.
PE   2: Evidence at transcript level;
KW   Cell adhesion; Cell junction; Cell membrane; Cell projection; Cytoplasm;
KW   Cytoskeleton; Developmental protein; Differentiation; Membrane; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..966
FT                   /note="Catenin alpha-2"
FT                   /id="PRO_0000383570"
FT   REGION          924..952
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        924..944
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   966 AA;  107101 MW;  44DAC3F5BAF130B9 CRC64;
     MSSATSPIIL KWDPKSLEIR TLTVESLLEP LVTQVTTLVN TSNKGPSGKK KGRSKKAHVL
     AASVEQATQN FLEKGEQIAK ESQDLKDELI SAVEDVRKQG ETMRIASSEF ADDPCSSVKR
     GTMVRAARAL LSAVTRLLIL ADMADVMRLL THLKIVEEAL EMVKNATNEQ DLAHRFKEFG
     KEMVKLNYVA ARRQQELKDP HCRDEMAAAR GALKKNATML YTASQAFLRH SDVAATRANR
     DYVFKQVQEA IAGISNAAQA TSPTDEKQAH TGIGELAAAL NEFDNKIILD PLTFSEARFR
     PSLEERLESI ISGAALMADS SCTRDDRRER IVAECNSVRQ ALQDLLSEYM NNCRYGTWMD
     ESSKSGRKEK GDPLNIAIDK MTKKTRDLRR QLRKAVMDHI SDSFLETNVP LLVLIEAAKS
     GNEKEVKEYA QVFREHANKL VEVANLACSI SNNEEGVKLV RMAATQIDSL CPQVINAALT
     LAARPQSKVA QDNMDVFKDQ WEKQVRVLTE AVDDITSVDD FLSVSENHIL EDVNKCVIAL
     QEGDVDTLDR TAGAIRGRAA RVIHIINAEM ENYEAGVYTE KVLETTKLLS ETVMPRFAEQ
     VEVAIEALST NIPQPFEENE FIDASRLVYD GVRDIRKAVL MIRTPEELED DSDFEQEDYD
     VRSRTSVQTE DDQLIAGQSA RAIMAQLPQE EKAKIAEQVE IFHQEKSKLD AEVAKWDDSG
     NDIIVLAKQM CMIMMEMTDF TRGKGPLKNT SDVINAAKKI AEAGSRMDKL ARAVADQCPD
     SACKQDLLAY LQRIALYCHQ LNICSKVKAE VQNLGGELIV SGTGVQSTFT TFYEVAGDVI
     AGGRDSQLSL DLLPSCTEGS LFGSGSRDST MLDSATSLIQ AAKNLMNAVV LTVKASYVAS
     TKYQKVYGTA AVNSPVVSWK MKAPEKKPLV KREKPEEYQT RVRRGSQKKH ISPVQALSEF
     KAMDSF