ID   CTNA2_XENTR             Reviewed;         966 AA.
AC   A4IGI7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Catenin alpha-2;
DE   AltName: Full=Alpha N-catenin;
GN   Name=ctnna2;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2007) 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; BC135120; AAI35121.1; -; mRNA.
DR   RefSeq; NP_001090774.1; NM_001097305.1.
DR   AlphaFoldDB; A4IGI7; -.
DR   SMR; A4IGI7; -.
DR   STRING; 8364.ENSXETP00000058946; -.
DR   PaxDb; A4IGI7; -.
DR   PRIDE; A4IGI7; -.
DR   GeneID; 100037860; -.
DR   KEGG; xtr:100037860; -.
DR   CTD; 1496; -.
DR   Xenbase; XB-GENE-5955201; ctnna2.
DR   eggNOG; KOG3681; Eukaryota.
DR   InParanoid; A4IGI7; -.
DR   OrthoDB; 953344at2759; -.
DR   Reactome; R-XTR-525793; Myogenesis.
DR   Proteomes; UP000008143; Chromosome 1.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000040099; Expressed in brain and 7 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:0016342; C:catenin complex; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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: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: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   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   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_0000383571"
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;  107112 MW;  44945FE499F3C608 CRC64;
     MSSATSPIIL KWDPKSLEIR TLTVESLLEP LVTQVTTLVN TSNKGPSGKK KGRSKKAHVL
     AASVEQATQN FLEKGEQIAK ESQDLKEELI SAVEDVRKQG DTMRITSSEF ADDPCSSVKR
     GTMVRAARAL LSAVTRLLIL ADMADVMRLL IHLKIVEEAL ESVKNATNEQ DLAHRFKEFG
     KEMVKLNYVA ARRQQELKDP HCRDEMAAAR GALKKNATML YTASQAFLRH PDVAATRANR
     DYVFKQVQEA IAGIANAAQA TSPTDEKQAH TGIGELAAAL NEFDNKIILD PLTFSEARFR
     PSLEEKLESI ISGAALMADS SCTRDDRRER IVAECNSVRQ ALQDLLSEYM NNCRYGTWMD
     ESCKSGRKEK GDPLNIAIDK MTKKTRDLRR QLRKAVMDHI SDSFLETNVP LLVLIEAAKN
     GNEKEVKEYA QVFREHANKL VEVANLACSI SNNEEGVKLV RMAATQIDSL CPQVINAALT
     LAARPQSKVA QDNMDVFKDQ WEKQVRVLTE AVDDITSVDD FLSVSENHIL EDVNKCVIAL
     QEGDVDTLDR TAGAIRGRAA RVIHIINAEM ENYEAGVYTE KVLDATKLLC ETVMPRFAEQ
     VEFAIEALSA NIPQPFEENE FIDASRLVYD GVRDIRKAVL MIRTPEELED DSDFEQEDYD
     VRSRTSVQTE DDQLIAGQSA RAIMAQLPQE EKAKIAEQVE IFHQEKSKLD AEVAKWDDSG
     NDIIVLAKQM CMIMMEMTDF TRGKGPLKNT SDVINAAKKI AEAGSRMDKL ARAVADQCPD
     SACKQDLIAY LQRIALYCHQ LNICSKVKAE VQNLGGELIV SGTAVQSTFT TFYEVAGDVI
     AGGRDSQLSL DLLPSCTEGS LFGSGSRDST MLDSATSLIQ AAKNLMNAVV LTVKASYVAS
     TKYQKVYGTA AVNSPVVSWK MKAPEKKPLV KREKPEEYQT RVRRGSQKKH ISPVQALSEF
     KAMDSF