CTNA2_PONAB
ID CTNA2_PONAB Reviewed; 905 AA.
AC Q5R416; Q5R4P9;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Catenin alpha-2;
DE AltName: Full=Alpha N-catenin;
GN Name=CTNNA2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-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. Required for proper regulation of cortical
CC neuronal migration and neurite growth. It acts as negative regulator of
CC Arp2/3 complex activity and Arp2/3-mediated actin polymerization. It
CC thereby suppresses excessive actin branching which would impair neurite
CC growth and stability. Regulates morphological plasticity of synapses
CC and cerebellar and hippocampal lamination during development. Functions
CC in the control of startle modulation. {ECO:0000250|UniProtKB:P26232,
CC ECO:0000250|UniProtKB:Q61301}.
CC -!- SUBUNIT: Interacts with CDH1 and CDH2 (By similarity). Interacts with
CC ZNF639; recruits CTNNA2 to the nucleus (By similarity). Interacts with
CC F-actin (By similarity). {ECO:0000250|UniProtKB:P26232,
CC 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR861196; CAH93267.1; -; mRNA.
DR EMBL; CR861444; CAH93500.1; -; mRNA.
DR RefSeq; NP_001127048.1; NM_001133576.1.
DR AlphaFoldDB; Q5R416; -.
DR SMR; Q5R416; -.
DR STRING; 9601.ENSPPYP00000013655; -.
DR Ensembl; ENSPPYT00000034973; ENSPPYP00000042775; ENSPPYG00000012245.
DR GeneID; 100174076; -.
DR KEGG; pon:100174076; -.
DR CTD; 1496; -.
DR eggNOG; KOG3681; Eukaryota.
DR GeneTree; ENSGT01030000234543; -.
DR HOGENOM; CLU_015314_2_0_1; -.
DR InParanoid; Q5R416; -.
DR OMA; QDELMNN; -.
DR TreeFam; TF313686; -.
DR Proteomes; UP000001595; Chromosome 2A.
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; ISS:UniProtKB.
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:0034316; P:negative regulation of Arp2/3 complex-mediated actin nucleation; ISS: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; ISS:UniProtKB.
DR GO; GO:0010975; P:regulation of neuron projection development; 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 Phosphoprotein; Reference proteome.
FT CHAIN 1..905
FT /note="Catenin alpha-2"
FT /id="PRO_0000248839"
FT REGION 869..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..883
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:0000250|UniProtKB:P26232"
FT MOD_RES 651
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61301"
FT MOD_RES 853
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61301"
FT MOD_RES 891
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61301"
FT CONFLICT 285
FT /note="N -> I (in Ref. 1; CAH93267)"
FT /evidence="ECO:0000305"
FT CONFLICT 569
FT /note="K -> R (in Ref. 1; CAH93267)"
FT /evidence="ECO:0000305"
FT CONFLICT 666
FT /note="Q -> R (in Ref. 1; CAH93267)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 905 AA; 100447 MW; ECDB5DA119B443CF 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 LDSATSLIQA AKNLMNAVVL TVKASYVAST
KYQKVYGTAA VNSPVVSWKM KAPEKKPLVK REKPEEFQTR VRRGSQKKHI SPVQALSEFK
AMDSF
