CTNA2_CHICK
ID CTNA2_CHICK Reviewed; 906 AA.
AC P30997;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Catenin alpha-2;
DE AltName: Full=Alpha N-catenin;
DE AltName: Full=Neural alpha-catenin;
GN Name=CTNNA2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH CDH1 AND CDH2,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryonic brain;
RX PubMed=1638632; DOI=10.1016/0092-8674(92)90103-j;
RA Hirano S., Kimoto N., Shimoyama Y., Hirohashi S., Takeichi M.;
RT "Identification of a neural alpha-catenin as a key regulator of cadherin
RT function and multicellular organization.";
RL Cell 70:293-301(1992).
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:0000269|PubMed:1638632}.
CC -!- SUBUNIT: Interacts with CDH1 and CDH2. {ECO:0000269|PubMed:1638632}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1638632};
CC Peripheral membrane protein {ECO:0000305|PubMed:1638632}; Cytoplasmic
CC side {ECO:0000305|PubMed:1638632}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q61301}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q61301}. Cell junction, adherens junction
CC {ECO:0000269|PubMed:1638632}. Cell projection, axon
CC {ECO:0000305|PubMed:1638632}. Nucleus {ECO:0000250|UniProtKB:P26232}.
CC -!- TISSUE SPECIFICITY: Mainly in the nervous system (at protein level).
CC {ECO:0000269|PubMed:1638632}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the neural tube, dorsal root
CC glanglia, spinal nerves and myotome at E4. Expressed in neuronal and
CC glial cell populations as detected at E10 (at protein level).
CC {ECO:0000269|PubMed:1638632}.
CC -!- SIMILARITY: Belongs to the vinculin/alpha-catenin family.
CC {ECO:0000305}.
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DR EMBL; D11090; BAA01863.1; -; mRNA.
DR PIR; A43000; A43000.
DR RefSeq; NP_990467.1; NM_205136.1.
DR AlphaFoldDB; P30997; -.
DR SMR; P30997; -.
DR STRING; 9031.ENSGALP00000025681; -.
DR PaxDb; P30997; -.
DR GeneID; 396035; -.
DR KEGG; gga:396035; -.
DR CTD; 1496; -.
DR VEuPathDB; HostDB:geneid_396035; -.
DR eggNOG; KOG3681; Eukaryota.
DR HOGENOM; CLU_015314_0_0_1; -.
DR InParanoid; P30997; -.
DR OrthoDB; 953344at2759; -.
DR PhylomeDB; P30997; -.
DR PRO; PR:P30997; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
DR GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:AgBase.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:AgBase.
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; IDA:UniProtKB.
DR GO; GO:0048813; P:dendrite morphogenesis; ISS:UniProtKB.
DR GO; GO:0030855; P:epithelial cell differentiation; IDA:UniProtKB.
DR GO; GO:0001755; P:neural crest cell migration; IMP:AgBase.
DR GO; GO:0008104; P:protein localization; IMP:AgBase.
DR GO; GO:0051823; P:regulation of synapse structural plasticity; ISS:UniProtKB.
DR GO; GO:0061561; P:trigeminal ganglion formation; IMP:AgBase.
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 Cell adhesion; Cell junction; Cell membrane; Cell projection; Cytoplasm;
KW Cytoskeleton; Developmental protein; Differentiation; Membrane; Nucleus;
KW Reference proteome.
FT CHAIN 1..906
FT /note="Catenin alpha-2"
FT /id="PRO_0000064265"
FT REGION 866..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..884
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 906 AA; 100691 MW; 7714D04918572DB7 CRC64;
MTSATSPIIL KWDPKSLEIR TLTVERLLEP LVTQVTTLVN TSNKGPSGKK KGRSKKAHVL
AASVEQATQN FLEKGDQIAK ESQDLKEELV AAVEDVRKQG ETMRIASSEF ADDPCSSVKR
GTMVRAARAL LSAVTRLLIL ADMADVMRLL SHLKIVEEAL EAVKNATNEQ DLANRFKEFG
KEMVKLNYVA ARRQQELKDP HCRDEMAAAR GALKKNATML YTASQAFLRH PDVAATRANR
DYVFKQVQEA IAGISNAAQA TSPTDENKGH TGIGELAAAL NEFDNKIILD PMTFSEARFR
PSLEERLESI ISGAALMADS SCTRDDRRKR IVAECKRAVR QALQDLLSEY MNNTGRKEKG
DPLNIAIDKM TKKTRDLRRQ LRKAVMDHIS DSFLETNVPL LVLIEAAKSG NEKEVKEYAQ
VFREHANKLV EVANLACSIS NNEEGVKLVR MAATQIDSLC PQVINAALTL AARPQSKVAQ
DNMDVFKDQW EKQVRVLTEA VDDITSVDDF LSVSENHILE DVNKCVIALQ EGDVDTLDRT
AGAIRGRAAR VIHIINAEME NYETGVYTEK VLEATKLLSE TVMPRFAEQV EVAIEALSAN
VPQPFEENEF IDASRLVYDG VRDIRKAVLM IRTPEELEDD SDFEQEDYDV RSRTSVQTED
DQLIAGQSAR AIMAQLPQEE KAKIAEQVEI FHQEKSKLDA EVAKWDDSGN DIIVLAKQMC
MIMMEMTDFT RGKGPLKNTS DVINAAKKIA EAGSRMDKLA RAVADQCPDS ACKQDLLAYL
QRIALYCHQL NICSKVKAEV QNLGGELIVS GLDSATSLIQ AAKNLMNAVV LTVKASYVAS
TKYQKVYGTA AVNSPVVSWK MKAPEKKPLV KREKPEEYQT RVRRGSQKKH ISPVQALSEF
KAMDSF
