ID A0A1U7QDJ2_MESAU Unreviewed; 905 AA.
AC A0A1U7QDJ2;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Catenin alpha-1 {ECO:0000313|RefSeq:XP_005065341.1};
GN Name=Ctnna1 {ECO:0000313|RefSeq:XP_005065341.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_005065341.1};
RN [1] {ECO:0000313|RefSeq:XP_005065341.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC {ECO:0000256|ARBA:ARBA00004536}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004413}. Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
CC -!- SIMILARITY: Belongs to the vinculin/alpha-catenin family.
CC {ECO:0000256|ARBA:ARBA00008376}.
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DR RefSeq; XP_005065341.1; XM_005065284.3.
DR AlphaFoldDB; A0A1U7QDJ2; -.
DR CORUM; A0A1U7QDJ2; -.
DR STRING; 10036.ENSMAUP00000023812; -.
DR GeneID; 101837296; -.
DR KEGG; maua:101837296; -.
DR CTD; 1495; -.
DR eggNOG; KOG3681; Eukaryota.
DR OrthoDB; 2875365at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
DR GO; GO:0016342; C:catenin complex; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016600; C:flotillin complex; IEA:Ensembl.
DR GO; GO:0014704; C:intercalated disc; IEA:Ensembl.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR GO; GO:0005915; C:zonula adherens; IEA:Ensembl.
DR GO; GO:0051015; F:actin filament binding; IEA:Ensembl.
DR GO; GO:0008013; F:beta-catenin binding; IEA:Ensembl.
DR GO; GO:0045296; F:cadherin binding; IEA:Ensembl.
DR GO; GO:0045295; F:gamma-catenin binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0017166; F:vinculin binding; IEA:Ensembl.
DR GO; GO:0043297; P:apical junction assembly; IEA:Ensembl.
DR GO; GO:0048870; P:cell motility; IEA:Ensembl.
DR GO; GO:0071681; P:cellular response to indole-3-methanol; IEA:Ensembl.
DR GO; GO:0090136; P:epithelial cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IEA:Ensembl.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:2000146; P:negative regulation of cell motility; IEA:Ensembl.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
DR GO; GO:2001045; P:negative regulation of integrin-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0007406; P:negative regulation of neuroblast proliferation; IEA:Ensembl.
DR GO; GO:1900181; P:negative regulation of protein localization to nucleus; IEA:Ensembl.
DR GO; GO:0007405; P:neuroblast proliferation; IEA:Ensembl.
DR GO; GO:2001241; P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IEA:Ensembl.
DR GO; GO:0008104; P:protein localization; IEA:Ensembl.
DR GO; GO:0007224; P:smoothened signaling pathway; IEA:Ensembl.
DR Gene3D; 6.10.250.2510; -; 1.
DR Gene3D; 1.20.120.230; Alpha-catenin/vinculin-like; 5.
DR InterPro; IPR036723; Alpha-catenin/vinculin-like_sf.
DR InterPro; IPR001033; Alpha_catenin.
DR InterPro; IPR006077; Vinculin/catenin.
DR InterPro; IPR000633; Vinculin_CS.
DR PANTHER; PTHR18914; ALPHA CATENIN; 1.
DR PANTHER; PTHR18914:SF24; CATENIN ALPHA-1; 1.
DR Pfam; PF01044; Vinculin; 1.
DR PRINTS; PR00805; ALPHACATENIN.
DR SUPFAM; SSF47220; alpha-catenin/vinculin-like; 4.
DR PROSITE; PS00663; VINCULIN_1; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000189706}.
FT REGION 863..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..883
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 905 AA; 100071 MW; 37E7FF8D0A5A058C CRC64;
MTAVHTGNIN FKWDPKSLEI RTLAVERLLE PLVTQVTTLV NTNSKGPSNK KRGRSKKAHV
LAASVEQATE NFLEKGDKIA KESQFLKEEL VAAVEDVRKQ GDLMRSAAGE FADDPCSSVK
RGNMVRAARA LLSAVTRLLI LADMADVYKL LVQLKVVEDG ILKLRNAGNE QDLGIQYKAL
KPEVDKLNIM AAKRQQELKD VGHRDQMAAA RGILQKNVPI LYTASQACLQ HPDVAAYKAN
RDLIYKQLQQ AVTGISNAAQ ATAPDDASQH QGGGGELAYA LNNFDKQIIV DPLSFSEERF
RPSLEERLES IISGAALMAD SSCTRDDRRE RIVAECNAVR QALQDLLSEY MGNAGRKERS
DALNSAIDKM TKKTRDLRRQ LRKAVMDHVS DSFLETNVPL LVLIEAAKNG NEKEVKEYAQ
VFREHANKLI EVANLACSIS NNEEGVKLVR MSASQLEALC PQVINAALAL AAKPQSKLAQ
ENMDLFKEQW EKQVRVLTDA VDDITSIDDF LAVSENHILE DVNKCVIALQ EKDVDGLDRT
AGAIRGRAAR VIHVVTSEMD NYEPGVYTEK VLEATKLLSN TVMPRFTEQV EAAVEALSSD
PAQPMDENEF IDASRLVYDG IRDIRKAVLM IRTPEELDDS DFETEDFDVR SRTSVQTEDD
QLIAGQSARA IMAQLPQEQK AKIAEQVASF QEEKSKLDAE VSKWDDSGND IIVLAKQMCM
IMMEMTDFTR GKGPLKNTSD VISAAKKIAE AGSRMDKLGR TIADHCPDSA CKQDLLAYLQ
RIALYCHQLN ICSKVKAEVQ NLGGELVVSG VDSAMSLIQA AKNLMNAVVQ TVKASYVAST
KYQKSQGMAS LNLPAVSWKM KAPEKKPLVK REKQDETQTK IKRASQKKHV SPVQALSEFK
AMDSI
//
