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Database: UniProt
Entry: F7DN38_MACMU
LinkDB: F7DN38_MACMU
Original site: F7DN38_MACMU 
ID   F7DN38_MACMU            Unreviewed;       906 AA.
AC   F7DN38; F6UDA1;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 2.
DT   27-MAR-2024, entry version 83.
DE   SubName: Full=Catenin alpha 1 {ECO:0000313|Ensembl:ENSMMUP00000023641.3};
GN   Name=CTNNA1 {ECO:0000313|Ensembl:ENSMMUP00000023641.3,
GN   ECO:0000313|VGNC:VGNC:84291};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000023641.3, ECO:0000313|Proteomes:UP000006718};
RN   [1] {ECO:0000313|Proteomes:UP000006718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17573 {ECO:0000313|Proteomes:UP000006718};
RX   PubMed=17431167; DOI=10.1126/science.1139247;
RA   Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA   Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA   Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA   Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA   Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA   Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA   Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA   Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA   Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA   Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA   Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA   Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA   Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA   Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA   Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA   Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA   Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA   Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA   Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA   Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA   Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA   Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA   Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA   Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA   Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA   Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA   Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA   Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA   Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA   Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA   Kuhn R.M., Smith K.E., Zwieg A.S.;
RT   "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL   Science 316:222-234(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMMUP00000023641.3}
RP   IDENTIFICATION.
RC   STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000023641.3};
RG   Ensembl;
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   STRING; 9544.ENSMMUP00000023641; -.
DR   PaxDb; 9544-ENSMMUP00000023642; -.
DR   Ensembl; ENSMMUT00000021250.4; ENSMMUP00000019871.4; ENSMMUG00000017985.4.
DR   Ensembl; ENSMMUT00000025270.4; ENSMMUP00000023641.3; ENSMMUG00000017985.4.
DR   VEuPathDB; HostDB:ENSMMUG00000017985; -.
DR   VGNC; VGNC:84291; CTNNA1.
DR   eggNOG; KOG3681; Eukaryota.
DR   GeneTree; ENSGT01030000234543; -.
DR   HOGENOM; CLU_015314_2_0_1; -.
DR   OMA; VHMSASQ; -.
DR   Proteomes; UP000006718; Chromosome 6.
DR   Bgee; ENSMMUG00000017985; Expressed in colon and 22 other cell types or tissues.
DR   GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
DR   GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR   GO; GO:0016342; C:catenin complex; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0008013; F:beta-catenin binding; IBA:GO_Central.
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:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
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:UP000006718}.
FT   REGION          864..894
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        864..884
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   906 AA;  100133 MW;  FDBA0E60776C437E CRC64;
     MTAVQAGNIN FKWDPKSLEI RTLAVERLLE PLVTQVTTLV NTNSKGPSNK KRGRSKKAHV
     LAASVEQATE NFLEKGDKIA KESQFLKEEL VAAVEDVRKQ GDLMKTAAGE FADDPCSSVK
     RGNMVRAARA LLSAVTRLLI LADMADVYKL LVQLKVVEDG ILKLRNAGNE QDLGIQYKAL
     KPEVDKLNIM AAKRQQELKD VGHRDQMAAA RGILQKNLPI LYTASQACLQ HPDVAAYKAN
     RDLIYKQLQQ AVTGISNAAQ ATASDDASQH QGGGGGELAY ALNNFDKQII VDPLSFSEER
     FRPSLEERLE SIISGAALMA DSSCTRDDRR ERIVAECNAV RQALQDLLSE YMGNAGRKER
     SDALNSAIDK MTKKTRDLRR QLRKAVMDHV SDSFLETNVP LLVLIEAAKN GNEKEVKEYA
     QVFREHANKL IEVANLACSI SNNEEGVKLV RMSASQLEAL CPQVINAALA LAAKPQSKLA
     QENMDLFKEQ WEKQVRVLTD AVDDITSIDD FLAVSENHIL EDVNKCVIAL QEKDVDGLDR
     TAGAIRGRAA RVIHVVTSEM DNYEPGVYTE KVLEATKLLS NTVMPRFTEQ VEAAVEALSS
     DPAQPMDENE FIDASRLVYD GIRDIRKAVL MIRTPEELDD SDFETEDFDV RSRTSVQTED
     DQLIAGQSAR AIMAQLPQEQ KAKIAEQVAS FQEEKSKLDA EVSKWDDSGN DIIVLAKQMC
     MIMMEMTDFT RGKGPLKNTS DVISAAKKIA EAGSRMDRLG RTIANHCPDS ACKQDLLAYL
     QRIALYCHQL NICSKVKAEV QNLGGELVVS GVDSAMSLIQ AAKNLMNAVV QTVKASYVAS
     TKYQKSQGMA SLNLPAVSWK MKAPEKKPLV KREKQDETQT KIKRASQKKH VNPVQALSEF
     KAMDSI
//
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