ID   CTNA_DROME              Reviewed;         917 AA.
AC   P35220; Q960Y2; Q9W5V9;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 2.
DT   04-NOV-2026, entry version 200.
DE   RecName: Full=Catenin alpha;
GN   Name=alpha-Cat {ECO:0000312|FlyBase:FBgn0010215};
GN   ORFNames=CG17947 {ECO:0000312|FlyBase:FBgn0010215};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida;
OC   Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota;
OC   Aparaglossata; Panorpida; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8501118; DOI=10.1083/jcb.121.5.1133;
RA   Oda H., Uemura T., Shiomi K., Nagafuchi A., Tsukita S., Takeichi M.;
RT   "Identification of a Drosophila homologue of alpha-catenin and its
RT   association with the armadillo protein.";
RL   J. Cell Biol. 121:1133-1140(1993).
RN   [2]
RP   SEQUENCE REVISION TO N-TERMINUS.
RA   Takeichi M.;
RL   Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-643; THR-645; SER-659 AND
RP   SER-662, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18327897; DOI=10.1021/pr700696a;
RA   Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT   "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL   J. Proteome Res. 7:1675-1682(2008).
RN   [7]
RP   PHOSPHORYLATION, SUBCELLULAR LOCATION, INTERACTION WITH ARM, AND
RP   MUTAGENESIS OF 632-VAL--PRO-674; 637-SER--THR-669 AND THR-645.
RX   PubMed=25653389; DOI=10.1242/jcs.163824;
RA   Escobar D.J., Desai R., Ishiyama N., Folmsbee S.S., Novak M.N.,
RA   Flozak A.S., Daugherty R.L., Mo R., Nanavati D., Sarpal R., Leckband D.,
RA   Ikura M., Tepass U., Gottardi C.J.;
RT   "alpha-Catenin phosphorylation promotes intercellular adhesion through a
RT   dual-kinase mechanism.";
RL   J. Cell Sci. 128:1150-1165(2015).
RN   [8]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=25739458; DOI=10.1091/mbc.e14-08-1266;
RA   Verboon J.M., Rahe T.K., Rodriguez-Mesa E., Parkhurst S.M.;
RT   "Wash functions downstream of Rho1 GTPase in a subset of Drosophila immune
RT   cell developmental migrations.";
RL   Mol. Biol. Cell 26:1665-1674(2015).
CC   -!- FUNCTION: Associates with the cytoplasmic domain of a variety of
CC       cadherins. The association of catenins to cadherins produces a complex
CC       which is linked to the actin filament network, and which seems to be of
CC       primary importance for cadherins cell-adhesion properties.
CC   -!- SUBUNIT: Interacts with arm/armadillo protein.
CC       {ECO:0000269|PubMed:25653389}.
CC   -!- INTERACTION:
CC       P35220; P35220: alpha-Cat; NbExp=2; IntAct=EBI-126806, EBI-126806;
CC       P35220; P18824: arm; NbExp=4; IntAct=EBI-126806, EBI-216128;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell
CC       junction, adherens junction {ECO:0000269|PubMed:25653389}. Cell
CC       membrane {ECO:0000269|PubMed:25653389}; Peripheral membrane protein
CC       {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell junction.
CC       Note=Found only at cell-cell boundaries.
CC   -!- DEVELOPMENTAL STAGE: Present at all stages, but reached the highest
CC       levels during early to mid-embryogenesis.
CC   -!- PTM: Rapidly phosphorylated by CK2 and more slowly by CK1.
CC       {ECO:0000269|PubMed:25653389}.
CC   -!- DISRUPTION PHENOTYPE: Mutants die at a late embryonic stage with severe
CC       defects in head morphogenesis (PubMed:25653389). In embryos, RNAi-
CC       mediated knockdown in the hemocytes has no effect on their
CC       developmental migration during stages 10-14 of embryogenesis
CC       (PubMed:25739458). {ECO:0000269|PubMed:25653389,
CC       ECO:0000269|PubMed:25739458}.
CC   -!- SIMILARITY: Belongs to the vinculin/alpha-catenin family.
CC       {ECO:0000305}.
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DR   EMBL; D13964; BAA03067.2; -; mRNA.
DR   EMBL; AE014296; AAF45466.1; -; Genomic_DNA.
DR   EMBL; AY051780; AAK93204.1; -; mRNA.
DR   PIR; A40694; A40694.
DR   RefSeq; NP_524219.1; NM_079495.3.
DR   AlphaFoldDB; P35220; -.
DR   SMR; P35220; -.
DR   BioGRID; 65744; 23.
DR   DIP; DIP-21662N; -.
DR   FunCoup; P35220; 271.
DR   IntAct; P35220; 9.
DR   STRING; 7227.FBpp0070037; -.
DR   iPTMnet; P35220; -.
DR   PaxDb; 7227-FBpp0070037; -.
DR   PeptideAtlas; P35220; -.
DR   EnsemblMetazoa; FBtr0070038; FBpp0070037; FBgn0010215.
DR   GeneID; 40517; -.
DR   KEGG; dme:Dmel_CG17947; -.
DR   AGR; FB:FBgn0010215; -.
DR   CTD; 40517; -.
DR   FlyBase; FBgn0010215; alpha-Cat.
DR   VEuPathDB; VectorBase:FBgn0010215; -.
DR   eggNOG; KOG3681; Eukaryota.
DR   HOGENOM; CLU_015314_2_0_1; -.
DR   InParanoid; P35220; -.
DR   OMA; AAEMVCV; -.
DR   OrthoDB; 6376697at2759; -.
DR   PhylomeDB; P35220; -.
DR   Reactome; R-DME-5218920; VEGFR2 mediated vascular permeability.
DR   Reactome; R-DME-525793; Myogenesis.
DR   Reactome; R-DME-9764561; Regulation of CDH1 Function.
DR   Reactome; R-DME-9958825; Activation of STAT3 by cadherin engagement.
DR   SignaLink; P35220; -.
DR   BioGRID-ORCS; 40517; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 40517; -.
DR   PRO; PR:P35220; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0010215; Expressed in eye disc (Drosophila) and 286 other cell types or tissues.
DR   ExpressionAtlas; P35220; baseline and differential.
DR   GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
DR   GO; GO:0005912; C:adherens junction; IDA:FlyBase.
DR   GO; GO:0016342; C:catenin complex; IDA:FlyBase.
DR   GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
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:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0034333; P:adherens junction assembly; IMP:FlyBase.
DR   GO; GO:0034332; P:adherens junction organization; IMP:FlyBase.
DR   GO; GO:0003383; P:apical constriction; IMP:FlyBase.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR   GO; GO:0046664; P:dorsal closure, amnioserosa morphology change; IMP:FlyBase.
DR   GO; GO:0060323; P:head morphogenesis; IMP:FlyBase.
DR   FunFam; 1.20.120.230:FF:000020; Catenin alpha; 1.
DR   FunFam; 1.20.120.230:FF:000006; Catenin alpha 1; 1.
DR   FunFam; 1.20.120.230:FF:000007; Catenin alpha 1; 1.
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:SF9; CATENIN ALPHA; 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   1: Evidence at protein level;
KW   Cell adhesion; Cell junction; Cell membrane; Cytoplasm; Cytoskeleton;
KW   Membrane; Phosphoprotein; Reference proteome.
FT   CHAIN           1..917
FT                   /note="Catenin alpha"
FT                   /id="PRO_0000064260"
FT   REGION          878..905
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        878..890
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         643
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         645
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         659
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         662
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MUTAGEN         632..674
FT                   /note="Missing: Decreases animal survival. No effect on
FT                   head morphogenesis."
FT                   /evidence="ECO:0000269|PubMed:25653389"
FT   MUTAGEN         637..669
FT                   /note="SSEDLDTDTEFEPVEDLTLETRSRSSAHTGDQT->AAEDLDADAEFEPVEDL
FT                   ALEARARAAAHAGDQA: Decreases animal survival. No effect on
FT                   head morphogenesis."
FT                   /evidence="ECO:0000269|PubMed:25653389"
FT   MUTAGEN         637..669
FT                   /note="SSEDLDTDTEFEPVEDLTLETRSRSSAHTGDQT->DDEDLDDDDEFEPVEDL
FT                   DLEDRDRDDAHDGDQD: Decreases animal survival. No effect on
FT                   head morphogenesis."
FT                   /evidence="ECO:0000269|PubMed:25653389"
FT   MUTAGEN         645
FT                   /note="T->A: Decreases animal survival. No effect on head
FT                   morphogenesis."
FT                   /evidence="ECO:0000269|PubMed:25653389"
FT   MUTAGEN         645
FT                   /note="T->D: Decreases animal survival. No effect on head
FT                   morphogenesis."
FT                   /evidence="ECO:0000269|PubMed:25653389"
FT   CONFLICT        711
FT                   /note="F -> S (in Ref. 5; AAK93204)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   917 AA;  102444 MW;  1F0B243DE7474E6F CRC64;
     MLKPDKMGTL TDFGQIALKW DPKNLEIRTM SVEKTLEPLV LQVTTLVNTK GPSKKKKGKS
     KRASALVAAV EKATENFIQK GEQIAYENPD ITQEMLTAVD EVKKTGDAMS IAAREFSEDP
     CSSLKRGNMV RAARNLLSAV TRLLILADMV DVHLLLKSLH IVEDDLNKLK NASSQDELMD
     NMRQFGRNAG ELIKQAAKRQ QELKDPQLRD DLAAARAMLK KHSTMLLTAS KVYVRHPELD
     LAKVNRDFIL KQVCDAVNTI SDVAQGKSSQ PTDIYSGAGE LAAALDDFDE GIVMDPMTYS
     EKRSRQLLEE RLESIISAAA LMADADCTRD ERRERIVAEC NAVRQALQDL LSEYMSNMSQ
     KDNSPGLSRA IDQMCRKTRD LRRQLRKAVV DHVSDSFLET TTPLLDLIEA AKSGNEKKVR
     EKSEIFTKHA EKLVEVANLV CSMSNNEDGV KMVRYAAAQI ESLCPQVINA ASILTVRPNS
     KVAQENMTTY RQAWEVQVRI LTEAVDDITT IDDFLAVSEN HILEDVNKCV MALQVGDARD
     LRATAGAIQG RSSRVCNVVE AEMDNYEPCI YTKRVLEAVK VLRDQVMMKF DQRVGAAVGA
     LSNNSNKDVD ENDFIDASRL VYDGVREIRR AVLMNRSSED LDTDTEFEPV EDLTLETRSR
     SSAHTGDQTV DEYPDISGIC TAREAMRKMT EEDKQKIAQQ VELFRREKLT FDSEVAKWDD
     TGNDIIFLAK HMCMIMMEMT DFTRGRGPLK TTMDVINAAK KISEAGTKLD KLTREIAEQC
     PESSTKKDLL AYLQRIALYC HQIQITSKVK ADVQNISGEL IVSGLDSATS LIQAAKNLMN
     AVVLTVKYSY VASTKYTRQG TVSSPIVVWK MKAPEKKPLV RPEKPEEVRA KVRKGSQKKV
     QNPIHALSEF QSPADAV
//