CTNA_DROME
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 03-AUG-2022, entry version 187.
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; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; 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=3; 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 IntAct; P35220; 9.
DR STRING; 7227.FBpp0070037; -.
DR iPTMnet; P35220; -.
DR PaxDb; P35220; -.
DR PRIDE; P35220; -.
DR EnsemblMetazoa; FBtr0070038; FBpp0070037; FBgn0010215.
DR GeneID; 40517; -.
DR KEGG; dme:Dmel_CG17947; -.
DR CTD; 40517; -.
DR FlyBase; FBgn0010215; alpha-Cat.
DR VEuPathDB; VectorBase:FBgn0010215; -.
DR eggNOG; KOG3681; Eukaryota.
DR GeneTree; ENSGT01030000234543; -.
DR HOGENOM; CLU_015314_2_0_1; -.
DR InParanoid; P35220; -.
DR OMA; QDELMNN; -.
DR PhylomeDB; P35220; -.
DR Reactome; R-DME-418990; Adherens junctions interactions.
DR Reactome; R-DME-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-DME-525793; Myogenesis.
DR SignaLink; P35220; -.
DR BioGRID-ORCS; 40517; 0 hits in 3 CRISPR screens.
DR ChiTaRS; alpha-Cat; fly.
DR GenomeRNAi; 40517; -.
DR PRO; PR:P35220; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0010215; Expressed in eye disc (Drosophila) and 27 other tissues.
DR ExpressionAtlas; P35220; baseline and differential.
DR Genevisible; P35220; DM.
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:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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 InterPro; IPR036723; Alpha-catenin/vinculin-like_sf.
DR InterPro; IPR001033; Alpha_catenin.
DR InterPro; IPR006077; Vinculin/catenin.
DR InterPro; IPR000633; Vinculin_CS.
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; 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..894
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
