TCPA_DROME
ID TCPA_DROME Reviewed; 557 AA.
AC P12613; Q9VCZ6;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 04-MAY-2001, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=T-complex protein 1 subunit alpha;
DE Short=TCP-1-alpha;
DE AltName: Full=CCT-alpha;
DE AltName: Full=Chaperonin containing TCP1 subunit 1 {ECO:0000312|FlyBase:FBgn0003676};
GN Name=CCT1 {ECO:0000312|FlyBase:FBgn0003676};
GN Synonyms=CCT-1, T-cp1, Tcp-1 {ECO:0000303|PubMed:3146529};
GN ORFNames=CG5374 {ECO:0000312|FlyBase:FBgn0003676};
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=3146529; DOI=10.1016/0378-1119(88)90029-7;
RA Ursic D., Ganetzky B.;
RT "A Drosophila melanogaster gene encodes a protein homologous to the mouse t
RT complex polypeptide 1.";
RL Gene 68:267-274(1988).
RN [2]
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 [3]
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 [4]
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).
CC -!- FUNCTION: Molecular chaperone; assists the folding of proteins upon ATP
CC hydrolysis. Known to play a role, in vitro, in the folding of actin and
CC tubulin.
CC -!- SUBUNIT: Heterooligomeric complex of about 850 to 900 kDa that forms
CC two stacked rings, 12 to 16 nm in diameter.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR EMBL; M21159; AAA28927.1; -; mRNA.
DR EMBL; AE014297; AAF56009.1; -; Genomic_DNA.
DR EMBL; AY118416; AAM48445.1; -; mRNA.
DR PIR; JT0367; JT0367.
DR RefSeq; NP_524450.2; NM_079726.4.
DR RefSeq; NP_732748.1; NM_170016.2.
DR AlphaFoldDB; P12613; -.
DR SMR; P12613; -.
DR BioGRID; 67604; 39.
DR DIP; DIP-22081N; -.
DR STRING; 7227.FBpp0083683; -.
DR PaxDb; P12613; -.
DR PRIDE; P12613; -.
DR DNASU; 42649; -.
DR EnsemblMetazoa; FBtr0084290; FBpp0083683; FBgn0003676.
DR EnsemblMetazoa; FBtr0084291; FBpp0083684; FBgn0003676.
DR GeneID; 42649; -.
DR KEGG; dme:Dmel_CG5374; -.
DR CTD; 42649; -.
DR FlyBase; FBgn0003676; CCT1.
DR VEuPathDB; VectorBase:FBgn0003676; -.
DR eggNOG; KOG0360; Eukaryota.
DR GeneTree; ENSGT00550000074878; -.
DR HOGENOM; CLU_008891_7_3_1; -.
DR InParanoid; P12613; -.
DR OMA; KNYKNYG; -.
DR OrthoDB; 335406at2759; -.
DR PhylomeDB; P12613; -.
DR BRENDA; 3.6.4.B10; 1994.
DR Reactome; R-DME-390471; Association of TriC/CCT with target proteins during biosynthesis.
DR Reactome; R-DME-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR BioGRID-ORCS; 42649; 1 hit in 1 CRISPR screen.
DR ChiTaRS; T-cp1; fly.
DR GenomeRNAi; 42649; -.
DR PRO; PR:P12613; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0003676; Expressed in eye disc (Drosophila) and 40 other tissues.
DR ExpressionAtlas; P12613; baseline and differential.
DR Genevisible; P12613; DM.
DR GO; GO:0005832; C:chaperonin-containing T-complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR CDD; cd03335; TCP1_alpha; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR012715; Chap_CCT_alpha.
DR InterPro; IPR017998; Chaperone_TCP-1.
DR InterPro; IPR002194; Chaperonin_TCP-1_CS.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR027413; GROEL-like_equatorial_sf.
DR InterPro; IPR027410; TCP-1-like_intermed_sf.
DR PANTHER; PTHR11353; PTHR11353; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00304; TCOMPLEXTCP1.
DR SUPFAM; SSF48592; SSF48592; 1.
DR SUPFAM; SSF52029; SSF52029; 1.
DR SUPFAM; SSF54849; SSF54849; 1.
DR TIGRFAMs; TIGR02340; chap_CCT_alpha; 1.
DR PROSITE; PS00750; TCP1_1; 1.
DR PROSITE; PS00751; TCP1_2; 1.
DR PROSITE; PS00995; TCP1_3; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome.
FT CHAIN 1..557
FT /note="T-complex protein 1 subunit alpha"
FT /id="PRO_0000128310"
FT CONFLICT 17..19
FT /note="GAS -> RRI (in Ref. 1; AAA28927)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="A -> V (in Ref. 1; AAA28927)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="I -> V (in Ref. 1; AAA28927)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="L -> H (in Ref. 1; AAA28927)"
FT /evidence="ECO:0000305"
FT CONFLICT 413
FT /note="A -> R (in Ref. 1; AAA28927)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 557 AA; 59557 MW; 6F4A28237456F3A2 CRC64;
MSTLASPLSI AGTRQSGASV RTQNVMAALS ISNIVKSSLG PVGLDKMLVD DIGDVTVTND
GATILRLLEV EHPAAKVLVE LAQLQDEEVG DGTTSVVILA AELLKNADEL VKQKIHPTSI
ISGYRIACKE ACKYISEHLT APVDELGRDS LINIAKTSMS SKIIGADAEF FSAMVVDAAQ
SVKITDPRGQ AAYSIKAINV LKAHGKSARE SVLIPGYALN CTIASQQMPK KIVNAKIACL
DFSLQKTKMK MGVQVLINDP DKLEAIRARE LDITKERINM ILGTGVNVVL VSGGVDDLCM
KYFVEAGAMA VRRVKKSDLK IIAKATGAAF ITSLTNMDGE ESFDASMVGE AAEVAQERIC
DDELILIKGT KARAAASIIL RGPNDFYCDE MERSVHDALC VVKRVLESKK VVAGGGCVEA
ALSIYLENFA TSLASREQLA IAEFAKSLLV IPKTLSVNAA KDATDLVAKL RSYHNSSQTK
PERSDLKWTG LDLIEGVVRD NKKAGVLEPA MSKIKSLKFA TEAAITILRI DDMIKLNPED
KSGKSYADAC AAGELDG
