TCPG_DROME
ID TCPG_DROME Reviewed; 544 AA.
AC P48605; Q9VER9;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=T-complex protein 1 subunit gamma;
DE Short=TCP-1-gamma;
DE AltName: Full=CCT-gamma {ECO:0000303|PubMed:8666276};
DE AltName: Full=Chaperonin containing TCP1 subunit 3 {ECO:0000312|FlyBase:FBgn0015019};
GN Name=CCT3 {ECO:0000312|FlyBase:FBgn0015019};
GN Synonyms=Cctg {ECO:0000303|PubMed:8666276};
GN ORFNames=CG8977 {ECO:0000312|FlyBase:FBgn0015019};
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 [GENOMIC DNA].
RC STRAIN=Canton-S;
RX PubMed=7667301; DOI=10.1073/pnas.92.18.8398;
RA Martin C.H., Mayeda C.A., Davis C.A., Ericsson C.L., Knafels J.D.,
RA Mathog D.R., Celniker S.E., Lewis E.B., Palazzolo M.J.;
RT "Complete sequence of the bithorax complex of Drosophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:8398-8402(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8666276; DOI=10.1016/0378-1119(96)00097-2;
RA Walkley N.A., Malik A.N.;
RT "Drosophila melanogaster P1 genomic clone DS05563 contains the chaperonin-
RT encoding gene Cctg.";
RL Gene 171:221-223(1996).
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).
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; U31961; AAA84416.1; -; Genomic_DNA.
DR EMBL; X95602; CAA64860.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF55350.1; -; Genomic_DNA.
DR EMBL; AY089543; AAL90281.1; -; mRNA.
DR RefSeq; NP_001189236.1; NM_001202307.2.
DR RefSeq; NP_001189237.1; NM_001202308.2.
DR RefSeq; NP_650572.2; NM_142315.4.
DR RefSeq; NP_732167.1; NM_169727.2.
DR AlphaFoldDB; P48605; -.
DR SMR; P48605; -.
DR BioGRID; 67074; 93.
DR DIP; DIP-20434N; -.
DR IntAct; P48605; 16.
DR MINT; P48605; -.
DR STRING; 7227.FBpp0082787; -.
DR PaxDb; P48605; -.
DR PRIDE; P48605; -.
DR DNASU; 42029; -.
DR EnsemblMetazoa; FBtr0083337; FBpp0082787; FBgn0015019.
DR EnsemblMetazoa; FBtr0083338; FBpp0082788; FBgn0015019.
DR EnsemblMetazoa; FBtr0302370; FBpp0291565; FBgn0015019.
DR EnsemblMetazoa; FBtr0302371; FBpp0291566; FBgn0015019.
DR GeneID; 42029; -.
DR KEGG; dme:Dmel_CG8977; -.
DR CTD; 7203; -.
DR FlyBase; FBgn0015019; CCT3.
DR VEuPathDB; VectorBase:FBgn0015019; -.
DR eggNOG; KOG0364; Eukaryota.
DR GeneTree; ENSGT00570000079224; -.
DR HOGENOM; CLU_008891_7_3_1; -.
DR InParanoid; P48605; -.
DR OMA; RYCRIEK; -.
DR OrthoDB; 391677at2759; -.
DR PhylomeDB; P48605; -.
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 SignaLink; P48605; -.
DR BioGRID-ORCS; 42029; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 42029; -.
DR PRO; PR:P48605; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0015019; Expressed in egg cell and 59 other tissues.
DR ExpressionAtlas; P48605; baseline and differential.
DR Genevisible; P48605; DM.
DR GO; GO:0005832; C:chaperonin-containing T-complex; ISS: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:0035149; P:lumen formation, open tracheal system; HMP:FlyBase.
DR GO; GO:0006457; P:protein folding; ISS:FlyBase.
DR GO; GO:0007430; P:terminal branching, open tracheal system; HMP:FlyBase.
DR CDD; cd03337; TCP1_gamma; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR012719; Chap_CCT_gamma.
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; TIGR02344; chap_CCT_gamma; 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; Disulfide bond; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..544
FT /note="T-complex protein 1 subunit gamma"
FT /id="PRO_0000128327"
FT REGION 525..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 368..374
FT /evidence="ECO:0000250"
FT CONFLICT 12
FT /note="S -> SD (in Ref. 2; CAA64860)"
FT /evidence="ECO:0000305"
FT CONFLICT 35..47
FT /note="Missing (in Ref. 1; AAA84416)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 544 AA; 59395 MW; DD5E635809B322C2 CRC64;
MFGGQQPILV LSQNTKRESG RKVQLENIQA GKAIADVIRT CLGPQAMLKM LMDPMGGIVM
TNDGNAILRE ITVQHPAAKS MIEIARTQDE EVGDGTTSVI VLAGEMLAAA EPFLQQQIHP
TVIIRAYREA LEDIVGHLQS QLSIQLDVKD KAKMADVVKA CVGTKFIGKW SDLAVKIALD
AVETVTLSEN GRLEVDIKRY AKVEKIPGGA IEESCVLKGV MINKDVTHPK MRRLIENPRI
VLLDCSLEYK KGESQTNVEI IGEQDFTRML QIEEEFVQRI CADIIAVKPD LVFTEKGVSD
LAQHYLLKAG ITAIRRLRKT DNLRIARACG ATIVNRTEEL TEKDVGTGAG LFEVKKIGDE
YFTFVTECKE PKACTILLRG ASKDILNETE RNLQDALHVA RNLVLEPRLV AGGGAVEMAA
SQLLTRKQVK GPYTAVAHAL EIIPRTLAQN CGANTIRALT ALRAKHASHT GDGVCAWGID
GESGEIVDMN VKNIWEPLAV KLQTYKTAVE TAILLLRIDD IVSGSKKRGG NEPTNPAAMA
QGQE
