TCPG_YEAST
ID TCPG_YEAST Reviewed; 534 AA.
AC P39077; D6VWG3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=T-complex protein 1 subunit gamma;
DE Short=TCP-1-gamma;
DE AltName: Full=CCT-gamma;
GN Name=CCT3; Synonyms=BIN2, TCP3; OrderedLocusNames=YJL014W; ORFNames=J1336;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7916460; DOI=10.1073/pnas.91.19.9111;
RA Chen X., Sullivan D.S., Huffaker T.C.;
RT "Two yeast genes with similarity to TCP-1 are required for microtubule and
RT actin function in vivo.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:9111-9115(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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. In yeast may play a role in mitotic spindle formation.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U09480; AAA21658.1; -; Genomic_DNA.
DR EMBL; Z49289; CAA89305.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08779.1; -; Genomic_DNA.
DR PIR; S56785; S56785.
DR RefSeq; NP_012520.1; NM_001181448.1.
DR PDB; 4V81; X-ray; 3.80 A; C/K/c/k=1-534.
DR PDB; 4V8R; X-ray; 3.80 A; AG/Ag/BG/Bg=1-534.
DR PDB; 4V94; X-ray; 3.80 A; C/K/c/k=1-534.
DR PDB; 5GW4; EM; 4.70 A; G/g=1-534.
DR PDB; 5GW5; EM; 4.60 A; G/g=1-534.
DR PDB; 6KRD; EM; 4.38 A; G/g=1-534.
DR PDB; 6KRE; EM; 4.45 A; G/g=1-534.
DR PDB; 6KS6; EM; 2.99 A; G/g=1-534.
DR PDB; 6KS7; EM; 4.62 A; G/g=1-534.
DR PDB; 6KS8; EM; 4.69 A; G/g=1-534.
DR PDBsum; 4V81; -.
DR PDBsum; 4V8R; -.
DR PDBsum; 4V94; -.
DR PDBsum; 5GW4; -.
DR PDBsum; 5GW5; -.
DR PDBsum; 6KRD; -.
DR PDBsum; 6KRE; -.
DR PDBsum; 6KS6; -.
DR PDBsum; 6KS7; -.
DR PDBsum; 6KS8; -.
DR AlphaFoldDB; P39077; -.
DR SMR; P39077; -.
DR BioGRID; 33741; 301.
DR ComplexPortal; CPX-2156; Chaperonin-containing T-complex.
DR DIP; DIP-6400N; -.
DR IntAct; P39077; 34.
DR MINT; P39077; -.
DR STRING; 4932.YJL014W; -.
DR CarbonylDB; P39077; -.
DR iPTMnet; P39077; -.
DR MaxQB; P39077; -.
DR PaxDb; P39077; -.
DR PRIDE; P39077; -.
DR DNASU; 853438; -.
DR EnsemblFungi; YJL014W_mRNA; YJL014W; YJL014W.
DR GeneID; 853438; -.
DR KEGG; sce:YJL014W; -.
DR SGD; S000003551; CCT3.
DR VEuPathDB; FungiDB:YJL014W; -.
DR eggNOG; KOG0364; Eukaryota.
DR GeneTree; ENSGT00570000079224; -.
DR HOGENOM; CLU_008891_7_3_1; -.
DR InParanoid; P39077; -.
DR OMA; RYCRIEK; -.
DR BioCyc; YEAST:G3O-31489-MON; -.
DR BRENDA; 3.6.4.B10; 984.
DR Reactome; R-SCE-390471; Association of TriC/CCT with target proteins during biosynthesis.
DR Reactome; R-SCE-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR PRO; PR:P39077; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P39077; protein.
DR GO; GO:0005832; C:chaperonin-containing T-complex; IDA:SGD.
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; IDA:SGD.
DR GO; GO:0051086; P:chaperone mediated protein folding independent of cofactor; IDA:ComplexPortal.
DR GO; GO:0006457; P:protein folding; IDA:SGD.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Chaperone; Cytoplasm;
KW Disulfide bond; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..534
FT /note="T-complex protein 1 subunit gamma"
FT /id="PRO_0000128331"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT DISULFID 371..377
FT /evidence="ECO:0000250"
FT CONFLICT 25..26
FT /note="IT -> HA (in Ref. 1; AAA21658)"
FT /evidence="ECO:0000305"
FT CONFLICT 86..89
FT /note="DEEV -> ERRG (in Ref. 1; AAA21658)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="L -> F (in Ref. 1; AAA21658)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="K -> M (in Ref. 1; AAA21658)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="Q -> L (in Ref. 1; AAA21658)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="Missing (in Ref. 1; AAA21658)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="G -> A (in Ref. 1; AAA21658)"
FT /evidence="ECO:0000305"
FT STRAND 7..10
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 18..34
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 61..66
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 73..79
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 81..88
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 93..107
FT /evidence="ECO:0007829|PDB:6KS6"
FT TURN 109..114
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 118..139
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 148..159
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 163..167
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 168..182
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 243..246
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 260..263
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 266..287
FT /evidence="ECO:0007829|PDB:6KS6"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 293..299
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 304..308
FT /evidence="ECO:0007829|PDB:6KS6"
FT TURN 309..313
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 322..332
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 340..342
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 353..359
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 364..369
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 377..382
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 386..408
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 411..414
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 418..434
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 439..448
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 451..460
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 464..475
FT /evidence="ECO:0007829|PDB:6KS6"
FT TURN 476..478
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 486..488
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 494..497
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 500..502
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 503..520
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 523..527
FT /evidence="ECO:0007829|PDB:6KS6"
SQ SEQUENCE 534 AA; 58814 MW; 5C5AFF3D67D9A3B6 CRC64;
MQAPVVFMNA SQERTTGRQA QISNITAAKA VADVIRTCLG PKAMLKMLLD PMGGLVLTND
GHAILREIDV AHPAAKSMLE LSRTQDEEVG DGTTTVIILA GEILAQCAPY LIEKNIHPVI
IIQALKKALT DALEVIKQVS KPVDVENDAA MKKLIQASIG TKYVIHWSEK MCELALDAVK
TVRKDLGQTV EGEPNFEIDI KRYVRVEKIP GGDVLDSRVL KGVLLNKDVV HPKMSRHIEN
PRVVLLDCPL EYKKGESQTN IEIEKEEDWN RILQIEEEQV QLMCEQILAV RPTLVITEKG
VSDLAQHYLL KGGCSVLRRV KKSDNNRIAR VTGATIVNRV EDLKESDVGT NCGLFKVEMI
GDEYFSFLDN CKEPKACTIM LRGGSKDILN EIDRNLQDAM AVARNVMLSP SLSPGGGATE
MAVSVKLAEK AKQLEGIQQW PYQAVADAME CIPRTLIQNA GGDPIRLLSQ LRAKHAQGNF
TTGIDGDKGK IVDMVSYGIW EPEVIKQQSV KTAIESACLL LRVDDIVSGV RKQE
