TCPQ_YEAST
ID TCPQ_YEAST Reviewed; 568 AA.
AC P47079; D6VWG8;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=T-complex protein 1 subunit theta;
DE Short=TCP-1-theta;
DE AltName: Full=CCT-theta;
GN Name=CCT8; OrderedLocusNames=YJL008C; ORFNames=J1374;
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 [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 [2]
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 [3]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-15, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=SUB592;
RX PubMed=12872131; DOI=10.1038/nbt849;
RA Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G.,
RA Roelofs J., Finley D., Gygi S.P.;
RT "A proteomics approach to understanding protein ubiquitination.";
RL Nat. Biotechnol. 21:921-926(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-505, 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).
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterooligomeric complex of about 850 to 900 kDa that forms
CC two stacked rings, 12 to 16 nm in diameter. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR EMBL; Z49284; CAA89300.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08784.1; -; Genomic_DNA.
DR PIR; S56779; S56779.
DR RefSeq; NP_012526.1; NM_001181442.2.
DR PDB; 4V81; X-ray; 3.80 A; H/P/h/p=1-568.
DR PDB; 4V8R; X-ray; 3.80 A; AQ/Aq/BQ/Bq=1-568.
DR PDB; 4V94; X-ray; 3.80 A; H/P/h/p=1-568.
DR PDB; 5GW4; EM; 4.70 A; Q/q=1-568.
DR PDB; 5GW5; EM; 4.60 A; Q/q=1-568.
DR PDB; 6KRD; EM; 4.38 A; Q/q=1-568.
DR PDB; 6KRE; EM; 4.45 A; Q/q=1-568.
DR PDB; 6KS6; EM; 2.99 A; Q/q=1-568.
DR PDB; 6KS7; EM; 4.62 A; Q/q=1-568.
DR PDB; 6KS8; EM; 4.69 A; Q/q=1-568.
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; P47079; -.
DR SMR; P47079; -.
DR BioGRID; 33748; 421.
DR ComplexPortal; CPX-2156; Chaperonin-containing T-complex.
DR DIP; DIP-2697N; -.
DR IntAct; P47079; 100.
DR MINT; P47079; -.
DR STRING; 4932.YJL008C; -.
DR iPTMnet; P47079; -.
DR MaxQB; P47079; -.
DR PaxDb; P47079; -.
DR PRIDE; P47079; -.
DR DNASU; 853447; -.
DR EnsemblFungi; YJL008C_mRNA; YJL008C; YJL008C.
DR GeneID; 853447; -.
DR KEGG; sce:YJL008C; -.
DR SGD; S000003545; CCT8.
DR VEuPathDB; FungiDB:YJL008C; -.
DR eggNOG; KOG0362; Eukaryota.
DR GeneTree; ENSGT00550000074783; -.
DR HOGENOM; CLU_008891_4_2_1; -.
DR InParanoid; P47079; -.
DR OMA; WGLKYAV; -.
DR BioCyc; YEAST:G3O-31485-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-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR PRO; PR:P47079; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47079; protein.
DR GO; GO:0005832; C:chaperonin-containing T-complex; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA: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; cd03341; TCP1_theta; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR012721; Chap_CCT_theta.
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; TIGR02346; chap_CCT_theta; 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; ATP-binding; Chaperone; Cytoplasm; Isopeptide bond;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..568
FT /note="T-complex protein 1 subunit theta"
FT /id="PRO_0000128378"
FT MOD_RES 505
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CROSSLNK 15
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:12872131"
FT HELIX 9..12
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 30..34
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 36..43
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 68..74
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 80..94
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 100..119
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 124..141
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 156..160
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 163..169
FT /evidence="ECO:0007829|PDB:6KS6"
FT TURN 170..173
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 176..189
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:6KS6"
FT TURN 239..242
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 244..252
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 271..293
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 296..303
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 307..315
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 329..336
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 341..343
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 349..351
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 353..356
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 359..370
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 383..389
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 391..412
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:6KS6"
FT TURN 422..424
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 425..440
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 446..454
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 455..457
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 458..465
FT /evidence="ECO:0007829|PDB:6KS6"
FT TURN 466..468
FT /evidence="ECO:0007829|PDB:6KS6"
FT TURN 471..473
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 474..481
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 488..490
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 494..496
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 505..507
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 512..515
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 521..540
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 543..545
FT /evidence="ECO:0007829|PDB:6KS6"
SQ SEQUENCE 568 AA; 61662 MW; 90817CA3151A52FD CRC64;
MSLRLPQNPN AGLFKQGYNS YSNADGQIIK SIAAIRELHQ MCLTSMGPCG RNKIIVNHLG
KIIITNDAAT MLRELDIVHP AVKVLVMATE QQKIDMGDGT NLVMILAGEL LNVSEKLISM
GLSAVEIIQG YNMARKFTLK ELDEMVVGEI TDKNDKNELL KMIKPVISSK KYGSEDILSE
LVSEAVSHVL PVAQQAGEIP YFNVDSIRVV KIMGGSLSNS TVIKGMVFNR EPEGHVKSLS
EDKKHKVAVF TCPLDIANTE TKGTVLLHNA QEMLDFSKGE EKQIDAMMKE IADMGVECIV
AGAGVGELAL HYLNRYGILV LKVPSKFELR RLCRVCGATP LPRLGAPTPE ELGLVETVKT
MEIGGDRVTV FKQEQGEISR TSTIILRGAT QNNLDDIERA IDDGVAAVKG LMKPSGGKLL
PGAGATEIEL ISRITKYGER TPGLLQLAIK QFAVAFEVVP RTLAETAGLD VNEVLPNLYA
AHNVTEPGAV KTDHLYKGVD IDGESDEGVK DIREENIYDM LATKKFAINV ATEAATTVLS
IDQIIMAKKA GGPRAPQGPR PGNWDQED
