TCPZ_YEAST
ID TCPZ_YEAST Reviewed; 546 AA.
AC P39079; D6VSH1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=T-complex protein 1 subunit zeta;
DE Short=TCP-1-zeta;
DE AltName: Full=CCT-zeta;
GN Name=CCT6; Synonyms=TCP20, TCP6; OrderedLocusNames=YDR188W;
GN ORFNames=YD9395.21;
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=8034610; DOI=10.1016/s0021-9258(17)32354-2;
RA Li W.-Z., Lin P., Frydman J., Boal T.R., Cardillo T.S., Richard L.M.,
RA Toth D., Lichtman M.A., Hartl F.-U., Sherman F., Segel G.B.;
RT "Tcp20, a subunit of the eukaryotic TRiC chaperonin from humans and
RT yeast.";
RL J. Biol. Chem. 269:18616-18622(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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}.
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DR EMBL; L27698; AAA35140.1; -; Genomic_DNA.
DR EMBL; Z46727; CAA86694.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12031.1; -; Genomic_DNA.
DR PIR; S48086; S48086.
DR RefSeq; NP_010474.3; NM_001180496.3.
DR PDB; 4V81; X-ray; 3.80 A; F/N/f/n=1-546.
DR PDB; 4V8R; X-ray; 3.80 A; AZ/Az/BZ/Bz=1-546.
DR PDB; 4V94; X-ray; 3.80 A; F/N/f/n=1-546.
DR PDB; 5GW4; EM; 4.70 A; Z/z=1-546.
DR PDB; 5GW5; EM; 4.60 A; Z/z=1-546.
DR PDB; 6KRD; EM; 4.38 A; Z/z=1-546.
DR PDB; 6KRE; EM; 4.45 A; Z/z=1-546.
DR PDB; 6KS6; EM; 2.99 A; Z/z=1-546.
DR PDB; 6KS7; EM; 4.62 A; Z/z=1-546.
DR PDB; 6KS8; EM; 4.69 A; Z/z=1-546.
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; P39079; -.
DR SMR; P39079; -.
DR BioGRID; 32241; 720.
DR ComplexPortal; CPX-2156; Chaperonin-containing T-complex.
DR DIP; DIP-6401N; -.
DR IntAct; P39079; 44.
DR MINT; P39079; -.
DR STRING; 4932.YDR188W; -.
DR iPTMnet; P39079; -.
DR MaxQB; P39079; -.
DR PaxDb; P39079; -.
DR PRIDE; P39079; -.
DR DNASU; 851768; -.
DR EnsemblFungi; YDR188W_mRNA; YDR188W; YDR188W.
DR GeneID; 851768; -.
DR KEGG; sce:YDR188W; -.
DR SGD; S000002596; CCT6.
DR VEuPathDB; FungiDB:YDR188W; -.
DR eggNOG; KOG0359; Eukaryota.
DR HOGENOM; CLU_008891_3_1_1; -.
DR InParanoid; P39079; -.
DR OMA; LHPRIMT; -.
DR BioCyc; YEAST:G3O-29776-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:P39079; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P39079; 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; cd03342; TCP1_zeta; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR012722; Chap_CCT_zeta.
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; TIGR02347; chap_CCT_zeta; 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 Nucleotide-binding; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..546
FT /note="T-complex protein 1 subunit zeta"
FT /id="PRO_0000128362"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT TURN 4..6
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 16..33
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 59..65
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 71..86
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 91..109
FT /evidence="ECO:0007829|PDB:6KS6"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 115..136
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 147..158
FT /evidence="ECO:0007829|PDB:6KS6"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 164..176
FT /evidence="ECO:0007829|PDB:6KS6"
FT TURN 177..180
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 228..236
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 249..255
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 259..284
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 291..299
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 306..311
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 324..331
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 338..342
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 351..359
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 362..368
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 377..381
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 385..407
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 409..413
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 417..425
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 435..439
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 440..450
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 453..462
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 466..482
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:6KS6"
FT TURN 493..496
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 497..499
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 501..504
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 510..528
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 530..535
FT /evidence="ECO:0007829|PDB:6KS6"
SQ SEQUENCE 546 AA; 59924 MW; 7D2A2AB4526D3DB4 CRC64;
MSLQLLNPKA ESLRRDAALK VNVTSAEGLQ SVLETNLGPK GTLKMLVDGA GNIKLTKDGK
VLLTEMQIQS PTAVLIARAA AAQDEITGDG TTTVVCLVGE LLRQAHRFIQ EGVHPRIITD
GFEIARKESM KFLDEFKISK TNLSNDREFL LQVARSSLLT KVDADLTEVL TPIVTDAVLS
VYDAQADNLD LHMVEIMQMQ HLSPKDTTFI KGLVLDHGGR HPDMPTRVKN AYVLILNVSL
EYEKTEVNSG FFYSSADQRD KLAASERKFV DAKLKKIIDL KNEVCGMDPD KGFVIINQKG
IDPMSLDVFA KHNILALRRA KRRNMERLQL VTGGEAQNSV EDLSPQILGF SGLVYQETIG
EEKFTYVTEN TDPKSCTILI KGSTHYALAQ TKDAVRDGLR AVANVLKDKN IIPGAGAFYI
ALSRYLRSAN MNKLGAKGKT KTGIEAFAEA LLVIPKTLVK NSGFDPLDVL AMVEDELDDA
QDSDETRYVG VDLNIGDSCD PTIEGIWDSY RVLRNAITGA TGIASNLLLC DELLRAGRST
LKETPQ
