TCPA_YEAST
ID TCPA_YEAST Reviewed; 559 AA.
AC P12612; D6VSJ6;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=T-complex protein 1 subunit alpha;
DE Short=TCP-1-alpha;
DE AltName: Full=CCT-alpha;
GN Name=TCP1; Synonyms=CCT1; OrderedLocusNames=YDR212W;
GN ORFNames=YD8142.13, YD8142B.04;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1901944; DOI=10.1128/mcb.11.5.2629-2640.1991;
RA Ursic D., Culbertson M.R.;
RT "The yeast homolog to mouse Tcp-1 affects microtubule-mediated processes.";
RL Mol. Cell. Biol. 11:2629-2640(1991).
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 MUTAGENESIS.
RX PubMed=7908441; DOI=10.1073/pnas.91.7.2743;
RA Miklos D., Caplan S., Mertens D., Hynes G., Pitluk Z., Kashi Y.,
RA Harrison-Lavoie K., Stevenson S., Brown C., Barrell B.G., Horwich A.L.,
RA Willison K.;
RT "Primary structure and function of a second essential member of the
RT heterooligomeric TCP1 chaperonin complex of yeast, TCP1 beta.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:2743-2747(1994).
RN [5]
RP IDENTIFICATION BY 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 [6]
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 -!- INTERACTION:
CC P12612; P60010: ACT1; NbExp=3; IntAct=EBI-19045, EBI-2169;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR EMBL; M21160; AAA35139.1; -; Genomic_DNA.
DR EMBL; Z68194; CAA92355.1; -; Genomic_DNA.
DR EMBL; Z68195; CAA92363.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12056.1; -; Genomic_DNA.
DR PIR; A39793; A39793.
DR RefSeq; NP_010498.1; NM_001180520.1.
DR PDB; 4V81; X-ray; 3.80 A; A/I/a/i=1-559.
DR PDB; 4V8R; X-ray; 3.80 A; AA/Aa/BA/Ba=1-559.
DR PDB; 4V94; X-ray; 3.80 A; A/I/a/i=1-559.
DR PDB; 5GW4; EM; 4.70 A; A/a=1-559.
DR PDB; 5GW5; EM; 4.60 A; A/a=1-559.
DR PDB; 6KRD; EM; 4.38 A; A/a=1-559.
DR PDB; 6KRE; EM; 4.45 A; A/a=1-559.
DR PDB; 6KS6; EM; 2.99 A; A/a=1-559.
DR PDB; 6KS7; EM; 4.62 A; A/a=1-559.
DR PDB; 6KS8; EM; 4.69 A; A/a=1-559.
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; P12612; -.
DR SMR; P12612; -.
DR BioGRID; 32266; 525.
DR ComplexPortal; CPX-2156; Chaperonin-containing T-complex.
DR DIP; DIP-2965N; -.
DR IntAct; P12612; 55.
DR MINT; P12612; -.
DR STRING; 4932.YDR212W; -.
DR iPTMnet; P12612; -.
DR MaxQB; P12612; -.
DR PaxDb; P12612; -.
DR PRIDE; P12612; -.
DR DNASU; 851798; -.
DR EnsemblFungi; YDR212W_mRNA; YDR212W; YDR212W.
DR GeneID; 851798; -.
DR KEGG; sce:YDR212W; -.
DR SGD; S000002620; TCP1.
DR VEuPathDB; FungiDB:YDR212W; -.
DR eggNOG; KOG0360; Eukaryota.
DR GeneTree; ENSGT00550000074878; -.
DR HOGENOM; CLU_008891_5_1_1; -.
DR InParanoid; P12612; -.
DR OMA; KNYKNYG; -.
DR BioCyc; YEAST:G3O-29794-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:P12612; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P12612; protein.
DR GO; GO:0005832; C:chaperonin-containing T-complex; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; 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; 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 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Chaperone; Cytoplasm;
KW Nucleotide-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..559
FT /note="T-complex protein 1 subunit alpha"
FT /id="PRO_0000128315"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MUTAGEN 48
FT /note="G->E: Temperature-sensitive."
FT /evidence="ECO:0000269|PubMed:7908441"
FT CONFLICT 530
FT /note="S -> L (in Ref. 1; AAA35139)"
FT /evidence="ECO:0000305"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:6KS6"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 15..20
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 23..42
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 66..72
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 80..93
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 98..117
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 122..143
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 156..164
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 168..172
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 173..186
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:6KS6"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 203..211
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 218..225
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 269..291
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 294..300
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 304..312
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 323..333
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 338..341
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 344..347
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 352..354
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 359..366
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 369..375
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 384..391
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 392..414
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 418..420
FT /evidence="ECO:0007829|PDB:6KS6"
FT TURN 421..423
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 424..440
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 444..454
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 457..464
FT /evidence="ECO:0007829|PDB:6KS6"
FT TURN 465..467
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 470..485
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 499..503
FT /evidence="ECO:0007829|PDB:6KS6"
FT TURN 504..507
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 508..511
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 512..515
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 518..520
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 521..539
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 541..546
FT /evidence="ECO:0007829|PDB:6KS6"
SQ SEQUENCE 559 AA; 60481 MW; 02C625D329359E61 CRC64;
MSQLFNNSRS DTLFLGGEKI SGDDIRNQNV LATMAVANVV KSSLGPVGLD KMLVDDIGDF
TVTNDGATIL SLLDVQHPAG KILVELAQQQ DREIGDGTTS VVIIASELLK RANELVKNKI
HPTTIITGFR VALREAIRFI NEVLSTSVDT LGKETLINIA KTSMSSKIIG ADSDFFSNMV
VDALLAVKTQ NSKGEIKYPV KAVNVLKAHG KSATESLLVP GYALNCTVAS QAMPKRIAGG
NVKIACLDLN LQKARMAMGV QINIDDPEQL EQIRKREAGI VLERVKKIID AGAQVVLTTK
GIDDLCLKEF VEAKIMGVRR CKKEDLRRIA RATGATLVSS MSNLEGEETF ESSYLGLCDE
VVQAKFSDDE CILIKGTSKH SSSSIILRGA NDYSLDEMER SLHDSLSVVK RTLESGNVVP
GGGCVEAALN IYLDNFATTV GSREQLAIAE FAAALLIIPK TLAVNAAKDS SELVAKLRSY
HAASQMAKPE DVKRRSYRNY GLDLIRGKIV DEIHAGVLEP TISKVKSLKS ALEACVAILR
IDTMITVDPE PPKEDPHDH
