TCPD_YEAST
ID TCPD_YEAST Reviewed; 528 AA.
AC P39078; D6VRK5; Q07561;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=T-complex protein 1 subunit delta;
DE Short=TCP-1-delta;
DE AltName: Full=CCT-delta;
GN Name=CCT4; Synonyms=ANC2, TCP4; OrderedLocusNames=YDL143W;
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=7916461; DOI=10.1073/pnas.91.19.9116;
RA Vinh D., Drubin D.G.;
RT "A yeast TCP-1-like protein is required for actin function in vivo.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:9116-9120(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 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
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 -!- MISCELLANEOUS: Present with 5530 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR EMBL; Z33504; CAA83912.1; -; Genomic_DNA.
DR EMBL; Z74191; CAA98716.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11715.1; -; Genomic_DNA.
DR PIR; S67690; S67690.
DR RefSeq; NP_010138.1; NM_001180203.1.
DR PDB; 4V81; X-ray; 3.80 A; D/L/d/l=1-528.
DR PDB; 4V8R; X-ray; 3.80 A; AD/Ad/BD/Bd=1-528.
DR PDB; 4V94; X-ray; 3.80 A; D/L/d/l=1-528.
DR PDB; 5GW4; EM; 4.70 A; D/d=1-528.
DR PDB; 5GW5; EM; 4.60 A; D/d=1-528.
DR PDB; 6KRD; EM; 4.38 A; D/d=1-528.
DR PDB; 6KRE; EM; 4.45 A; D/d=1-528.
DR PDB; 6KS6; EM; 2.99 A; D/d=1-528.
DR PDB; 6KS7; EM; 4.62 A; D/d=1-528.
DR PDB; 6KS8; EM; 4.69 A; D/d=1-528.
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; P39078; -.
DR SMR; P39078; -.
DR BioGRID; 31918; 386.
DR ComplexPortal; CPX-2156; Chaperonin-containing T-complex.
DR DIP; DIP-6753N; -.
DR IntAct; P39078; 50.
DR MINT; P39078; -.
DR STRING; 4932.YDL143W; -.
DR iPTMnet; P39078; -.
DR MaxQB; P39078; -.
DR PaxDb; P39078; -.
DR PRIDE; P39078; -.
DR DNASU; 851412; -.
DR EnsemblFungi; YDL143W_mRNA; YDL143W; YDL143W.
DR GeneID; 851412; -.
DR KEGG; sce:YDL143W; -.
DR SGD; S000002302; CCT4.
DR VEuPathDB; FungiDB:YDL143W; -.
DR eggNOG; KOG0358; Eukaryota.
DR GeneTree; ENSGT00550000074956; -.
DR HOGENOM; CLU_008891_9_1_1; -.
DR InParanoid; P39078; -.
DR OMA; HPAANMI; -.
DR BioCyc; YEAST:G3O-29540-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:P39078; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P39078; 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; cd03338; TCP1_delta; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR012717; Chap_CCT_delta.
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; TIGR02342; chap_CCT_delta; 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; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..528
FT /note="T-complex protein 1 subunit delta"
FT /id="PRO_0000128345"
FT CONFLICT 254
FT /note="V -> A (in Ref. 1; CAA83912)"
FT /evidence="ECO:0000305"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 16..36
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..67
FT /evidence="ECO:0007829|PDB:6KS6"
FT TURN 73..76
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 77..87
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 93..111
FT /evidence="ECO:0007829|PDB:6KS6"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 117..138
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 147..158
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 167..179
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 194..202
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 257..280
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 299..307
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 311..316
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 321..328
FT /evidence="ECO:0007829|PDB:6KS6"
FT TURN 336..338
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 347..355
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 358..364
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 375..383
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 384..406
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 410..412
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 416..429
FT /evidence="ECO:0007829|PDB:6KS6"
FT TURN 430..432
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 435..446
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 449..457
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 462..475
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 480..483
FT /evidence="ECO:0007829|PDB:6KS6"
FT TURN 484..487
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 488..491
FT /evidence="ECO:0007829|PDB:6KS6"
FT TURN 492..496
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 498..500
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 501..518
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 521..527
FT /evidence="ECO:0007829|PDB:6KS6"
SQ SEQUENCE 528 AA; 57604 MW; F01146D76F4E850C CRC64;
MSAKVPSNAT FKNKEKPQEV RKANIIAARS VADAIRTSLG PKGMDKMIKT SRGEIIISND
GHTILKQMAI LHPVARMLVE VSAAQDSEAG DGTTSVVILT GALLGAAERL LNKGIHPTII
ADSFQSAAKR SVDILLEMCH KVSLSDREQL VRAASTSLSS KIVSQYSSFL APLAVDSVLK
ISDENSKNVD LNDIRLVKKV GGTIDDTEMI DGVVLTQTAI KSAGGPTRKE KAKIGLIQFQ
ISPPKPDTEN NIIVNDYRQM DKILKEERAY LLNICKKIKK AKCNVLLIQK SILRDAVNDL
ALHFLSKLNI MVVKDIEREE IEFLSKGLGC KPIADIELFT EDRLGSADLV EEIDSDGSKI
VRVTGIRNNN ARPTVSVVIR GANNMIIDET ERSLHDALCV IRCLVKERGL IAGGGAPEIE
ISRRLSKEAR SMEGVQAFIW QEFASALEVI PTTLAENAGL NSIKVVTELR SKHENGELND
GISVRRSGTT NTYEEHILQP VLVSTSAITL ASECVKSILR IDDIAFSR
