TCPB_YEAST
ID TCPB_YEAST Reviewed; 527 AA.
AC P39076; D6VVE5;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=T-complex protein 1 subunit beta;
DE Short=TCP-1-beta;
DE AltName: Full=CCT-beta;
GN Name=CCT2; Synonyms=BIN3, TCP2; OrderedLocusNames=YIL142W;
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 204511 / S288c / AB972;
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 461-527.
RA Roemer T., Madden K., Chang J., Snyder M.;
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP INTERACTION WITH PLP2.
RX PubMed=17429077; DOI=10.1091/mbc.e07-01-0069;
RA Stirling P.C., Srayko M., Takhar K.S., Pozniakovsky A., Hyman A.A.,
RA Leroux M.R.;
RT "Functional interaction between phosducin-like protein 2 and cytosolic
RT chaperonin is essential for cytoskeletal protein function and cell cycle
RT progression.";
RL Mol. Biol. Cell 18:2336-2345(2007).
RN [8]
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 [9]
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 (By similarity). Interacts
CC with PLP2; this interaction leads to inhibition of CCT complex mediated
CC actin folding (PubMed:17429077). {ECO:0000250|UniProtKB:P78371,
CC ECO:0000269|PubMed:17429077}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR EMBL; X77675; CAA54745.1; -; Genomic_DNA.
DR EMBL; U16761; AAA53433.1; -; Genomic_DNA.
DR EMBL; Z38059; CAA86136.1; -; Genomic_DNA.
DR EMBL; AY723831; AAU09748.1; -; Genomic_DNA.
DR EMBL; U49845; AAA98665.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08411.1; -; Genomic_DNA.
DR PIR; S48232; S48232.
DR RefSeq; NP_012124.1; NM_001179490.1.
DR PDB; 4V81; X-ray; 3.80 A; B/J/b/j=1-527.
DR PDB; 4V8R; X-ray; 3.80 A; AB/Ab/BB/Bb=1-527.
DR PDB; 4V94; X-ray; 3.80 A; B/J/b/j=1-527.
DR PDB; 5GW4; EM; 4.70 A; B/b=1-527.
DR PDB; 5GW5; EM; 4.60 A; B/b=1-527.
DR PDB; 6KRD; EM; 4.38 A; B/b=1-527.
DR PDB; 6KRE; EM; 4.45 A; B/b=1-527.
DR PDB; 6KS6; EM; 2.99 A; B/b=1-527.
DR PDB; 6KS7; EM; 4.62 A; B/b=1-527.
DR PDB; 6KS8; EM; 4.69 A; B/b=1-527.
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; P39076; -.
DR SMR; P39076; -.
DR BioGRID; 34850; 278.
DR ComplexPortal; CPX-2156; Chaperonin-containing T-complex.
DR DIP; DIP-4451N; -.
DR IntAct; P39076; 51.
DR MINT; P39076; -.
DR STRING; 4932.YIL142W; -.
DR iPTMnet; P39076; -.
DR MaxQB; P39076; -.
DR PaxDb; P39076; -.
DR PRIDE; P39076; -.
DR DNASU; 854664; -.
DR EnsemblFungi; YIL142W_mRNA; YIL142W; YIL142W.
DR GeneID; 854664; -.
DR KEGG; sce:YIL142W; -.
DR SGD; S000001404; CCT2.
DR VEuPathDB; FungiDB:YIL142W; -.
DR eggNOG; KOG0363; Eukaryota.
DR GeneTree; ENSGT00550000074930; -.
DR HOGENOM; CLU_008891_6_2_1; -.
DR InParanoid; P39076; -.
DR OMA; YCTGGEI; -.
DR BioCyc; YEAST:G3O-31392-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:P39076; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P39076; 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; cd03336; TCP1_beta; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR012716; Chap_CCT_beta.
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 PANTHER; PTHR11353:SF23; PTHR11353:SF23; 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; TIGR02341; chap_CCT_beta; 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..527
FT /note="T-complex protein 1 subunit beta"
FT /id="PRO_0000128320"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:6KS6"
FT TURN 15..20
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 21..34
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 60..66
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 74..87
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 92..111
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 117..137
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 146..163
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 170..182
FT /evidence="ECO:0007829|PDB:6KS6"
FT TURN 183..186
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 193..201
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 243..248
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 250..254
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 256..277
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 282..288
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 292..300
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 311..321
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 332..335
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 345..348
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 351..355
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 363..373
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 374..396
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 406..419
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 426..437
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 439..447
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 452..464
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 470..473
FT /evidence="ECO:0007829|PDB:6KS6"
FT TURN 474..477
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 478..481
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 482..485
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 488..490
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 491..508
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 511..516
FT /evidence="ECO:0007829|PDB:6KS6"
SQ SEQUENCE 527 AA; 57203 MW; C5DB2BC3660EC7E6 CRC64;
MSVQIFGDQV TEERAENARL SAFVGAIAVG DLVKSTLGPK GMDKLLQSAS SNTCMVTNDG
ATILKSIPLD NPAAKVLVNI SKVQDDEVGD GTTSVTVLSA ELLREAEKLI DQSKIHPQTI
IEGYRLASAA ALDALTKAAV DNSHDKTMFR EDLIHIAKTT LSSKILSQDK DHFAELATNA
ILRLKGSTNL EHIQIIKILG GKLSDSFLDE GFILAKKFGN NQPKRIENAK ILIANTTLDT
DKVKIFGTKF KVDSTAKLAQ LEKAEREKMK NKIAKISKFG INTFINRQLI YDYPEQLFTD
LGINSIEHAD FEGVERLALV TGGEVVSTFD EPSKCKLGEC DVIEEIMLGE QPFLKFSGCK
AGEACTIVLR GATDQTLDEA ERSLHDALSV LSQTTKETRT VLGGGCAEMV MSKAVDTEAQ
NIDGKKSLAV EAFARALRQL PTILADNAGF DSSELVSKLR SSIYNGISTS GLDLNNGTIA
DMRQLGIVES YKLKRAVVSS ASEAAEVLLR VDNIIRARPR TANRQHM
