TCPH_YEAST
ID TCPH_YEAST Reviewed; 550 AA.
AC P42943; D6VW73;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=T-complex protein 1 subunit eta;
DE Short=TCP-1-eta;
DE AltName: Full=CCT-eta;
GN Name=CCT7; OrderedLocusNames=YJL111W; ORFNames=J0804;
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 96604 / S288c / FY1679;
RX PubMed=7483851; DOI=10.1002/yea.320110909;
RA Rasmussen S.W.;
RT "A 37.5 kb region of yeast chromosome X includes the SME1, MEF2, GSH1 and
RT CSD3 genes, a TCP-1-related gene, an open reading frame similar to the
RT DAL80 gene, and a tRNA(Arg).";
RL Yeast 11:873-883(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8948101;
RX DOI=10.1002/(sici)1097-0061(199611)12:14<1471::aid-yea30>3.0.co;2-4;
RA Cziepluch C., Kordes E., Pujol A., Jauniaux J.-C.;
RT "Sequencing analysis of a 40.2 kb fragment of yeast chromosome X reveals 19
RT open reading frames including URA2 (5' end), TRK1, PBS2, SPT10, GCD14,
RT RPE1, PHO86, NCA3, ASF1, CCT7, GZF3, two tRNA genes, three remnant delta
RT elements and a Ty4 transposon.";
RL Yeast 12:1471-1474(1996).
RN [3]
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 [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).
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; X85021; CAA59383.1; -; Genomic_DNA.
DR EMBL; Z49386; CAA89406.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08689.1; -; Genomic_DNA.
DR PIR; S53376; S53376.
DR RefSeq; NP_012424.1; NM_001181544.1.
DR PDB; 4V81; X-ray; 3.80 A; G/O/g/o=1-550.
DR PDB; 4V8R; X-ray; 3.80 A; AH/Ah/BH/Bh=1-550.
DR PDB; 4V94; X-ray; 3.80 A; G/O/g/o=1-550.
DR PDB; 5GW4; EM; 4.70 A; H/h=1-550.
DR PDB; 5GW5; EM; 4.60 A; H/h=1-550.
DR PDB; 6KRD; EM; 4.38 A; H/h=1-550.
DR PDB; 6KRE; EM; 4.45 A; H/h=1-550.
DR PDB; 6KS6; EM; 2.99 A; H/h=1-550.
DR PDB; 6KS7; EM; 4.62 A; H/h=1-550.
DR PDB; 6KS8; EM; 4.69 A; H/h=1-550.
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; P42943; -.
DR SMR; P42943; -.
DR BioGRID; 33645; 156.
DR ComplexPortal; CPX-2156; Chaperonin-containing T-complex.
DR DIP; DIP-6758N; -.
DR IntAct; P42943; 44.
DR MINT; P42943; -.
DR STRING; 4932.YJL111W; -.
DR iPTMnet; P42943; -.
DR MaxQB; P42943; -.
DR PaxDb; P42943; -.
DR PRIDE; P42943; -.
DR DNASU; 853333; -.
DR EnsemblFungi; YJL111W_mRNA; YJL111W; YJL111W.
DR GeneID; 853333; -.
DR KEGG; sce:YJL111W; -.
DR SGD; S000003647; CCT7.
DR VEuPathDB; FungiDB:YJL111W; -.
DR eggNOG; KOG0361; Eukaryota.
DR GeneTree; ENSGT00550000074832; -.
DR HOGENOM; CLU_008891_7_1_1; -.
DR InParanoid; P42943; -.
DR OMA; HRKGNTW; -.
DR BioCyc; YEAST:G3O-31565-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:P42943; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P42943; 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; cd03340; TCP1_eta; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR012720; Chap_CCT_eta.
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:SF22; PTHR11353:SF22; 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; TIGR02345; chap_CCT_eta; 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..550
FT /note="T-complex protein 1 subunit eta"
FT /id="PRO_0000128372"
FT REGION 529..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 23..40
FT /evidence="ECO:0007829|PDB:6KS6"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 66..72
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 78..93
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 98..111
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 113..117
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 122..142
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 154..165
FT /evidence="ECO:0007829|PDB:6KS6"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 171..188
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:6KS6"
FT TURN 227..231
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 250..254
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 265..288
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 291..297
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 301..309
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 320..329
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 350..357
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 360..366
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 375..378
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 380..382
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 383..405
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 415..428
FT /evidence="ECO:0007829|PDB:6KS6"
FT TURN 429..431
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 434..445
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 448..457
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 461..471
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 477..480
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 483..487
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 489..491
FT /evidence="ECO:0007829|PDB:6KS6"
FT TURN 492..495
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 500..518
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 520..525
FT /evidence="ECO:0007829|PDB:6KS6"
SQ SEQUENCE 550 AA; 59736 MW; A428FEC2ACD54B4B CRC64;
MNFGSQTPTI VVLKEGTDAS QGKGQIISNI NACVAVQEAL KPTLGPLGSD ILIVTSNQKT
TISNDGATIL KLLDVVHPAA KTLVDISRAQ DAEVGDGTTS VTILAGELMK EAKPFLEEGI
SSHLIMKGYR KAVSLAVEKI NELAVDITSE KSSGRELLER CARTAMSSKL IHNNADFFVK
MCVDAVLSLD RNDLDDKLIG IKKIPGGAME ESLFINGVAF KKTFSYAGFE QQPKKFNNPK
ILSLNVELEL KAEKDNAEVR VEHVEDYQAI VDAEWQLIFE KLRQVEETGA NIVLSKLPIG
DLATQFFADR NIFCAGRVSA DDMNRVIQAV GGSIQSTTSD IKPEHLGTCA LFEEMQIGSE
RYNLFQGCPQ AKTCTLLLRG GAEQVIAEVE RSLHDAIMIV KRALQNKLIV AGGGATEMEV
SKCLRDYSKT IAGKQQMIIN AFAKALEVIP RQLCENAGFD AIEILNKLRL AHSKGEKWYG
VVFETENIGD NFAKFVWEPA LVKINALNSA TEATNLILSV DETITNKGSE SANAGMMPPQ
GAGRGRGMPM
