ID   TCPH_SCHPO              Reviewed;         558 AA.
AC   P87153;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=Probable T-complex protein 1 subunit eta;
DE            Short=TCP-1-eta;
DE   AltName: Full=CCT-eta;
GN   Name=cct7; ORFNames=SPBC25H2.12c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
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 (By 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:0000305}.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR   EMBL; CU329671; CAB08778.1; -; Genomic_DNA.
DR   PIR; T40007; T40007.
DR   RefSeq; NP_596355.1; NM_001022275.2.
DR   AlphaFoldDB; P87153; -.
DR   SMR; P87153; -.
DR   BioGRID; 277099; 2.
DR   IntAct; P87153; 1.
DR   STRING; 4896.SPBC25H2.12c.1; -.
DR   iPTMnet; P87153; -.
DR   MaxQB; P87153; -.
DR   PaxDb; P87153; -.
DR   PRIDE; P87153; -.
DR   EnsemblFungi; SPBC25H2.12c.1; SPBC25H2.12c.1:pep; SPBC25H2.12c.
DR   GeneID; 2540572; -.
DR   KEGG; spo:SPBC25H2.12c; -.
DR   PomBase; SPBC25H2.12c; cct7.
DR   VEuPathDB; FungiDB:SPBC25H2.12c; -.
DR   eggNOG; KOG0361; Eukaryota.
DR   HOGENOM; CLU_008891_7_3_1; -.
DR   InParanoid; P87153; -.
DR   OMA; HRKGNTW; -.
DR   PhylomeDB; P87153; -.
DR   Reactome; R-SPO-390471; Association of TriC/CCT with target proteins during biosynthesis.
DR   Reactome; R-SPO-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR   PRO; PR:P87153; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005832; C:chaperonin-containing T-complex; IDA:PomBase.
DR   GO; GO:0005856; C:cytoskeleton; ISO:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
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; ISO:PomBase.
DR   GO; GO:0006457; P:protein folding; ISO:PomBase.
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; PS00750; TCP1_1; 1.
DR   PROSITE; PS00751; TCP1_2; 1.
DR   PROSITE; PS00995; TCP1_3; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..558
FT                   /note="Probable T-complex protein 1 subunit eta"
FT                   /id="PRO_0000128371"
FT   REGION          527..558
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         176
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   558 AA;  60687 MW;  C4C1F843F44C5253 CRC64;
     MSLGGPQIPV IVLKEGTDDS QGRGQLLSNI NACVAVQDTI RTTLGPLGAD KLMVDDRGEV
     VISNDGATIM KLLDIVHPAA KTLVDIARAQ DAEVGDGTTS VVVFAGELLR EARTFVEDGV
     SSHLIIRGYR KAAQLAVNKI KEIAIHLDLS DEGKLRDLLT KCASTAMNSK LIRSNSTFFT
     KMVVDAVLTL DQEDLNENMI GIKKVPGGAM EDSLLVKGVA FKKTFSYAGF EQQPKFFKNP
     KILCLDVELE LKAEKDNAEV RVDKVQEYQN IVDAEWRIIF SKLEAIVATG AKVVLSKLPI
     GDLATQYFAD RDIFCAGRVA ADDLNRVVQA VGGSIQSTCS NIEEKHLGTC DTFEERQIGG
     DRFNLFEGCP KAKTCTLILR GGADQFIAEV ERSLHDAIMI VKHALKNNLV VAGGGACEME
     LSKYLRDYSL TISGKQQNFI AAFARSLEVI PRQLCDNAGF DSTNILNKLR MQHAKGEMWA
     GVDMDSEGVA NNFEKFVWEP STVKSNAILS ATEAATLILS VDETIKNEPS QQPQAPQGAL
     PPGAANRIMR GRGRGMPR