TCPG_SCHPO
ID TCPG_SCHPO Reviewed; 528 AA.
AC O74341;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=T-complex protein 1 subunit gamma;
DE Short=TCP-1-gamma;
DE AltName: Full=CCT-gamma;
GN Name=cct3; ORFNames=SPBC1A4.08c;
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-250, 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:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329671; CAA20112.1; -; Genomic_DNA.
DR PIR; T39856; T39856.
DR RefSeq; NP_595810.1; NM_001021713.2.
DR AlphaFoldDB; O74341; -.
DR SMR; O74341; -.
DR BioGRID; 277094; 7.
DR IntAct; O74341; 1.
DR STRING; 4896.SPBC1A4.08c.1; -.
DR iPTMnet; O74341; -.
DR MaxQB; O74341; -.
DR PaxDb; O74341; -.
DR PRIDE; O74341; -.
DR EnsemblFungi; SPBC1A4.08c.1; SPBC1A4.08c.1:pep; SPBC1A4.08c.
DR GeneID; 2540567; -.
DR KEGG; spo:SPBC1A4.08c; -.
DR PomBase; SPBC1A4.08c; cct3.
DR VEuPathDB; FungiDB:SPBC1A4.08c; -.
DR eggNOG; KOG0364; Eukaryota.
DR HOGENOM; CLU_008891_7_3_1; -.
DR InParanoid; O74341; -.
DR OMA; RYCRIEK; -.
DR PhylomeDB; O74341; -.
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:O74341; -.
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; cd03337; TCP1_gamma; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR012719; Chap_CCT_gamma.
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; TIGR02344; chap_CCT_gamma; 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; Disulfide bond; Nucleotide-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..528
FT /note="T-complex protein 1 subunit gamma"
FT /id="PRO_0000128330"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT DISULFID 364..370
FT /evidence="ECO:0000250"
SQ SEQUENCE 528 AA; 58481 MW; 260BC1A6DA295E8E CRC64;
MQSPVFVMNT NGNRQVGHKA QMSNIQAAKA VADVIRTCLG PRAMLKMLLD PVGSVLLTND
GHAILREIEV AHPAAKSMIE LARTQDEEVG DGTTSVIILA GEILAAASPL LDRKIHPVVM
IRSFKQALED ALSIIDEITL PVNVDDNAEM FRLIRTCIGT KLVARWSDLM CHLALRAVRT
VASTSNGRME IDIKRYARVE KVPGGEIESS CVLDGVMLNK DVTHPKMRRR IENPRIVLLD
CPLEYRKGES QTNIEISKDT DWNRILEIEE EQVKRMCDYI IAVKPDLVIT EKGVSDLAQH
YLLKANITAL RRTRKSDNNR IARACGANIV NRLEDLREKD VGTGCGLFYI DKLGDEYYTF
LTGCKNPKAC TILLRGPSKD IINEVERNLQ DAMAVARNVF FHPKLSPGGG ATEMAVSVRL
AEKARSIEGV AQWPYRAVAD AIEIIPRTLV QNCGANPIKA LTELRAKHAE GQHSFGIDGE
TGRVVDMHEY GVWEPEAVKL QSIKTAIESA CLLLRVDDIV SGVRKHSE