TCPQ_DICDI
ID TCPQ_DICDI Reviewed; 537 AA.
AC Q552J0; Q75JG7;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=T-complex protein 1 subunit theta;
DE Short=TCP-1-theta;
DE AltName: Full=CCT-theta;
GN Name=cct8; ORFNames=DDB_G0276233;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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. {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; AAFI02000014; EAL69416.1; -; Genomic_DNA.
DR RefSeq; XP_643258.1; XM_638166.1.
DR AlphaFoldDB; Q552J0; -.
DR SMR; Q552J0; -.
DR STRING; 44689.DDB0233996; -.
DR PaxDb; Q552J0; -.
DR PRIDE; Q552J0; -.
DR EnsemblProtists; EAL69416; EAL69416; DDB_G0276233.
DR GeneID; 8620301; -.
DR KEGG; ddi:DDB_G0276233; -.
DR dictyBase; DDB_G0276233; cct8.
DR eggNOG; KOG0362; Eukaryota.
DR HOGENOM; CLU_008891_4_2_1; -.
DR InParanoid; Q552J0; -.
DR OMA; WGLKYAV; -.
DR PhylomeDB; Q552J0; -.
DR BRENDA; 3.6.4.B10; 1939.
DR Reactome; R-DDI-390471; Association of TriC/CCT with target proteins during biosynthesis.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR Reactome; R-DDI-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR PRO; PR:Q552J0; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005832; C:chaperonin-containing T-complex; ISS:dictyBase.
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; ISS:dictyBase.
DR GO; GO:0006457; P:protein folding; ISS:dictyBase.
DR CDD; cd03341; TCP1_theta; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR012721; Chap_CCT_theta.
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; TIGR02346; chap_CCT_theta; 1.
DR PROSITE; PS00750; TCP1_1; 1.
DR PROSITE; PS00751; TCP1_2; 1.
DR PROSITE; PS00995; TCP1_3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome.
FT CHAIN 1..537
FT /note="T-complex protein 1 subunit theta"
FT /id="PRO_0000327900"
SQ SEQUENCE 537 AA; 58540 MW; 681373B401BE596E CRC64;
MLGLTDMLKD GAKHFAGKDE AILRNIDATK QLSEITRTSL GPNGMNKMII NHLEKLFVTN
DAATIIRELD VIHPAAKMLV MAAQMQEQEM GDGTNYVVTL TGEFLQKAAT LLEMGLHPSE
IITGFEKAGA KLQEIIESMI VYNLKDITDK KEVTKCLKSA IASKQYGYEE FLSEIITNAC
LQVLPKKAVN FNIDNVRVTK IPGGGVTDTS VIKGFVIPMD AEGTIKRMEK AKIAVFTMGI
DLGRTETTGK VLITNEDELL QFSKGEEDSI RETITAIANT GVKVIISGST VSELALHYIE
RFKIMLVRIQ SKFQLRRVCK AIGATPLVKL GAPIPEELGY CDEVLVEEIG STKCCIFRQN
KEESEISTIV VRGSTNNILD DIERAIDDGV NVFKGMCKDG RFLAGAGAFE IEASRKLQAF
ADATPGLSQY SIRQYAEAFE IIPRTLAETS GHDSSKAISN IYAAHTKGNT NYGLDIESGQ
PKSVLEMDVL DAFASKLFAI KLATNTANTV LRVDQIIMSK PAGGPKPPKM GPTDADD
