TCPB_DICDI
ID TCPB_DICDI Reviewed; 532 AA.
AC Q54ES9;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=T-complex protein 1 subunit beta;
DE Short=TCP-1-beta;
DE AltName: Full=CCT-beta;
GN Name=cct2; ORFNames=DDB_G0291358;
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=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).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=AX2;
RX PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA Soldati T.;
RT "Proteomics fingerprinting of phagosome maturation and evidence for the
RT role of a Galpha during uptake.";
RL Mol. Cell. Proteomics 5:2228-2243(2006).
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:0000250}.
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR EMBL; AAFI02000177; EAL61663.1; -; Genomic_DNA.
DR RefSeq; XP_635161.1; XM_630069.1.
DR AlphaFoldDB; Q54ES9; -.
DR SMR; Q54ES9; -.
DR STRING; 44689.DDB0233992; -.
DR PaxDb; Q54ES9; -.
DR EnsemblProtists; EAL61663; EAL61663; DDB_G0291358.
DR GeneID; 8628107; -.
DR KEGG; ddi:DDB_G0291358; -.
DR dictyBase; DDB_G0291358; cct2.
DR eggNOG; KOG0363; Eukaryota.
DR HOGENOM; CLU_008891_6_2_1; -.
DR InParanoid; Q54ES9; -.
DR OMA; YCTGGEI; -.
DR PhylomeDB; Q54ES9; -.
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 Reactome; R-DDI-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-DDI-9013422; RHOBTB1 GTPase cycle.
DR PRO; PR:Q54ES9; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005832; C:chaperonin-containing T-complex; ISS:dictyBase.
DR GO; GO:0045335; C:phagocytic vesicle; HDA: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; 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 ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome.
FT CHAIN 1..532
FT /note="T-complex protein 1 subunit beta"
FT /id="PRO_0000327381"
SQ SEQUENCE 532 AA; 57955 MW; CD579703FFD2F8A1 CRC64;
MSSQLAPIPI LNQNASEERG EIARLSSFVG AIAITDLVKT TLGPKGMDKI LISASNPNEL
IITNDGATIL TKIYIDNPAA KILVDISRTQ DDEVGDGTTS VCVLAGELLR EGERLVQQKV
HPQTIISGWR LALETARAAL QSSTQDHSSD KVKFREDLLN IARTTLSSKI LHTEKDHFAN
MVVDAVLRLN GNTNLDNIHI IKKSGGSLRE SYLDEGFILE KKIGVGCPKR LENPKILIAN
TAMDTDKIKI FGGKVVVDSM TELAKMEDAE KEKMLNKCKK IVDHGINCFV NRQLVYNLPE
QYFAEHGVMS IEHADFDGIE RLALVTGAEI VSTFDHPELV KIGTCKLIEE VMIGEDKVIR
FSGIPSGEAC TIVLRGATSH ILEEAERSIH DALCVLAVTV AETRTVLGAG CSEMIMSKAV
DELAAITPGK KAMAIESFAK ALRQIPTIIA NNAGYDSSEL VSQLKAAHHQ GDKKAGLNMR
DGCIGNAEEL GVIESFKVKQ QVLVSAHEAA EMIMRVDDIL RAAPRQRSNL QH
