ID   TCPZ_CAEEL              Reviewed;         539 AA.
AC   P46550;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=T-complex protein 1 subunit zeta;
DE            Short=TCP-1-zeta;
DE   AltName: Full=CCT-zeta;
GN   Name=cct-6; ORFNames=F01F1.8;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   CHARACTERIZATION.
RX   PubMed=7576182; DOI=10.1089/dna.1995.14.951;
RA   Leroux M.R., Candido E.P.M.;
RT   "Characterization of four new tcp-1-related cct genes from the nematode
RT   Caenorhabditis elegans.";
RL   DNA Cell Biol. 14:951-960(1995).
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; FO080705; CCD65990.1; -; Genomic_DNA.
DR   PIR; T15943; T15943.
DR   RefSeq; NP_741153.1; NM_171135.6.
DR   AlphaFoldDB; P46550; -.
DR   SMR; P46550; -.
DR   BioGRID; 41041; 14.
DR   IntAct; P46550; 1.
DR   STRING; 6239.F01F1.8a.1; -.
DR   EPD; P46550; -.
DR   PaxDb; P46550; -.
DR   PeptideAtlas; P46550; -.
DR   EnsemblMetazoa; F01F1.8a.1; F01F1.8a.1; WBGene00000381.
DR   EnsemblMetazoa; F01F1.8a.2; F01F1.8a.2; WBGene00000381.
DR   GeneID; 175819; -.
DR   KEGG; cel:CELE_F01F1.8; -.
DR   UCSC; F01F1.8a.1; c. elegans.
DR   CTD; 175819; -.
DR   WormBase; F01F1.8a; CE01234; WBGene00000381; cct-6.
DR   eggNOG; KOG0359; Eukaryota.
DR   GeneTree; ENSGT00940000156339; -.
DR   InParanoid; P46550; -.
DR   OMA; LHPRIMT; -.
DR   OrthoDB; 482152at2759; -.
DR   PhylomeDB; P46550; -.
DR   BRENDA; 3.6.4.B10; 1045.
DR   Reactome; R-CEL-390471; Association of TriC/CCT with target proteins during biosynthesis.
DR   Reactome; R-CEL-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR   PRO; PR:P46550; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00000381; Expressed in germ line (C elegans) and 4 other tissues.
DR   ExpressionAtlas; P46550; baseline and differential.
DR   GO; GO:0005832; C:chaperonin-containing T-complex; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   CDD; cd03342; TCP1_zeta; 1.
DR   Gene3D; 1.10.560.10; -; 1.
DR   Gene3D; 3.30.260.10; -; 1.
DR   Gene3D; 3.50.7.10; -; 1.
DR   InterPro; IPR012722; Chap_CCT_zeta.
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; TIGR02347; chap_CCT_zeta; 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..539
FT                   /note="T-complex protein 1 subunit zeta"
FT                   /id="PRO_0000128360"
SQ   SEQUENCE   539 AA;  58905 MW;  84DE24110A03CDE4 CRC64;
     MSSIQCLNPK AELARHAAAL ELNISGARGL QDVMRSNLGP KGTLKMLVSG AGDIKLTKDG
     NVLLHEMAIQ HPTASMIAKA STAQDDVTGD GTTSTVLLIG ELLKQAESLV LEGLHPRIVT
     EGFEWANTKT LELLEKFKKE APVERDLLVE VCRTALRTKL HQKLADHITE CVVDAVLAIR
     RDGEEPDLHM VEKMEMHHDS DMDTTLVRGL VLDHGARHPD MPRHVKDAYI LTCNVSLEYE
     KTEVNSGLFY KTAKEREALL AAEREFITRR VHKIIELKKK VIDNSPDGKN KGFVVINQKG
     IDPPSLDLLA SEGILALRRA KRRNMERLQL AVGGEAVNSV DDLTPEDLGW AGLVYEHSLG
     EEKYTFIEEC RAPKSVTLLI KGPNKHTITQ IKDAIHDGLR AVFNTIVDKA VLPGAAAFEI
     AAYVMLKKDV ENLKGRAKLG AEAFAQALLV IPKTLAVNGG YDAQETLVKL IEEKTAAGPD
     IAVGLDLETG GAVEPQGIWD NVTVKKNSIS SATVLACNLL LVDEVMRAGM TNLKQPQPE