ID   TCPQ_CAEEL              Reviewed;         548 AA.
AC   Q9N358;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 3.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=T-complex protein 1 subunit theta;
DE            Short=TCP-1-theta;
DE   AltName: Full=CCT-theta;
GN   Name=cct-8; ORFNames=Y55F3AR.3;
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] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 62-73; 138-148; 255-266; 372-378 AND 508-518, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RA   Bienvenut W.V.;
RL   Submitted (MAR-2006) to UniProtKB.
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19805813; DOI=10.1534/genetics.109.110171;
RA   Updike D.L., Strome S.;
RT   "A genomewide RNAi screen for genes that affect the stability, distribution
RT   and function of P granules in Caenorhabditis elegans.";
RL   Genetics 183:1397-1419(2009).
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). Required for correct subcellular localization
CC       of pgl-1. {ECO:0000250, ECO:0000269|PubMed:19805813}.
CC   -!- SUBUNIT: Heterooligomeric complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P50990}.
CC   -!- DISRUPTION PHENOTYPE: Low and diffuse subcellular localization of pgl-1
CC       in embryos rather than confined to granules in somatic cells.
CC       {ECO:0000269|PubMed:19805813}.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000255}.
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DR   EMBL; FO080854; CCD67240.1; -; Genomic_DNA.
DR   RefSeq; NP_500035.3; NM_067634.4.
DR   AlphaFoldDB; Q9N358; -.
DR   SMR; Q9N358; -.
DR   BioGRID; 42086; 12.
DR   IntAct; Q9N358; 2.
DR   STRING; 6239.Y55F3AR.3a; -.
DR   EPD; Q9N358; -.
DR   PaxDb; Q9N358; -.
DR   PeptideAtlas; Q9N358; -.
DR   PRIDE; Q9N358; -.
DR   EnsemblMetazoa; Y55F3AR.3a.1; Y55F3AR.3a.1; WBGene00021934.
DR   GeneID; 176928; -.
DR   KEGG; cel:CELE_Y55F3AR.3; -.
DR   CTD; 176928; -.
DR   WormBase; Y55F3AR.3a; CE44228; WBGene00021934; cct-8.
DR   eggNOG; KOG0362; Eukaryota.
DR   HOGENOM; CLU_008891_4_2_1; -.
DR   InParanoid; Q9N358; -.
DR   OMA; WGLKYAV; -.
DR   OrthoDB; 617040at2759; -.
DR   PhylomeDB; Q9N358; -.
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-6798695; Neutrophil degranulation.
DR   Reactome; R-CEL-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR   PRO; PR:Q9N358; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00021934; Expressed in adult organism and 4 other tissues.
DR   ExpressionAtlas; Q9N358; 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; 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.
PE   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Cytoplasm; Direct protein sequencing;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..548
FT                   /note="T-complex protein 1 subunit theta"
FT                   /id="PRO_0000239934"
FT   REGION          527..548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   548 AA;  59734 MW;  DB26D85844C0EFDD CRC64;
     MAMKIPKSGY NRFMKEGAQH FKGTDEAVQR NIEACTELAS QIRSAYGPNG MNKMVINHIE
     KLFVTNDAAT ILKELEIQHP AARIIIMATE MQEKQIGDNT NTVVILAAAL LEHAANLIHM
     GMTPQEVAAG YEQAAEKALE ILPTLVVKEA TDMKNIEEVR QYIRSAITSK QYDNEDIIAD
     LVAKACVTTC PANSFNFNVD NIRICKIIGS GVHTSTVMNG MVFKRGAEGE IREARDARIA
     VYTCPFDLTQ TETKGTVLIE NADELRNFSK GEEAEVEEQV KAIADNGVKV VVAAGKFGDM
     YLHFLNKYKI MAVRLTSKFD LRRLCRTVGA QPQARICAPA VNLLGHCDSV AVQEIGDENV
     VVFDKKSETG KVATIIIRGS SQSRIDDVER AVDDAVNTYK ALTKDGKLLA GAGAVEIELA
     KEIESFGAKA PGLEQYAIKK FAHALETLPK AIAENAGMPT TETLTKLYAE HVAGKKNAGI
     DIWKRETMDA VVNNIFDLYA GKRLAIKLAT DAASTILKVD QIIMSKQATG GPKPRGPKAQ
     DEDDDGMA