ID   TCPE_CAEEL              Reviewed;         542 AA.
AC   P47209;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 161.
DE   RecName: Full=T-complex protein 1 subunit epsilon;
DE            Short=TCP-1-epsilon;
DE   AltName: Full=CCT-epsilon;
GN   Name=cct-5; ORFNames=C07G2.3;
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 [MRNA].
RC   STRAIN=Bristol N2;
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).
RN   [2]
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).
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.
CC   -!- SUBUNIT: Heterooligomeric complex of about 850 to 900 kDa that forms
CC       two stacked rings, 12 to 16 nm in diameter.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR   EMBL; U25698; AAA92843.1; -; mRNA.
DR   EMBL; Z32840; CAA83681.1; -; Genomic_DNA.
DR   EMBL; Z35599; CAA83681.1; JOINED; Genomic_DNA.
DR   PIR; T19063; T19063.
DR   RefSeq; NP_741117.1; NM_171104.3.
DR   AlphaFoldDB; P47209; -.
DR   SMR; P47209; -.
DR   BioGRID; 40824; 19.
DR   DIP; DIP-25588N; -.
DR   IntAct; P47209; 4.
DR   STRING; 6239.C07G2.3a.1; -.
DR   iPTMnet; P47209; -.
DR   World-2DPAGE; 0011:P47209; -.
DR   World-2DPAGE; 0020:P47209; -.
DR   EPD; P47209; -.
DR   PaxDb; P47209; -.
DR   PeptideAtlas; P47209; -.
DR   EnsemblMetazoa; C07G2.3.1; C07G2.3.1; WBGene00000380.
DR   GeneID; 175588; -.
DR   KEGG; cel:CELE_C07G2.3; -.
DR   UCSC; C07G2.3b.3; c. elegans.
DR   CTD; 175588; -.
DR   WormBase; C07G2.3; CE02985; WBGene00000380; cct-5.
DR   eggNOG; KOG0357; Eukaryota.
DR   GeneTree; ENSGT00550000074988; -.
DR   HOGENOM; CLU_008891_7_2_1; -.
DR   InParanoid; P47209; -.
DR   OMA; QTGSNDM; -.
DR   OrthoDB; 511484at2759; -.
DR   PhylomeDB; P47209; -.
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:P47209; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00000380; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0005832; C:chaperonin-containing T-complex; IDA:WormBase.
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:WormBase.
DR   GO; GO:0006457; P:protein folding; ISS:WormBase.
DR   CDD; cd03339; TCP1_epsilon; 1.
DR   Gene3D; 1.10.560.10; -; 1.
DR   Gene3D; 3.30.260.10; -; 1.
DR   Gene3D; 3.50.7.10; -; 1.
DR   InterPro; IPR012718; Chap_CCT_epsi.
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; TIGR02343; chap_CCT_epsi; 1.
DR   PROSITE; PS00750; TCP1_1; 1.
DR   PROSITE; PS00751; TCP1_2; 1.
DR   PROSITE; PS00995; TCP1_3; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..542
FT                   /note="T-complex protein 1 subunit epsilon"
FT                   /id="PRO_0000128349"
SQ   SEQUENCE   542 AA;  59406 MW;  A87D3B3FD256D1E5 CRC64;
     MAQSSAQLLF DESGQPFIVM REQENQKRIT GVEAVKSHIL AARAVANTLR TSLGPRGLDK
     MLVSPDGDVT ITNDGATIME KMDVQHHVAK LMVELSKSQD HEIGDGTTGV VVLAGALLEE
     AEKLIDRGIH PIKIADGFDL ACKKALETLD SISDKFPVEN RERLVETAQT SLGSKIVNRS
     LRQFAEIAVD AVLSVADIES KDVNFEMIKM EGKVGGRLED TILVKGIVID KTMSHPQMPK
     ELKNAKVAIL TCPFEPPKPK TKHKLDITST EDFKALRDYE RETFETMIRQ VKESGATLAI
     CQWGFDDEAN HLLQANDLPA VRWVGGPEIE LLAIATNARI VPRFSELSKE KLGTAGLVRE
     ITFGAAKDRM LSIEQCPNNK AVTIFVRGGN KMIIDEAKRA LHDALCVIRN LVRDSRIVYG
     GGSAELAAAI QVAKEADRID GIEQYAFRAF ADALESIPMA LAENSGLAPI DALSDLKAKQ
     IETGKSSLGI DAVFAGTNDM KEQKVIETLL SKREQISLAT QVVRMILKID DVRVPDDERM
     GY