ID   TCPE_RAT                Reviewed;         541 AA.
AC   Q68FQ0; Q6PCT4;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=T-complex protein 1 subunit epsilon;
DE            Short=TCP-1-epsilon;
DE   AltName: Full=CCT-epsilon;
GN   Name=Cct5;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pituitary, and Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 248-261 AND 324-340, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA   Lubec G., Afjehi-Sadat L., Diao W.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Component of the chaperonin-containing T-complex (TRiC), a
CC       molecular chaperone complex that assists the folding of proteins upon
CC       ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1,
CC       thereby regulating telomere maintenance. As part of the TRiC complex
CC       may play a role in the assembly of BBSome, a complex involved in
CC       ciliogenesis regulating transports vesicles to the cilia. The TRiC
CC       complex plays a role in the folding of actin and tubulin.
CC       {ECO:0000250|UniProtKB:P48643}.
CC   -!- SUBUNIT: Component of the chaperonin-containing T-complex (TRiC), a
CC       heterooligomeric complex of about 850 to 900 kDa that forms two stacked
CC       rings, 12 to 16 nm in diameter. Interacts with PACRG (By similarity).
CC       Interacts with DNAAF4 (By similarity). Interacts with DLEC1 (By
CC       similarity). {ECO:0000250|UniProtKB:P48643,
CC       ECO:0000250|UniProtKB:P80316}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P48643}.
CC       Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC       {ECO:0000250|UniProtKB:P48643}.
CC   -!- PTM: Ubiquitinated by the DCX(DCAF12) complex specifically recognizes
CC       the diglutamate (Glu-Glu) at the C-terminus, leading to its
CC       degradation. {ECO:0000250|UniProtKB:P48643}.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH59165.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR   EMBL; BC059165; AAH59165.1; ALT_SEQ; mRNA.
DR   EMBL; BC079441; AAH79441.1; -; mRNA.
DR   RefSeq; NP_001004078.1; NM_001004078.1.
DR   AlphaFoldDB; Q68FQ0; -.
DR   SMR; Q68FQ0; -.
DR   BioGRID; 254817; 5.
DR   IntAct; Q68FQ0; 7.
DR   MINT; Q68FQ0; -.
DR   STRING; 10116.ENSRNOP00000015886; -.
DR   iPTMnet; Q68FQ0; -.
DR   PhosphoSitePlus; Q68FQ0; -.
DR   World-2DPAGE; 0004:Q68FQ0; -.
DR   jPOST; Q68FQ0; -.
DR   PaxDb; Q68FQ0; -.
DR   PRIDE; Q68FQ0; -.
DR   Ensembl; ENSRNOT00000015886; ENSRNOP00000015886; ENSRNOG00000011632.
DR   GeneID; 294864; -.
DR   KEGG; rno:294864; -.
DR   UCSC; RGD:735161; rat.
DR   CTD; 22948; -.
DR   RGD; 735161; Cct5.
DR   eggNOG; KOG0357; Eukaryota.
DR   GeneTree; ENSGT00550000074988; -.
DR   HOGENOM; CLU_008891_7_2_1; -.
DR   InParanoid; Q68FQ0; -.
DR   OMA; QTGSNDM; -.
DR   OrthoDB; 511484at2759; -.
DR   PhylomeDB; Q68FQ0; -.
DR   TreeFam; TF105638; -.
DR   BRENDA; 3.6.4.B10; 5301.
DR   Reactome; R-RNO-390471; Association of TriC/CCT with target proteins during biosynthesis.
DR   Reactome; R-RNO-5620922; BBSome-mediated cargo-targeting to cilium.
DR   Reactome; R-RNO-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR   PRO; PR:Q68FQ0; -.
DR   Proteomes; UP000002494; Chromosome 2.
DR   Bgee; ENSRNOG00000011632; Expressed in thymus and 19 other tissues.
DR   Genevisible; Q68FQ0; RN.
DR   GO; GO:0044297; C:cell body; ISO:RGD.
DR   GO; GO:0005813; C:centrosome; ISO:RGD.
DR   GO; GO:0005832; C:chaperonin-containing T-complex; ISS:UniProtKB.
DR   GO; GO:0005874; C:microtubule; ISO:RGD.
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:0048487; F:beta-tubulin binding; ISO:RGD.
DR   GO; GO:0031681; F:G-protein beta-subunit binding; ISS:CAFA.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; ISO:RGD.
DR   GO; GO:0048027; F:mRNA 5'-UTR binding; ISO:RGD.
DR   GO; GO:0044183; F:protein folding chaperone; ISO:RGD.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0007339; P:binding of sperm to zona pellucida; ISO:RGD.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; ISO:RGD.
DR   GO; GO:1904851; P:positive regulation of establishment of protein localization to telomere; ISO:RGD.
DR   GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; ISO:RGD.
DR   GO; GO:0006457; P:protein folding; ISO:RGD.
DR   GO; GO:0050821; P:protein stabilization; ISO:RGD.
DR   GO; GO:0009615; P:response to virus; ISO:RGD.
DR   GO; GO:1901998; P:toxin transport; ISO:RGD.
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   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Chaperone; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Isopeptide bond; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P48643"
FT   CHAIN           2..541
FT                   /note="T-complex protein 1 subunit epsilon"
FT                   /id="PRO_0000271396"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P48643"
FT   MOD_RES         26
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P48643"
FT   MOD_RES         346
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P48643"
FT   MOD_RES         539
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P48643"
FT   CROSSLNK        20
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P48643"
FT   CROSSLNK        210
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P48643"
FT   CROSSLNK        214
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P48643"
FT   CROSSLNK        265
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P48643"
FT   CROSSLNK        275
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P48643"
FT   CROSSLNK        279
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P48643"
FT   CROSSLNK        392
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P48643"
SQ   SEQUENCE   541 AA;  59537 MW;  B19EFC616DB63C7E CRC64;
     MASVGTLAFD EYGRPFLIIK DQDRKSRLMG LEALKSHIMA AKAVANTMRT SLGPNGLDKM
     MVDKDGDVTV TNDGATILSM MDVDHQIAKL MVELSKSQDD EIGDGTTGVV VLAGALLEEA
     EQLLDRGIHP IRIADGYEQA ARIAIQHLDK ISDNVLVDIN NPEPLIQTAK TTLGSKVVNS
     CHRQMAEIAV NAVLTVADME RRDVDFELIK VEGKVGGRLE DTKLIKGVIV DKDFSHPQMP
     KEVLNAKIAI LTCPFEPPKP KTKHKLDVTS VEDYKALQKY EKEKFEEMIA QIKETGANLA
     ICQWGFDDEA NHLLLQNGLP AVRWVGGPEI ELIAIATGGR IVPRFSELTS EKLGFAGVVR
     EISFGTTKDK MLVIEQCKNS RAVTIFIRGG NKMIIEEAKR SLHDALCVIR NLIRDNRVVY
     GGGAAEISCA LAVSQEADKC PTLEQYAMRA FADALEVIPM ALSENSGMNP IQTMTEVRAR
     QVKESNPALG IDCLHKGSND MQYQHVIETL IGKKQQISLA TQMVRMILKI DDIRKPGESE
     E