TCPE_PONAB
ID TCPE_PONAB Reviewed; 541 AA.
AC Q5RF02;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=T-complex protein 1 subunit epsilon;
DE Short=TCP-1-epsilon;
DE AltName: Full=CCT-epsilon;
GN Name=CCT5;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CR857360; CAH89655.1; -; mRNA.
DR AlphaFoldDB; Q5RF02; -.
DR SMR; Q5RF02; -.
DR STRING; 9601.ENSPPYP00000017138; -.
DR eggNOG; KOG0357; Eukaryota.
DR InParanoid; Q5RF02; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005832; C:chaperonin-containing T-complex; ISS:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
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:0031681; F:G-protein beta-subunit binding; ISS:CAFA.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
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 Acetylation; ATP-binding; Chaperone; Cytoplasm; Cytoskeleton;
KW Isopeptide bond; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW 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_0000128348"
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; 59687 MW; 62FCD76A45346ED4 CRC64;
MASMGTLAFD EYGRPFLIIK DQDRKSRLMG LEALKSHIMA AKAVANTMRT SLGPNGLDKM
MVDKDGDVTV TNDGATILSM MDVDHQIAKL MVELSKSQDD EIGDGTTGVV VLAGALLEEA
EQLLDRGIHP IRIADGYEQA ARVAIEHLDK ISDSVLVDIK DTEPLIQTAK TTLGSKVVNS
CHRQMAEIAV NAVLTVADME RRDVDFELIK VEGKVGGRLE DTKLIKGVIV DKDFSHPRMP
KKVEDAKIAI LTCPFEPPKP KTKHKLDVTS VEDYKALQKY EKEKFEEMIQ QIKETGANLA
ICQWGFDDEA NHLLLQNNLP AVRWVGGPEI ELIAIATGGR IVPRFSELTA EKLGFAGLVQ
EISFGTTKDK MLVIEQCKNS RAVTIFIRGG NKMIIEEAKR SLHDALCVIR NLIRDNRVVY
GGGAAETSCA LAVSQEADKC PTLEQYAMRA FADALEVIPM ALSENSGMNP IQTMTEVRAR
QVKEMNPALG IDCLHKGTND MKQQHVIETL IGKKQQISLA TQMVRMILKI DDIRKPGESE
E
