UniProtKB - Q68FQ0 (TCPE_RAT)
Protein
T-complex protein 1 subunit epsilon
Gene
Cct5
Organism
Rattus norvegicus (Rat)
Status
Functioni
Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin.By similarity
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- beta-tubulin binding Source: RGD
- G-protein beta-subunit binding Source: UniProtKB
- mRNA 3'-UTR binding Source: RGD
- mRNA 5'-UTR binding Source: RGD
- unfolded protein binding Source: GO_Central
GO - Biological processi
- binding of sperm to zona pellucida Source: RGD
- positive regulation of establishment of protein localization to telomere Source: RGD
- positive regulation of telomere maintenance via telomerase Source: RGD
- protein folding Source: GO_Central
- protein stabilization Source: RGD
- response to virus Source: RGD
- toxin transport Source: RGD
Keywordsi
Molecular function | Chaperone |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
Reactomei | R-RNO-390471, Association of TriC/CCT with target proteins during biosynthesis R-RNO-5620922, BBSome-mediated cargo-targeting to cilium R-RNO-6814122, Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding |
Names & Taxonomyi
Protein namesi | Recommended name: T-complex protein 1 subunit epsilonShort name: TCP-1-epsilon Alternative name(s): CCT-epsilon |
Gene namesi | Name:Cct5 |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 735161, Cct5 |
Subcellular locationi
Cytoskeleton
- centrosome By similarity
Other locations
- Cytoplasm By similarity
Cytoskeleton
- centrosome Source: RGD
- microtubule Source: RGD
Cytosol
- chaperonin-containing T-complex Source: UniProtKB
Other locations
- cell body Source: RGD
- zona pellucida receptor complex Source: RGD
Keywords - Cellular componenti
Cytoplasm, CytoskeletonPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedBy similarity | |||
ChainiPRO_0000271396 | 2 – 541 | T-complex protein 1 subunit epsilonAdd BLAST | 540 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylalanineBy similarity | 1 | |
Cross-linki | 20 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Modified residuei | 26 | PhosphoserineBy similarity | 1 | |
Cross-linki | 210 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Cross-linki | 214 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Cross-linki | 265 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Cross-linki | 275 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Cross-linki | 279 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Modified residuei | 346 | PhosphoserineBy similarity | 1 | |
Cross-linki | 392 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Modified residuei | 539 | PhosphoserineBy similarity | 1 |
Keywords - PTMi
Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
jPOSTi | Q68FQ0 |
PaxDbi | Q68FQ0 |
PRIDEi | Q68FQ0 |
2D gel databases
World-2DPAGEi | 0004:Q68FQ0 |
PTM databases
iPTMneti | Q68FQ0 |
PhosphoSitePlusi | Q68FQ0 |
Expressioni
Gene expression databases
Bgeei | ENSRNOG00000011632, Expressed in testis and 20 other tissues |
Genevisiblei | Q68FQ0, RN |
Interactioni
Subunit structurei
Component of the chaperonin-containing T-complex (TRiC), a heterooligomeric complex of about 850 to 900 kDa that forms two stacked rings, 12 to 16 nm in diameter.
Interacts with PACRG (By similarity).
Interacts with DNAAF4 (By similarity).
By similarityGO - Molecular functioni
- beta-tubulin binding Source: RGD
- G-protein beta-subunit binding Source: UniProtKB
- unfolded protein binding Source: GO_Central
Protein-protein interaction databases
BioGRIDi | 254817, 4 interactors |
IntActi | Q68FQ0, 6 interactors |
MINTi | Q68FQ0 |
STRINGi | 10116.ENSRNOP00000015886 |
Family & Domainsi
Sequence similaritiesi
Belongs to the TCP-1 chaperonin family.Curated
Phylogenomic databases
eggNOGi | KOG0357, Eukaryota |
GeneTreei | ENSGT00550000074988 |
HOGENOMi | CLU_008891_7_2_1 |
InParanoidi | Q68FQ0 |
OMAi | AHDQFAN |
OrthoDBi | 511484at2759 |
PhylomeDBi | Q68FQ0 |
TreeFami | TF105638 |
Family and domain databases
Gene3Di | 1.10.560.10, 1 hit 3.30.260.10, 1 hit 3.50.7.10, 1 hit |
InterProi | View protein in InterPro IPR017998, Chaperone_TCP-1 IPR002194, Chaperonin_TCP-1_CS IPR002423, Cpn60/TCP-1 IPR027409, GroEL-like_apical_dom_sf IPR027413, GROEL-like_equatorial_sf IPR027410, TCP-1-like_intermed_sf |
Pfami | View protein in Pfam PF00118, Cpn60_TCP1, 1 hit |
PRINTSi | PR00304, TCOMPLEXTCP1 |
SUPFAMi | SSF48592, SSF48592, 1 hit SSF52029, SSF52029, 1 hit SSF54849, SSF54849, 1 hit |
PROSITEi | View protein in PROSITE PS00750, TCP1_1, 1 hit PS00751, TCP1_2, 1 hit PS00995, TCP1_3, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
Q68FQ0-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MASVGTLAFD EYGRPFLIIK DQDRKSRLMG LEALKSHIMA AKAVANTMRT
60 70 80 90 100
SLGPNGLDKM MVDKDGDVTV TNDGATILSM MDVDHQIAKL MVELSKSQDD
110 120 130 140 150
EIGDGTTGVV VLAGALLEEA EQLLDRGIHP IRIADGYEQA ARIAIQHLDK
160 170 180 190 200
ISDNVLVDIN NPEPLIQTAK TTLGSKVVNS CHRQMAEIAV NAVLTVADME
210 220 230 240 250
RRDVDFELIK VEGKVGGRLE DTKLIKGVIV DKDFSHPQMP KEVLNAKIAI
260 270 280 290 300
LTCPFEPPKP KTKHKLDVTS VEDYKALQKY EKEKFEEMIA QIKETGANLA
310 320 330 340 350
ICQWGFDDEA NHLLLQNGLP AVRWVGGPEI ELIAIATGGR IVPRFSELTS
360 370 380 390 400
EKLGFAGVVR EISFGTTKDK MLVIEQCKNS RAVTIFIRGG NKMIIEEAKR
410 420 430 440 450
SLHDALCVIR NLIRDNRVVY GGGAAEISCA LAVSQEADKC PTLEQYAMRA
460 470 480 490 500
FADALEVIPM ALSENSGMNP IQTMTEVRAR QVKESNPALG IDCLHKGSND
510 520 530 540
MQYQHVIETL IGKKQQISLA TQMVRMILKI DDIRKPGESE E
Sequence cautioni
The sequence AAH59165 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BC059165 mRNA Translation: AAH59165.1 Sequence problems. BC079441 mRNA Translation: AAH79441.1 |
RefSeqi | NP_001004078.1, NM_001004078.1 |
Genome annotation databases
Ensembli | ENSRNOT00000015886; ENSRNOP00000015886; ENSRNOG00000011632 |
GeneIDi | 294864 |
KEGGi | rno:294864 |
UCSCi | RGD:735161, rat |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BC059165 mRNA Translation: AAH59165.1 Sequence problems. BC079441 mRNA Translation: AAH79441.1 |
RefSeqi | NP_001004078.1, NM_001004078.1 |
3D structure databases
SMRi | Q68FQ0 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 254817, 4 interactors |
IntActi | Q68FQ0, 6 interactors |
MINTi | Q68FQ0 |
STRINGi | 10116.ENSRNOP00000015886 |
PTM databases
iPTMneti | Q68FQ0 |
PhosphoSitePlusi | Q68FQ0 |
2D gel databases
World-2DPAGEi | 0004:Q68FQ0 |
Proteomic databases
jPOSTi | Q68FQ0 |
PaxDbi | Q68FQ0 |
PRIDEi | Q68FQ0 |
Genome annotation databases
Ensembli | ENSRNOT00000015886; ENSRNOP00000015886; ENSRNOG00000011632 |
GeneIDi | 294864 |
KEGGi | rno:294864 |
UCSCi | RGD:735161, rat |
Organism-specific databases
CTDi | 22948 |
RGDi | 735161, Cct5 |
Phylogenomic databases
eggNOGi | KOG0357, Eukaryota |
GeneTreei | ENSGT00550000074988 |
HOGENOMi | CLU_008891_7_2_1 |
InParanoidi | Q68FQ0 |
OMAi | AHDQFAN |
OrthoDBi | 511484at2759 |
PhylomeDBi | Q68FQ0 |
TreeFami | TF105638 |
Enzyme and pathway databases
Reactomei | R-RNO-390471, Association of TriC/CCT with target proteins during biosynthesis R-RNO-5620922, BBSome-mediated cargo-targeting to cilium R-RNO-6814122, Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding |
Miscellaneous databases
PROi | PR:Q68FQ0 |
Gene expression databases
Bgeei | ENSRNOG00000011632, Expressed in testis and 20 other tissues |
Genevisiblei | Q68FQ0, RN |
Family and domain databases
Gene3Di | 1.10.560.10, 1 hit 3.30.260.10, 1 hit 3.50.7.10, 1 hit |
InterProi | View protein in InterPro IPR017998, Chaperone_TCP-1 IPR002194, Chaperonin_TCP-1_CS IPR002423, Cpn60/TCP-1 IPR027409, GroEL-like_apical_dom_sf IPR027413, GROEL-like_equatorial_sf IPR027410, TCP-1-like_intermed_sf |
Pfami | View protein in Pfam PF00118, Cpn60_TCP1, 1 hit |
PRINTSi | PR00304, TCOMPLEXTCP1 |
SUPFAMi | SSF48592, SSF48592, 1 hit SSF52029, SSF52029, 1 hit SSF54849, SSF54849, 1 hit |
PROSITEi | View protein in PROSITE PS00750, TCP1_1, 1 hit PS00751, TCP1_2, 1 hit PS00995, TCP1_3, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | TCPE_RAT | |
Accessioni | Q68FQ0Primary (citable) accession number: Q68FQ0 Secondary accession number(s): Q6PCT4 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | January 9, 2007 |
Last sequence update: | October 11, 2004 | |
Last modified: | February 10, 2021 | |
This is version 127 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencing, Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families