Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

T-complex protein 1 subunit epsilon

Gene

cct-5

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • unfolded protein binding Source: WormBase

GO - Biological processi

  • protein folding Source: WormBase
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-CEL-390471. Association of TriC/CCT with target proteins during biosynthesis.
R-CEL-6814122. Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.

Names & Taxonomyi

Protein namesi
Recommended name:
T-complex protein 1 subunit epsilon
Short name:
TCP-1-epsilon
Alternative name(s):
CCT-epsilon
Gene namesi
Name:cct-5
ORF Names:C07G2.3
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome III

Organism-specific databases

WormBaseiC07G2.3a; CE02985; WBGene00000380; cct-5.

Subcellular locationi

GO - Cellular componenti

  • chaperonin-containing T-complex Source: WormBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 542542T-complex protein 1 subunit epsilonPRO_0000128349Add
BLAST

Proteomic databases

EPDiP47209.
PaxDbiP47209.
PRIDEiP47209.

2D gel databases

World-2DPAGE0011:P47209.
0020:P47209.

PTM databases

iPTMnetiP47209.

Expressioni

Gene expression databases

ExpressionAtlasiP47209. baseline.

Interactioni

Subunit structurei

Heterooligomeric complex of about 850 to 900 kDa that forms two stacked rings, 12 to 16 nm in diameter.

GO - Molecular functioni

  • unfolded protein binding Source: WormBase

Protein-protein interaction databases

BioGridi40824. 6 interactions.
DIPiDIP-25588N.
IntActiP47209. 4 interactions.
MINTiMINT-1078976.
STRINGi6239.C07G2.3a.1.

Structurei

3D structure databases

ProteinModelPortaliP47209.
SMRiP47209. Positions 19-535.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TCP-1 chaperonin family.Curated

Phylogenomic databases

eggNOGiKOG0357. Eukaryota.
COG0459. LUCA.
GeneTreeiENSGT00550000074988.
HOGENOMiHOG000226735.
InParanoidiP47209.
KOiK09497.
OMAiVDHEIAK.
PhylomeDBiP47209.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012718. Chap_CCT_epsi.
IPR017998. Chaperone_TCP-1.
IPR002194. Chaperonin_TCP-1_CS.
IPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027413. GROEL-like_equatorial.
[Graphical view]
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00304. TCOMPLEXTCP1.
SUPFAMiSSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02343. chap_CCT_epsi. 1 hit.
PROSITEiPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P47209-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQSSAQLLF DESGQPFIVM REQENQKRIT GVEAVKSHIL AARAVANTLR
60 70 80 90 100
TSLGPRGLDK MLVSPDGDVT ITNDGATIME KMDVQHHVAK LMVELSKSQD
110 120 130 140 150
HEIGDGTTGV VVLAGALLEE AEKLIDRGIH PIKIADGFDL ACKKALETLD
160 170 180 190 200
SISDKFPVEN RERLVETAQT SLGSKIVNRS LRQFAEIAVD AVLSVADIES
210 220 230 240 250
KDVNFEMIKM EGKVGGRLED TILVKGIVID KTMSHPQMPK ELKNAKVAIL
260 270 280 290 300
TCPFEPPKPK TKHKLDITST EDFKALRDYE RETFETMIRQ VKESGATLAI
310 320 330 340 350
CQWGFDDEAN HLLQANDLPA VRWVGGPEIE LLAIATNARI VPRFSELSKE
360 370 380 390 400
KLGTAGLVRE ITFGAAKDRM LSIEQCPNNK AVTIFVRGGN KMIIDEAKRA
410 420 430 440 450
LHDALCVIRN LVRDSRIVYG GGSAELAAAI QVAKEADRID GIEQYAFRAF
460 470 480 490 500
ADALESIPMA LAENSGLAPI DALSDLKAKQ IETGKSSLGI DAVFAGTNDM
510 520 530 540
KEQKVIETLL SKREQISLAT QVVRMILKID DVRVPDDERM GY
Length:542
Mass (Da):59,406
Last modified:February 1, 1996 - v1
Checksum:iA87D3B3FD256D1E5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U25698 mRNA. Translation: AAA92843.1.
Z32840, Z35599 Genomic DNA. Translation: CAA83681.1.
PIRiT19063.
RefSeqiNP_741117.1. NM_171104.3.
UniGeneiCel.18128.

Genome annotation databases

EnsemblMetazoaiC07G2.3a.1; C07G2.3a.1; WBGene00000380.
C07G2.3a.2; C07G2.3a.2; WBGene00000380.
GeneIDi175588.
KEGGicel:CELE_C07G2.3.
UCSCiC07G2.3b.3. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U25698 mRNA. Translation: AAA92843.1.
Z32840, Z35599 Genomic DNA. Translation: CAA83681.1.
PIRiT19063.
RefSeqiNP_741117.1. NM_171104.3.
UniGeneiCel.18128.

3D structure databases

ProteinModelPortaliP47209.
SMRiP47209. Positions 19-535.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi40824. 6 interactions.
DIPiDIP-25588N.
IntActiP47209. 4 interactions.
MINTiMINT-1078976.
STRINGi6239.C07G2.3a.1.

PTM databases

iPTMnetiP47209.

2D gel databases

World-2DPAGE0011:P47209.
0020:P47209.

Proteomic databases

EPDiP47209.
PaxDbiP47209.
PRIDEiP47209.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiC07G2.3a.1; C07G2.3a.1; WBGene00000380.
C07G2.3a.2; C07G2.3a.2; WBGene00000380.
GeneIDi175588.
KEGGicel:CELE_C07G2.3.
UCSCiC07G2.3b.3. c. elegans.

Organism-specific databases

CTDi175588.
WormBaseiC07G2.3a; CE02985; WBGene00000380; cct-5.

Phylogenomic databases

eggNOGiKOG0357. Eukaryota.
COG0459. LUCA.
GeneTreeiENSGT00550000074988.
HOGENOMiHOG000226735.
InParanoidiP47209.
KOiK09497.
OMAiVDHEIAK.
PhylomeDBiP47209.

Enzyme and pathway databases

ReactomeiR-CEL-390471. Association of TriC/CCT with target proteins during biosynthesis.
R-CEL-6814122. Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.

Miscellaneous databases

PROiP47209.

Gene expression databases

ExpressionAtlasiP47209. baseline.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012718. Chap_CCT_epsi.
IPR017998. Chaperone_TCP-1.
IPR002194. Chaperonin_TCP-1_CS.
IPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027413. GROEL-like_equatorial.
[Graphical view]
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00304. TCOMPLEXTCP1.
SUPFAMiSSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02343. chap_CCT_epsi. 1 hit.
PROSITEiPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of four new tcp-1-related cct genes from the nematode Caenorhabditis elegans."
    Leroux M.R., Candido E.P.M.
    DNA Cell Biol. 14:951-960(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Bristol N2.
  2. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.

Entry informationi

Entry nameiTCPE_CAEEL
AccessioniPrimary (citable) accession number: P47209
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: June 8, 2016
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.