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cct-6 T-complex protein 1 subunit zeta [ Caenorhabditis elegans ]

Gene ID: 175819, updated on 2-Nov-2024

Summary

Official Symbol
cct-6
Official Full Name
T-complex protein 1 subunit zeta
Primary source
WormBase:WBGene00000381
Locus tag
CELE_F01F1.8
See related
AllianceGenome:WB:WBGene00000381
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Caenorhabditis elegans (strain: Bristol N2)
Lineage
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis
Summary
Predicted to enable unfolded protein binding activity. Predicted to be involved in protein folding. Predicted to be located in cytoplasm. Predicted to be part of chaperonin-containing T-complex. Orthologous to several human genes including CCT6B (chaperonin containing TCP1 subunit 6B). [provided by Alliance of Genome Resources, Nov 2024]
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Genomic context

See cct-6 in Genome Data Viewer
Location:
chromosome: III
Exon count:
6
Sequence:
Chromosome: III; NC_003281.10 (5853537..5855687, complement)

Chromosome III - NC_003281.10Genomic Context describing neighboring genes Neighboring gene ncRNA Neighboring gene RNA helicase Neighboring gene Putative aldehyde dehydrogenase family 7 member A1 homolog Neighboring gene Peptidase S9 prolyl oligopeptidase catalytic domain-containing protein Neighboring gene Aspartyl aminopeptidase

Pathways from PubChem

Interactions

Products Interactant Other Gene Complex Source Pubs Description

General gene information

Markers

Gene Ontology Provided by WormBase

Function Evidence Code Pubs
enables ATP binding IEA
Inferred from Electronic Annotation
more info
 
enables ATP hydrolysis activity IEA
Inferred from Electronic Annotation
more info
 
enables ATP-dependent protein folding chaperone IEA
Inferred from Electronic Annotation
more info
 
enables unfolded protein binding IBA
Inferred from Biological aspect of Ancestor
more info
 
enables unfolded protein binding IEA
Inferred from Electronic Annotation
more info
 
Process Evidence Code Pubs
involved_in protein folding IBA
Inferred from Biological aspect of Ancestor
more info
 
involved_in protein folding IEA
Inferred from Electronic Annotation
more info
 
Component Evidence Code Pubs
part_of chaperonin-containing T-complex IBA
Inferred from Biological aspect of Ancestor
more info
 
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
 

General protein information

Preferred Names
T-complex protein 1 subunit zeta
NP_741153.1
  • Confirmed by transcript evidence
NP_741154.1
  • Partially confirmed by transcript evidence

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_003281.10 Reference assembly

    Range
    5853537..5855687 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_171135.10NP_741153.1  T-complex protein 1 subunit zeta [Caenorhabditis elegans]

    See identical proteins and their annotated locations for NP_741153.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    P46550
    Conserved Domains (2) summary
    cd03342
    Location:7530
    TCP1_zeta; TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL) ...
    TIGR02347
    Location:3534
    chap_CCT_zeta; T-complex protein 1, zeta subunit
  2. NM_171136.7NP_741154.1  T-complex protein 1 subunit zeta [Caenorhabditis elegans]

    See identical proteins and their annotated locations for NP_741154.1

    Status: REVIEWED

    UniProtKB/TrEMBL
    G8JY43
    Conserved Domains (1) summary
    cd03342
    Location:7410
    TCP1_zeta; TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL) ...