cct-7 T-complex protein 1 subunit eta [Caenorhabditis elegans] - Gene

Summary

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Official Symbol: cct-7
Official Full Name: T-complex protein 1 subunit eta
Primary source: WormBase:WBGene00020391
Locus tag: CELE_T10B5.5
See related: AllianceGenome:WB:WBGene00020391
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. Is expressed in several structures, including anchor cell; head; pharynx; tail; and vulval muscle. Orthologous to human CCT7 (chaperonin containing TCP1 subunit 7). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See cct-7 in Genome Data Viewer

Location:: chromosome: V

Exon count:: 4

Sequence:: Chromosome: V; NC_003283.11 (1872246..1875505)

Chromosome V - NC_003283.11 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_003283.11

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

T10B5.4 (e-PCR)
- UniSTS:317739

T10B5.5 (e-PCR)
- UniSTS:314952

Homology

Orthologs from OrthoDB

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

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Preferred Names: T-complex protein 1 subunit eta

NP_503522.1

Confirmed by transcript evidence

NP_872179.1

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

NC_003283.11 Reference assembly

Range

1872246..1875505

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_071121.7 → NP_503522.1 T-complex protein 1 subunit eta [Caenorhabditis elegans]

See identical proteins and their annotated locations for NP_503522.1

Status: REVIEWED

UniProtKB/TrEMBL

Q9TZS5

Conserved Domains (2) summary

cd03340
Location:5 → 523

TCP1_eta; TCP-1 (CTT or eukaryotic type II) chaperonin family, eta 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), ...

TIGR02345
Location:3 → 520

chap_CCT_eta; T-complex protein 1, eta subunit
NM_182379.5 → NP_872179.1 T-complex protein 1 subunit eta [Caenorhabditis elegans]

See identical proteins and their annotated locations for NP_872179.1

Status: REVIEWED

UniProtKB/TrEMBL

Q86S29

Conserved Domains (1) summary

cd03340
Location:5 → 442

TCP1_eta; TCP-1 (CTT or eukaryotic type II) chaperonin family, eta 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), ...