CCT7 chaperonin-containing T-complex subunit CCT7 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: CCT7
Official Full Name: chaperonin-containing T-complex subunit CCT7
Primary source: SGD:S000003647
Locus tag: YJL111W
See related: AllianceGenome:SGD:S000003647; FungiDB:YJL111W; VEuPathDB:YJL111W
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Also known as: TCP7
Summary: Enables unfolded protein binding activity. Involved in protein folding. Located in cytoplasm. Part of chaperonin-containing T-complex. Orthologous to human CCT7 (chaperonin containing TCP1 subunit 7). [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

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See CCT7 in Genome Data Viewer

Location:: chromosome: X

Exon count:: 1

Sequence:: Chromosome: X; NC_001142.9 (207877..209529)

Chromosome X - NC_001142.9 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001142.9

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Chaperonin point mutation enhances cadmium endurance in Saccharomyces cerevisiae.
Title: Chaperonin point mutation enhances cadmium endurance in Saccharomyces cerevisiae.

Submit: New GeneRIF Correction

Pathways from PubChem

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

Gene Ontology Provided by SGD

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	IDA Inferred from Direct Assay more info	PubMed
enables unfolded protein binding	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in chaperone mediated protein folding independent of cofactor	IEA Inferred from Electronic Annotation more info
involved_in protein folding	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein folding	IDA Inferred from Direct Assay more info	PubMed
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
part_of chaperonin-containing T-complex	IDA Inferred from Direct Assay more info	PubMed
part_of chaperonin-containing T-complex	IEA Inferred from Electronic Annotation more info
part_of chaperonin-containing T-complex	IPI Inferred from Physical Interaction more info	PubMed
located_in cytoplasm	HDA more info	PubMed
located_in cytoplasm	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: chaperonin-containing T-complex subunit CCT7

NP_012424.1

Subunit of the cytosolic chaperonin Cct ring complex; related to Tcp1p, required for the assembly of actin and tubulins in vivo; mutant has increased aneuploidy tolerance

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_001142.9 Reference assembly

Range

207877..209529

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001181544.1 → NP_012424.1 TPA: chaperonin-containing T-complex subunit CCT7 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_012424.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VW73, P42943

UniProtKB/TrEMBL

A6ZQL6, B3LQ04, B5VL62, C7GR05, C8ZBA6, G2WGQ8, N1P1K8

Conserved Domains (1) summary

cd03340
Location:9 → 529

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), ...