CCT7 chaperonin containing TCP1 subunit 7 [Macaca mulatta (Rhesus monkey)] - Gene

Summary

Official Symbol: CCT7provided by VGNC
Official Full Name: chaperonin containing TCP1 subunit 7provided by VGNC
Primary source: VGNC:VGNC:103798
See related: Ensembl:ENSMMUG00000012448
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Macaca mulatta
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Cercopithecidae; Cercopithecinae; Macaca
Orthologs: human mouse all
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Genomic context

Location:: chromosome: 13

Exon count:: 13

Annotation release	Status	Assembly	Chr	Location
103	current	Mmul_10 (GCF_003339765.1)	13	NC_041766.1 (35520579..35538913, complement)
102	previous assembly	Mmul_8.0.1 (GCF_000772875.2)	13	NC_027905.1 (74327872..74346196)

Chromosome 13 - NC_041766.1 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

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General gene information

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Gene Ontology Provided by RefSeq

Function	Evidence Code	Pubs
enables ATP binding	IEA Inferred from Electronic Annotation more info	PubMed
enables ATP hydrolysis activity	IEA Inferred from Electronic Annotation more info	PubMed
enables ATP-dependent protein folding chaperone	IEA Inferred from Electronic Annotation more info	PubMed
enables unfolded protein binding	IEA Inferred from Electronic Annotation more info	PubMed

Process	Evidence Code	Pubs
involved_in protein folding	IEA Inferred from Electronic Annotation more info	PubMed

Component	Evidence Code	Pubs
part_of chaperonin-containing T-complex	IEA Inferred from Electronic Annotation more info	PubMed

General protein information

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Preferred Names: T-complex protein 1 subunit eta

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_001265751.1 → NP_001252680.1 T-complex protein 1 subunit eta

See identical proteins and their annotated locations for NP_001252680.1

Status: PROVISIONAL

Source sequence(s)

JV667163

UniProtKB/TrEMBL

A0A1D5RF71, I2CXZ1

Related

ENSMMUP00000058965.2, ENSMMUT00000061529.2

Conserved Domains (1) summary

cd03340
Location:5 → 525

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), ...

RefSeqs of Annotated Genomes: Macaca mulatta Annotation Release 103 details...

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

Reference Mmul_10 Primary Assembly

Genomic

NC_041766.1 Reference Mmul_10 Primary Assembly

Range

35520579..35538913 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_015112533.2 → XP_014968019.1 T-complex protein 1 subunit eta isoform X1

UniProtKB/TrEMBL

F6XZH8, H9F9H9

Related

ENSMMUP00000036471.3, ENSMMUT00000043469.3

Conserved Domains (1) summary

cd03340
Location:1 → 481

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), ...
XM_015112534.2 → XP_014968020.1 T-complex protein 1 subunit eta isoform X2

Conserved Domains (1) summary

cd03340
Location:22 → 397

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), ...