TCP-1 T-complex protein 1 alpha subunit [Arabidopsis thaliana (thale cress)] - Gene

Summary

Go to the top of the page Help

Official Symbol: TCP-1
Official Full Name: T-complex protein 1 alpha subunit
Primary source: TAIR:AT3G20050
Locus tag: AT3G20050
See related: Araport:AT3G20050
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Arabidopsis thaliana (ecotype: Columbia)
Lineage: Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis
Also known as: ATTCP-1; T-complex protein 1 alpha subunit
Summary: Encodes a putative cytoplasmic chaperonin that is similar to mouse Tcp-1 (t complex polypeptide 1).
NEW: Try the new Gene table
Try the new Transcript table

Genomic context

Go to the top of the page Help

See TCP-1 in Genome Data Viewer

Location:: chromosome: 3

Exon count:: 17

Sequence:: Chromosome: 3; NC_003074.8 (6998159..7002435, complement)

Chromosome 3 - NC_003074.8 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

Go to the top of the page Help

Go to reference sequence details

Genomic Sequence:: NC_003074.8

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the page Help

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Submit: New GeneRIF Correction

Pathways from PubChem

Go to the top of the page

Interactions

Go to the top of the page Help

Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

Go to the top of the page Help

Homology

Orthologs from OrthoDB

NM_112896.4

Supported by ESTs:

Gene Ontology Provided by TAIR

Function	Evidence Code	Pubs
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	IEA Inferred from Electronic Annotation more info

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

Component	Evidence Code	Pubs
located_in cytoplasm	ISM Inferred from Sequence Model more info
located_in cytosol	HDA more info	PubMed

General protein information

Go to the top of the page Help

Preferred Names: T-complex protein 1 alpha subunit

NP_188640.1

T-complex protein 1 alpha subunit (TCP-1); FUNCTIONS IN: unfolded protein binding, ATP binding; INVOLVED IN: protein folding, cellular protein metabolic process; LOCATED IN: cellular_component unknown; EXPRESSED IN: 24 plant structures; EXPRESSED DURING: 13 growth stages; CONTAINS InterPro DOMAIN/s: Chaperonin Cpn60/TCP-1 (InterPro:IPR002423), Chaperone, tailless complex polypeptide 1 (InterPro:IPR017998), Chaperonin TCP-1, conserved site (InterPro:IPR002194), T-complex protein 1, alpha subunit (InterPro:IPR012715); BEST Arabidopsis thaliana protein match is: TCP-1/cpn60 chaperonin family protein (TAIR:AT3G11830.1); Has 17155 Blast hits to 17114 proteins in 3594 species: Archae - 808; Bacteria - 7960; Metazoa - 2159; Fungi - 1408; Plants - 801; Viruses - 0; Other Eukaryotes - 4019 (source: NCBI BLink).

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

Genome Annotation

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

Reference assembly

Genomic

NC_003074.8 Reference assembly

Range

6998159..7002435 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_112896.4 → NP_188640.1 T-complex protein 1 alpha subunit [Arabidopsis thaliana]

See identical proteins and their annotated locations for NP_188640.1

Status: REVIEWED

UniProtKB/Swiss-Prot

P28769, Q5E917, Q8H0U0, Q9LJZ6

UniProtKB/TrEMBL

A0A178VBD4, A0A5S9XE97, A0A654FE88

Conserved Domains (1) summary

cd03335
Location:12 → 538

TCP1_alpha; TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha 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 ...