Tcp1 t-complex protein 1 [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Tcp1provided by MGI
Official Full Name: t-complex protein 1provided by MGI
Primary source: MGI:MGI:98535
See related: Ensembl:ENSMUSG00000068039 AllianceGenome:MGI:98535
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: CCT; p63; Cct1; Ccta; TRic; Tp63; Tcp-1; c-cpn
Summary: Predicted to enable protein folding chaperone; ubiquitin protein ligase binding activity; and unfolded protein binding activity. Acts upstream of or within binding activity of sperm to zona pellucida. Located in several cellular components, including acrosomal vesicle; heterochromatin; and pericentriolar material. Part of chaperonin-containing T-complex and zona pellucida receptor complex. Is expressed in several structures, including cerebral cortex; extraembryonic component; genitourinary system; humerus; and immune system. Orthologous to human TCP1 (t-complex 1). [provided by Alliance of Genome Resources, Dec 2024]
Expression: Ubiquitous expression in testis adult (RPKM 173.1), CNS E11.5 (RPKM 109.2) and 25 other tissues See more
Orthologs: human all
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Genomic context

Location:: 17 A1; 17 8.72 cM

Exon count:: 12

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	17	NC_000083.7 (13135216..13143954)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	17	NC_000083.6 (12916329..12925067)

Chromosome 17 - NC_000083.7 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?

The Molecular Chaperone CCT Sequesters Gelsolin and Protects it from Cleavage by Caspase-3.
Title: The Molecular Chaperone CCT Sequesters Gelsolin and Protects it from Cleavage by Caspase-3.
Resistance of Acta2(R149C/+) mice to aortic disease is associated with defective release of mutant smooth muscle alpha-actin from the chaperonin-containing TCP1 folding complex.
Title: Resistance of Acta2(R149C/+) mice to aortic disease is associated with defective release of mutant smooth muscle α-actin from the chaperonin-containing TCP1 folding complex.
chaperonin-containing TCP-1 complex required for lysosomal functioning and autophagosome degradation
Title: CCT complex restricts neuropathogenic protein aggregation via autophagy.
The authors identify and confirm interaction of M72 with the eukaryotic chaperonin tailless complex protein -1 (TCP-1) ring complex (TRiC) or chaperonin containing tailless complex polypeptide 1 (CCT). Accumulating biochemical evidence indicates M72 forms homo-oligomers and is a substrate of TRiC/CCT
Title: Murine cytomegalovirus M72 promotes acute virus replication in vivo and is a substrate of the TRiC/CCT complex.
treating BACHD cortical neurons with ApiCCT1 prevented BACHD striatal neuronal atrophy by enhancing release of BDNF that subsequently acts through tyrosine receptor kinase B (TrkB) receptor on striatal neurons. Our findings are evidence that TRiC reagent-mediated reductions in mHTT enhanced BDNF delivery to restore the trophic status of BACHD striatal neurons.
Title: TRiC subunits enhance BDNF axonal transport and rescue striatal atrophy in Huntington's disease.
this study shows that CCTalpha is required for antigen-specific, germinal center-derived memory B cells
Title: Phosphatidylcholine as a metabolic cue for determining B cell fate and function.
Data show that T-complex protein 1 (TCP-1) may be a crucial downstream molecule of purinergic receptor P2X 7 (P2X7R) and plays a role in lymphoid neoplasm metastasis.
Title: Silencing P2X7 receptor downregulates the expression of TCP-1 involved in lymphoma lymphatic metastasis.
The data presented here reveal an additional level of interplay between CCT and actin mediated via gelsolin, suggesting that CCT may influence processes depending on gelsolin activity, such as cell motility.
Title: The molecular chaperone CCT modulates the activity of the actin filament severing and capping protein gelsolin in vitro.
Host CCTalpha is required for efficient transcription and replication of rabies virus.
Title: The chaperonin CCTα is required for efficient transcription and replication of rabies virus.
Our data provide new evidence indicating the essential role of the chaperonin CCT in the biogenesis of vertebrate photoreceptor sensory cilia
Title: Essential role of the chaperonin CCT in rod outer segment biogenesis.

Submit: New GeneRIF Correction See all GeneRIFs (16)

Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Endonuclease-mediated (3)

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

D10Mit157.2 (e-PCR), detects polymorphism
- UniSTS:126061

TCP1 (e-PCR)
- UniSTS:266174

Tcp1 (e-PCR), detects polymorphism
- UniSTS:144574

AI528772 (e-PCR)
- UniSTS:180963

Gene Ontology Provided by MGI

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 protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein folding chaperone	ISO Inferred from Sequence Orthology more info
enables ubiquitin protein ligase binding	IEA Inferred from Electronic Annotation more info
enables ubiquitin protein ligase binding	ISO Inferred from Sequence Orthology 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
acts_upstream_of_or_within binding of sperm to zona pellucida	IDA Inferred from Direct Assay more info	PubMed
involved_in chaperone mediated protein folding independent of cofactor	IEA Inferred from Electronic Annotation more info
involved_in chaperone-mediated protein folding	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of establishment of protein localization to telomere	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of establishment of protein localization to telomere	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of telomerase RNA localization to Cajal body	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of telomerase RNA localization to Cajal body	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of telomere maintenance via telomerase	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of telomere maintenance via telomerase	ISO Inferred from Sequence Orthology more info
involved_in protein folding	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein folding	ISO Inferred from Sequence Orthology more info
involved_in protein stabilization	IEA Inferred from Electronic Annotation more info
involved_in protein stabilization	ISO Inferred from Sequence Orthology more info
involved_in scaRNA localization to Cajal body	IEA Inferred from Electronic Annotation more info
involved_in scaRNA localization to Cajal body	ISO Inferred from Sequence Orthology more info

Component	Evidence Code	Pubs
located_in Golgi apparatus	IDA Inferred from Direct Assay more info	PubMed
located_in acrosomal vesicle	IDA Inferred from Direct Assay more info	PubMed
located_in cell body	IDA Inferred from Direct Assay more info	PubMed
located_in centrosome	ISO Inferred from Sequence Orthology more info
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	ISO Inferred from Sequence Orthology more info
located_in heterochromatin	IDA Inferred from Direct Assay more info	PubMed
located_in heterochromatin	ISO Inferred from Sequence Orthology more info
located_in microtubule	IEA Inferred from Electronic Annotation more info
located_in microtubule	ISO Inferred from Sequence Orthology more info
located_in microtubule organizing center	IDA Inferred from Direct Assay more info	PubMed
located_in myelin sheath	HDA more info	PubMed
located_in pericentriolar material	IDA Inferred from Direct Assay more info	PubMed
part_of zona pellucida receptor complex	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: T-complex protein 1 subunit alpha

Names: CCT-alpha; T-complex protein 1 subunit alpha A; T-complex protein 1 subunit alpha B; TCP-1-A; TCP-1-B; TCP-1-alpha; t-complex polypeptide 1; tailless complex polypeptide 1A; tailless complex polypeptide 1B

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_001290712.1 → NP_001277641.1 T-complex protein 1 subunit alpha isoform 2

See identical proteins and their annotated locations for NP_001277641.1

Status: VALIDATED

Description

Transcript Variant: This variant (2) lacks an alternate exon in the 5' coding region and initiates translation at an alternate start codon compared to variant 1. The encoded protein (isoform 2) has a distinct N-terminus and is shorter than isoform 1.

Source sequence(s)

AK149611, AK153430, CN725473

Consensus CDS

CCDS70760.1

UniProtKB/Swiss-Prot

P11983

Related

ENSMUSP00000086418.7, ENSMUST00000089024.13

Conserved Domains (2) summary

cd03335
Location:2 → 486

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 ...

TIGR02340
Location:2 → 491

chap_CCT_alpha; T-complex protein 1, alpha subunit
NM_013686.4 → NP_038714.2 T-complex protein 1 subunit alpha isoform 1

See identical proteins and their annotated locations for NP_038714.2

Status: VALIDATED

Description

Transcript Variant: This variant (1) represents the longer transcript and encodes the longer protein (isoform 1).

Source sequence(s)

AK149611, AK166966, CN725473

Consensus CDS

CCDS28397.1

UniProtKB/Swiss-Prot

P11983, P11984, Q3TJ96, Q3TKU1, Q3U5T8, Q3U7I8, Q3UAA8, Q3UB80, Q3UE48

Related

ENSMUSP00000116108.2, ENSMUST00000151287.8

Conserved Domains (2) summary

cd03335
Location:9 → 535

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 ...

TIGR02340
Location:5 → 540

chap_CCT_alpha; T-complex protein 1, alpha subunit