UniProt functional annotation for P49368



	UniProt functional annotation for P49368

UniProt code: P49368.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Function: Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis (PubMed:25467444). The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance (PubMed:25467444). As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia (PubMed:20080638). The TRiC complex plays a role in the folding of actin and tubulin (Probable). {ECO:0000269|PubMed:20080638, ECO:0000269|PubMed:25467444, ECO:0000305}.

Subunit: Component of the chaperonin-containing T-complex (TRiC), a heterooligomeric complex of about 850 to 900 kDa that forms two stacked rings, 12 to 16 nm in diameter (PubMed:20080638, PubMed:25467444). Interacts with PACRG (PubMed:14532270). Interacts with DNAAF4 (By similarity). Interacts with DLEC1 (PubMed:33144677). {ECO:0000250|UniProtKB:P80318, ECO:0000269|PubMed:14532270, ECO:0000269|PubMed:20080638, ECO:0000269|PubMed:25467444, ECO:0000269|PubMed:33144677}.

Subcellular location: Cytoplasm {ECO:0000305}.

Similarity: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.

Sequence caution: Sequence=AAH08019.1; Type=Erroneous initiation; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



Function:		Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis (PubMed:25467444). The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance (PubMed:25467444). As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia (PubMed:20080638). The TRiC complex plays a role in the folding of actin and tubulin (Probable). {ECO:0000269\|PubMed:20080638, ECO:0000269\|PubMed:25467444, ECO:0000305}.


Subunit:		Component of the chaperonin-containing T-complex (TRiC), a heterooligomeric complex of about 850 to 900 kDa that forms two stacked rings, 12 to 16 nm in diameter (PubMed:20080638, PubMed:25467444). Interacts with PACRG (PubMed:14532270). Interacts with DNAAF4 (By similarity). Interacts with DLEC1 (PubMed:33144677). {ECO:0000250\|UniProtKB:P80318, ECO:0000269\|PubMed:14532270, ECO:0000269\|PubMed:20080638, ECO:0000269\|PubMed:25467444, ECO:0000269\|PubMed:33144677}.
Subcellular location:		Cytoplasm {ECO:0000305}.
Similarity:		Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
Sequence caution:		Sequence=AAH08019.1; Type=Erroneous initiation; Evidence={ECO:0000305};