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CCT6A

Gene
CCT6A
Protein
T-complex protein 1 subunit zeta 1
Organism
Arabidopsis thaliana
Length
535 amino acids
Function
Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.
Similarity
Belongs to the TCP-1 chaperonin family.
Mass
58.95 kDa
Sequence
MSVRVLNPNAEVLNKSAALHMTINAAKGLQDVLKSNLGPKGTIKMLVGGSGDIKLTKDGNTLLKEMQIQNPTAIMIARTAVAQDDISGDGTTSTVIFIGELMKQSERCIDEGMHPRVLVDGFEIAKRATLQFLDTFKTPVVMGDEPDKEILKMVARTTLRTKLYEGLADQLTDIVVNSVLCIRKPQEPIDLFMVEIMHMRHKFDVDTRLVEGLVLDHGSRHPDMKRRAENCHILTCNVSLEYEKSEINAGFFYSNAEQREAMVTAERRSVDERVQKIIELKNKVCAGNDNSFVILNQKGIDPPSLDLLAREGIIALRRAKRRNMERLVLACGGEAVNSVDDLTPDCLGWAGLVYEHVLGEEKYTFVEQVKNPHSCTILIKGPNDHTIAQIKDAVRDGLRSVKNTLEDECVVLGAGAFEVAARQHLINEVKKTVQGRAQLGVEAFANALLVVPKTLAENAGLDTQDVIISLTSEHDKGNIVGLDLQDGEPVDPQLAGIFDNYSVKRQLINSGPVIASQLLLVDEVIRAGRNMRKPT

Gene
CCT6A
Protein
T-complex protein 1 subunit zeta
Organism
Bos taurus
Length
531 amino acids
Function
Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. The TRiC complex plays a role in the folding of actin and tubulin.
Similarity
Belongs to the TCP-1 chaperonin family.
Mass
57.956 kDa
Sequence
MAAVKTLNPKAEVARAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEQVKVSKEMDRETLIDVARTSLRTKVHAELADVLTEAVVDSILAIKKQDEPIDLFMVEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSAEEREKLVKAERKFIEDRVKKIIELKKKVCGDSDKGFVVINQKGIDPFSLDALAKEGIIALRRAKRRNMERLTLACGGIALNSLDDLNPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAIRDGLRAVKNAIDDGCVVPGAGAVEVAMAEALVKYKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKVQAEHSESGQLVGVDLNTGEPMVAAEAGIWDNYCVKKQLLHSCTVIATNILLVDEIMRAGMSSLKG

Gene
CCT6A
Protein
T-complex protein 1 subunit zeta
Organism
Homo sapiens
Length
531 amino acids
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). The TRiC complex plays a role in the folding of actin and tubulin (Probable).
Similarity
Belongs to the TCP-1 chaperonin family.
Mass
58.024 kDa
Sequence
MAAVKTLNPKAEVARAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEEVKVSREMDRETLIDVARTSLRTKVHAELADVLTEAVVDSILAIKKQDEPIDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSAEEREKLVKAERKFIEDRVKKIIELKRKVCGDSDKGFVVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGGVALNSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEIMRAGMSSLKG

Gene
Cct6a
Protein
T-complex protein 1 subunit zeta
Organism
Mus musculus
Length
531 amino acids
Function
Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. The TRiC complex plays a role in the folding of actin and tubulin.
Similarity
Belongs to the TCP-1 chaperonin family.
Mass
58.004 kDa
Sequence
MAAVKTLNPKAEVARAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEQVKVSKEMDRETLIDVARTSLRTKVHAELADVLTEAVVDSILAIRKKDEPIDLFMVEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVENAYILTCNVSLEYEKTEVNSGFFYKSAEEREKLVKAERKFIEDRVKKIIELKKKVCGDSDKGFVVINQKGIDPFSLDALAKEGIVALRRAKRRNMERLTLACGGIALNSFDDLNPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLVKGPNKHTLTQIKDAIRDGLRAVKNAIDDGCVVPGAGAVEVALAEALIKYKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKVQAEHSESGQLVGVDLSTGEPMVAAEMGVWDNYCVKKQLLHSCTVIATNILLVDEIMRAGMSSLKG