TCPZ_BOVIN
ID TCPZ_BOVIN Reviewed; 531 AA.
AC Q3MHL7; A5D9B9;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=T-complex protein 1 subunit zeta;
DE Short=TCP-1-zeta;
DE AltName: Full=CCT-zeta;
DE AltName: Full=CCT-zeta-1;
GN Name=CCT6A;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the chaperonin-containing T-complex (TRiC), a
CC molecular chaperone complex that assists the folding of proteins upon
CC ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1,
CC thereby regulating telomere maintenance. The TRiC complex plays a role
CC in the folding of actin and tubulin. {ECO:0000250|UniProtKB:P40227}.
CC -!- SUBUNIT: Component of the chaperonin-containing T-complex (TRiC), a
CC heterooligomeric complex of about 850 to 900 kDa that forms two stacked
CC rings, 12 to 16 nm in diameter. Interacts with PACRG.
CC {ECO:0000250|UniProtKB:P40227}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P40227}.
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR EMBL; BT030538; ABQ12978.1; -; mRNA.
DR EMBL; BC105191; AAI05192.1; -; mRNA.
DR EMBL; BC142274; AAI42275.1; -; mRNA.
DR RefSeq; NP_001029714.1; NM_001034542.2.
DR PDB; 3IYG; EM; -; Z=9-525.
DR PDB; 4B2T; X-ray; 5.50 A; Z/z=1-531.
DR PDBsum; 3IYG; -.
DR PDBsum; 4B2T; -.
DR AlphaFoldDB; Q3MHL7; -.
DR SMR; Q3MHL7; -.
DR CORUM; Q3MHL7; -.
DR DIP; DIP-58623N; -.
DR IntAct; Q3MHL7; 2.
DR STRING; 9913.ENSBTAP00000010765; -.
DR PeptideAtlas; Q3MHL7; -.
DR PRIDE; Q3MHL7; -.
DR Ensembl; ENSBTAT00000071259; ENSBTAP00000069251; ENSBTAG00000008184.
DR GeneID; 521540; -.
DR KEGG; bta:521540; -.
DR CTD; 908; -.
DR VEuPathDB; HostDB:ENSBTAG00000008184; -.
DR VGNC; VGNC:97250; CCT6A.
DR eggNOG; KOG0359; Eukaryota.
DR GeneTree; ENSGT00940000154631; -.
DR InParanoid; Q3MHL7; -.
DR OMA; LHPRIMT; -.
DR OrthoDB; 482152at2759; -.
DR BRENDA; 3.6.4.B10; 908.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000008184; Expressed in conceptus and 104 other tissues.
DR ExpressionAtlas; Q3MHL7; baseline.
DR GO; GO:0005832; C:chaperonin-containing T-complex; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0071987; F:WD40-repeat domain binding; IEA:Ensembl.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IEA:Ensembl.
DR GO; GO:1904851; P:positive regulation of establishment of protein localization to telomere; IEA:Ensembl.
DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IEA:Ensembl.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR CDD; cd03342; TCP1_zeta; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR012722; Chap_CCT_zeta.
DR InterPro; IPR017998; Chaperone_TCP-1.
DR InterPro; IPR002194; Chaperonin_TCP-1_CS.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR027413; GROEL-like_equatorial_sf.
DR InterPro; IPR027410; TCP-1-like_intermed_sf.
DR PANTHER; PTHR11353; PTHR11353; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00304; TCOMPLEXTCP1.
DR SUPFAM; SSF48592; SSF48592; 1.
DR SUPFAM; SSF52029; SSF52029; 1.
DR SUPFAM; SSF54849; SSF54849; 1.
DR TIGRFAMs; TIGR02347; chap_CCT_zeta; 1.
DR PROSITE; PS00750; TCP1_1; 1.
DR PROSITE; PS00751; TCP1_2; 1.
DR PROSITE; PS00995; TCP1_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Chaperone; Cytoplasm;
KW Isopeptide bond; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P40227"
FT CHAIN 2..531
FT /note="T-complex protein 1 subunit zeta"
FT /id="PRO_0000236262"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P40227"
FT MOD_RES 5
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P80317"
FT MOD_RES 199
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P40227"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40227"
FT MOD_RES 287
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P80317"
FT MOD_RES 365
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P40227"
FT MOD_RES 377
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P40227"
FT MOD_RES 388
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P40227"
FT CROSSLNK 251
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P40227"
SQ SEQUENCE 531 AA; 57956 MW; 290F77CB5F0B12C2 CRC64;
MAAVKTLNPK AEVARAQAAL AVNISAARGL QDVLRTNLGP KGTMKMLVSG AGDIKLTKDG
NVLLHEMQIQ HPTASLIAKV ATAQDDITGD GTTSNVLIIG ELLKQADLYI SEGLHPRIIT
EGFEAAKEKA LQFLEQVKVS KEMDRETLID VARTSLRTKV HAELADVLTE AVVDSILAIK
KQDEPIDLFM VEIMEMKHKS ETDTSLIRGL VLDHGARHPD MKKRVEDAYI LTCNVSLEYE
KTEVNSGFFY KSAEEREKLV KAERKFIEDR VKKIIELKKK VCGDSDKGFV VINQKGIDPF
SLDALAKEGI IALRRAKRRN MERLTLACGG IALNSLDDLN PDCLGHAGLV YEYTLGEEKF
TFIEKCNNPR SVTLLIKGPN KHTLTQIKDA IRDGLRAVKN AIDDGCVVPG AGAVEVAMAE
ALVKYKPSVK GRAQLGVQAF ADALLIIPKV LAQNSGFDLQ ETLVKVQAEH SESGQLVGVD
LNTGEPMVAA EAGIWDNYCV KKQLLHSCTV IATNILLVDE IMRAGMSSLK G
