ID   TCPZ_PONAB              Reviewed;         531 AA.
AC   Q5RCD2;
DT   24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=T-complex protein 1 subunit zeta;
DE            Short=TCP-1-zeta;
DE   AltName: Full=CCT-zeta;
GN   Name=CCT6;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Molecular chaperone; assists the folding of proteins upon ATP
CC       hydrolysis. Known to play a role, in vitro, in the folding of actin and
CC       tubulin (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterooligomeric complex of about 850 to 900 kDa that forms
CC       two stacked rings, 12 to 16 nm in diameter. Interacts with PACRG (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR858342; CAH90575.1; -; mRNA.
DR   RefSeq; NP_001125308.1; NM_001131836.1.
DR   AlphaFoldDB; Q5RCD2; -.
DR   SMR; Q5RCD2; -.
DR   STRING; 9601.ENSPPYP00000023457; -.
DR   GeneID; 100172207; -.
DR   KEGG; pon:100172207; -.
DR   CTD; 908; -.
DR   eggNOG; KOG0359; Eukaryota.
DR   InParanoid; Q5RCD2; -.
DR   OrthoDB; 482152at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005832; C:chaperonin-containing T-complex; ISS:UniProtKB.
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; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Chaperone; Cytoplasm; Isopeptide bond;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; 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_0000128358"
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;  58077 MW;  1709B071EEB736C9 CRC64;
     MAAVKTLNPK AEVARAQAAL AVNISAARGL QDVLRTNLGP KGTMKMLVSG AGDIKLTKDG
     NVLLHEMQIQ HPTASLIAKV ATAQDDITGD GTTSNVLIIG ELLKQADLYI SEGLHPRIIT
     EGFEAAKEKA LQFLEEVKVS REMDRETLID VARTSLRTKV HAELADVLTE AVVDSILAIK
     KQDEPIDLFM IEIMEMKHKS ETDTSLIRGL VLDHGARHPD MKKRVEDAYI LTCNVSLEYE
     KTEVNSGFFY KSAEEREKLV KAERKFIEDR VKKIIELKRK VCGDSDKGFV VINQKGIDPF
     SLDALSKEGI VALRRAKRRN MERLTLACGG VALNSFDDLS PDQLGHAGLV YEYTLGEEKF
     TFIEKCNNPR SVTLLIKGPN KHTLTQIKDA VRDGLRAVRN AIDDGCVVPG AGAVEVAMAE
     ALIKHKPSVK GRAQLGVQAF ADALLIIPKV LAQNSGFDLQ ETLVKIQAEH SESGQLVGVD
     LNTGEPMVAA EVGVWDNYCV KKQLLHSCTV IATNILLVDE IMRAGMSSLK G