ID   TCPW_BOVIN              Reviewed;         531 AA.
AC   Q3T084;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=T-complex protein 1 subunit zeta-2;
DE            Short=TCP-1-zeta-2;
DE   AltName: Full=CCT-zeta-2;
GN   Name=CCT6B;
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].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) 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. {ECO:0000250|UniProtKB:Q92526}.
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. {ECO:0000250|UniProtKB:Q92526}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q92526}.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR   EMBL; BC102527; AAI02528.1; -; mRNA.
DR   RefSeq; NP_001029814.1; NM_001034642.2.
DR   AlphaFoldDB; Q3T084; -.
DR   SMR; Q3T084; -.
DR   CORUM; Q3T084; -.
DR   STRING; 9913.ENSBTAP00000027104; -.
DR   PaxDb; Q3T084; -.
DR   PeptideAtlas; Q3T084; -.
DR   PRIDE; Q3T084; -.
DR   GeneID; 538090; -.
DR   KEGG; bta:538090; -.
DR   CTD; 10693; -.
DR   eggNOG; KOG0359; Eukaryota.
DR   InParanoid; Q3T084; -.
DR   OrthoDB; 482152at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005832; C:chaperonin-containing T-complex; IEA:UniProt.
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   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..531
FT                   /note="T-complex protein 1 subunit zeta-2"
FT                   /id="PRO_0000236263"
SQ   SEQUENCE   531 AA;  58031 MW;  90604169095DED3C CRC64;
     MAAIKAINSK AEVARAQAAL AVNICAARGL QDVLRTNLGP KGTMKMLVSG AGDVKLTKDG
     NVLLHEMQIQ HPTASLIAKV ATAQDDITGD GTTSNVLIIG ELLKQADLYI SEGLHPRIIA
     EGFEIAKIKA LEVLEQVKIK KEMKREIHLD VARTSLQTKV HPQLADVLTE AVVDSVLAIR
     RPNYPIDLFM VEIMEMKHKS ETDTKLIKGL VLDHGARHPD MKKRVDDAFI LTCNVSLEYE
     KTEVSSGFFY KTAEEKEKLV KAERKFIEDR VQKIIDLKDK VCAQSNKGFV VINQKGIDPF
     SLDALAKHGI LALRRAKRRN MERLSLACGG VAVNSVEDLS VDCLGHAGLV YEYTLGEEKY
     TFIEDCINPR SVTLLVKGPN KHTLTQIKDA VRDGLRAIKN AIEDGCVVPG AGAVEVVIAE
     ALVTYKHTIQ GRARLGVQAF ADALLIIPKV LAQNSGYDLQ ETLVKVQAEH SNSKQPVGID
     LNTGEPMVAA DAGVWDNYCV KKQLLHSCTV IATNILLVDE IMRAGMSSLK G