ID   TCPZ_PIG                Reviewed;         104 AA.
AC   Q29236;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=T-complex protein 1 subunit zeta;
DE            Short=TCP-1-zeta;
DE   AltName: Full=CCT-zeta;
DE   Flags: Fragment;
GN   Name=CCT6; Synonyms=CCTZ;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Small intestine;
RX   PubMed=8672129; DOI=10.1007/s003359900153;
RA   Winteroe A.K., Fredholm M., Davies W.;
RT   "Evaluation and characterization of a porcine small intestine cDNA library:
RT   analysis of 839 clones.";
RL   Mamm. Genome 7:509-517(1996).
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.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR   EMBL; F14833; CAA23284.1; -; mRNA.
DR   STRING; 9823.ENSSSCP00000008274; -.
DR   PaxDb; Q29236; -.
DR   PeptideAtlas; Q29236; -.
DR   eggNOG; KOG0359; Eukaryota.
DR   InParanoid; Q29236; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; 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; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   Gene3D; 1.10.560.10; -; 1.
DR   InterPro; IPR017998; Chaperone_TCP-1.
DR   InterPro; IPR002194; Chaperonin_TCP-1_CS.
DR   InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR   InterPro; IPR027413; GROEL-like_equatorial_sf.
DR   PANTHER; PTHR11353; PTHR11353; 1.
DR   Pfam; PF00118; Cpn60_TCP1; 1.
DR   PRINTS; PR00304; TCOMPLEXTCP1.
DR   SUPFAM; SSF48592; SSF48592; 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..>104
FT                   /note="T-complex protein 1 subunit zeta"
FT                   /id="PRO_0000128357"
FT   NON_TER         1
FT   NON_TER         104
SQ   SEQUENCE   104 AA;  10938 MW;  AFB1758393FFA606 CRC64;
     SQAALAVNIS AARGLQDVLR TNLGPKGTMK MLVSGAGDIK LTKDGNVLLH EMQIQHPTAS
     LIAKVATAQD DITGDGXTSN VLIIGELLKQ ADLYISEGLH PRII