ID   TCPG_PIG                Reviewed;          82 AA.
AC   Q29068;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=T-complex protein 1 subunit gamma;
DE            Short=TCP-1-gamma;
DE   AltName: Full=CCT-gamma;
DE   AltName: Full=Matricin;
DE   Flags: Fragment;
GN   Name=CCT3; Synonyms=CCTG;
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 [MRNA].
RA   Anderson J.E., Matteri R.L., Prather R.S.;
RT   "Partial cDNA encoding a TCP-1 related protein expressed in day 17 porcine
RT   embryo.";
RL   Submitted (OCT-1995) 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. As part of the TRiC complex
CC       may play a role in the assembly of BBSome, a complex involved in
CC       ciliogenesis regulating transports vesicles to the cilia. The TRiC
CC       complex plays a role in the folding of actin and tubulin.
CC       {ECO:0000250|UniProtKB:P49368}.
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 (By similarity).
CC       Interacts with DNAAF4 (By similarity). Interacts with DLEC1 (By
CC       similarity). {ECO:0000250|UniProtKB:P49368,
CC       ECO:0000250|UniProtKB:P80318}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR   EMBL; L47772; AAA79024.1; -; mRNA.
DR   AlphaFoldDB; Q29068; -.
DR   SMR; Q29068; -.
DR   PeptideAtlas; Q29068; -.
DR   PRIDE; Q29068; -.
DR   InParanoid; Q29068; -.
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..>82
FT                   /note="T-complex protein 1 subunit gamma"
FT                   /id="PRO_0000128323"
FT   NON_TER         1
FT   NON_TER         82
SQ   SEQUENCE   82 AA;  8713 MW;  183FA85A84C4D3BB CRC64;
     NAAKTIADII RTCLGPKSMM KMLLDPMGGI VMTNDGNAIL REIQVQHPAA KSMIEISRTQ
     DEEVGDGTTS VIILAGEMLS VA