ID   TCPG_CAEEL              Reviewed;         543 AA.
AC   Q9N4J8;
DT   11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 3.
DT   03-AUG-2022, entry version 164.
DE   RecName: Full=T-complex protein 1 subunit gamma {ECO:0000305};
GN   Name=cct-3 {ECO:0000312|WormBase:F54A3.3};
GN   ORFNames=F54A3.3 {ECO:0000312|WormBase:F54A3.3};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN   [1] {ECO:0000312|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2] {ECO:0000305}
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=16054029; DOI=10.1016/j.devcel.2005.07.003;
RA   Srayko M., Kaya A., Stamford J., Hyman A.A.;
RT   "Identification and characterization of factors required for microtubule
RT   growth and nucleation in the early C. elegans embryo.";
RL   Dev. Cell 9:223-236(2005).
CC   -!- FUNCTION: Molecular chaperone; assists the folding of proteins upon ATP
CC       hydrolysis (By similarity). Known to play a role, in vitro, in the
CC       folding of actin and tubulin (By similarity). Plays a role in
CC       microtubule polymerization (PubMed:16054029).
CC       {ECO:0000250|UniProtKB:P48605, ECO:0000269|PubMed:16054029}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P49368}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in severely
CC       reduced microtubule growth rate. {ECO:0000269|PubMed:16054029}.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family.
CC       {ECO:0000255|RuleBase:RU004187}.
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DR   EMBL; BX284602; CCD71741.1; -; Genomic_DNA.
DR   RefSeq; NP_494218.2; NM_061817.5.
DR   AlphaFoldDB; Q9N4J8; -.
DR   SMR; Q9N4J8; -.
DR   STRING; 6239.F54A3.3; -.
DR   EPD; Q9N4J8; -.
DR   PaxDb; Q9N4J8; -.
DR   PeptideAtlas; Q9N4J8; -.
DR   EnsemblMetazoa; F54A3.3.1; F54A3.3.1; WBGene00018782.
DR   GeneID; 173581; -.
DR   KEGG; cel:CELE_F54A3.3; -.
DR   UCSC; F54A3.3; c. elegans.
DR   CTD; 173581; -.
DR   WormBase; F54A3.3; CE31540; WBGene00018782; cct-3.
DR   eggNOG; KOG0364; Eukaryota.
DR   GeneTree; ENSGT00570000079224; -.
DR   HOGENOM; CLU_008891_7_3_1; -.
DR   InParanoid; Q9N4J8; -.
DR   OMA; RYCRIEK; -.
DR   OrthoDB; 391677at2759; -.
DR   PhylomeDB; Q9N4J8; -.
DR   BRENDA; 3.6.4.B10; 1045.
DR   Reactome; R-CEL-390471; Association of TriC/CCT with target proteins during biosynthesis.
DR   Reactome; R-CEL-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR   PRO; PR:Q9N4J8; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00018782; Expressed in larva and 4 other tissues.
DR   GO; GO:0005832; C:chaperonin-containing T-complex; IBA:GO_Central.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
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   CDD; cd03337; TCP1_gamma; 1.
DR   Gene3D; 1.10.560.10; -; 1.
DR   Gene3D; 3.30.260.10; -; 1.
DR   Gene3D; 3.50.7.10; -; 1.
DR   InterPro; IPR012719; Chap_CCT_gamma.
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; TIGR02344; chap_CCT_gamma; 1.
DR   PROSITE; PS00750; TCP1_1; 1.
DR   PROSITE; PS00751; TCP1_2; 1.
DR   PROSITE; PS00995; TCP1_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Microtubule; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..543
FT                   /note="T-complex protein 1 subunit gamma"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000436249"
SQ   SEQUENCE   543 AA;  60457 MW;  DD5A55ACAE135F4F CRC64;
     MRGAGQQPII VLSQGTKRES GHQVQIGNIN ACKTIADVIR TSLGPRAMLK MLMDPMGGIV
     MTNDGNAILR EITVKHPAAK SMIEIARTQD EETGDGTTSV IILAGEVMAH AQTYLEQKTH
     PTLIIKAYRQ ALEDMIQWSE NKFSKTVDIT DDAEIAKVVK SCLGTKMISK WMDLAVNISI
     QAVKTIRVEK AGVREIDIKR YCRIEKIPGG RIEDSQVVKG IVVNKDILHA KMRRRIENPR
     IVLLDCNLEY KKGESQTSLE IMREEDISAI LEQEEQAIRK QCDEIIKLKP DLVFTEKGIS
     DLAQHFLLKA GITCLRRLKK TDNNRLARVC GARVVHDTSD LRDEDVGTKA QLFEVVKIAD
     EYYTYVTAET TTACTVVLRG PSKDVINEVE RNLQDSLHVV RNIMINPKLV PGGGALEMAL
     SREIEQQGAK MDGVKKWPYK AIGLALEVIP RTLIQNCGGS TIRKMTELRA IHAQNAENWT
     FGVDGTSGDL VDMNKLEIWD PLAVRIQVLK TAIETSVMLL RIDDIVSGTK KAVGGEKQEM
     MPQ