TCPG_RAT
ID TCPG_RAT Reviewed; 545 AA.
AC Q6P502;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=T-complex protein 1 subunit gamma;
DE Short=TCP-1-gamma;
DE AltName: Full=CCT-gamma;
GN Name=Cct3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PROTEIN SEQUENCE OF 295-306, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (NOV-2006) to UniProtKB.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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; BC063178; AAH63178.1; -; mRNA.
DR RefSeq; NP_954522.1; NM_199091.2.
DR AlphaFoldDB; Q6P502; -.
DR SMR; Q6P502; -.
DR BioGRID; 254921; 9.
DR IntAct; Q6P502; 5.
DR MINT; Q6P502; -.
DR STRING; 10116.ENSRNOP00000025824; -.
DR iPTMnet; Q6P502; -.
DR PhosphoSitePlus; Q6P502; -.
DR jPOST; Q6P502; -.
DR PaxDb; Q6P502; -.
DR PRIDE; Q6P502; -.
DR Ensembl; ENSRNOT00000025824; ENSRNOP00000025824; ENSRNOG00000019090.
DR GeneID; 295230; -.
DR KEGG; rno:295230; -.
DR UCSC; RGD:735038; rat.
DR CTD; 7203; -.
DR RGD; 735038; Cct3.
DR eggNOG; KOG0364; Eukaryota.
DR GeneTree; ENSGT00570000079224; -.
DR HOGENOM; CLU_008891_7_3_1; -.
DR InParanoid; Q6P502; -.
DR OMA; RYCRIEK; -.
DR OrthoDB; 391677at2759; -.
DR PhylomeDB; Q6P502; -.
DR TreeFam; TF105649; -.
DR BRENDA; 3.6.4.B10; 5301.
DR Reactome; R-RNO-390471; Association of TriC/CCT with target proteins during biosynthesis.
DR Reactome; R-RNO-5620922; BBSome-mediated cargo-targeting to cilium.
DR Reactome; R-RNO-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR PRO; PR:Q6P502; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000019090; Expressed in testis and 20 other tissues.
DR Genevisible; Q6P502; RN.
DR GO; GO:0044297; C:cell body; ISO:RGD.
DR GO; GO:0005832; C:chaperonin-containing T-complex; ISS:UniProtKB.
DR GO; GO:0005874; C:microtubule; ISO:RGD.
DR GO; GO:0002199; C:zona pellucida receptor complex; ISO:RGD.
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:0044183; F:protein folding chaperone; ISO:RGD.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; ISO:RGD.
DR GO; GO:0061077; P:chaperone-mediated protein folding; ISO:RGD.
DR GO; GO:0046931; P:pore complex assembly; ISO:RGD.
DR GO; GO:1904851; P:positive regulation of establishment of protein localization to telomere; ISO:RGD.
DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; ISO:RGD.
DR GO; GO:0006457; P:protein folding; ISO:RGD.
DR GO; GO:0050821; P:protein stabilization; ISO:RGD.
DR GO; GO:1901998; P:toxin transport; ISO:RGD.
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 1: Evidence at protein level;
KW Acetylation; ATP-binding; Chaperone; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Isopeptide bond; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..545
FT /note="T-complex protein 1 subunit gamma"
FT /id="PRO_0000270762"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P49368"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49368"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P80318"
FT MOD_RES 222
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P49368"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49368"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49368"
FT MOD_RES 247
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P49368"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 430
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49368"
FT MOD_RES 459
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49368"
FT DISULFID 366..372
FT /evidence="ECO:0000250"
FT CROSSLNK 15
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49368"
FT CROSSLNK 248
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49368"
FT CROSSLNK 249
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49368"
FT CROSSLNK 381
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49368"
SQ SEQUENCE 545 AA; 60647 MW; 76C2B128DA799809 CRC64;
MMGHRPVLVL SQNTKRESGR KVQSGNINAA KTIADIIRTC LGPKSMMKML LDPMGGIVMT
NDGNAILREI QVQHPAAKSM IEISRTQDEE VGDGTTSVII LAGEMLSVAE HFLEQQMHPT
VVISAYRMAL DDMVSTLKKI STPVDVNNRD MMLNIINSSI TTKVISRWSS LACNIALDAV
KTVQFEENGR KEIDIKKYAR VEKIPGGIIE DSCVLRGVMI NKDVTHPRMR RYIKNPRIVL
LDSSLEYKKG ESQTDIEITR EEDFTRILQM EEEYIQQLCE DIIQLKPDVV ITEKGISDLA
QHYLMRANVT AIRRVRKTDN NRIARACGAR IVSRPEELRE DDVGTGAGLL EIKKIGDEYF
TFITDCKDPK ACTILLRGAS KEILSEVERN LQDAMQVCRN VLLDPQLVPG GGASEMAVAH
ALTEKSKAMT GVEQWPYRAV AQALEVIPRT LIQNCGASTI RLLTSLRAKH TQENCETWGV
NGETGTLVDM KELGIWEPLA VKLQTYKTAV ETAVLLLRID DIVSGHKKKG DDQNRQTGAP
DAGQE
