TCPG_MOUSE
ID TCPG_MOUSE Reviewed; 545 AA.
AC P80318;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=T-complex protein 1 subunit gamma;
DE Short=TCP-1-gamma;
DE AltName: Full=CCT-gamma;
DE AltName: Full=Matricin;
DE AltName: Full=mTRiC-P5;
GN Name=Cct3; Synonyms=Cctg;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=129/Sv;
RX PubMed=7953530; DOI=10.1016/s0960-9822(94)00024-2;
RA Kubota H., Hynes G., Carne A., Ashworth A., Willison K.R.;
RT "Identification of six Tcp-1-related genes encoding divergent subunits of
RT the TCP-1-containing chaperonin.";
RL Curr. Biol. 4:89-99(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8110840; DOI=10.1016/0167-4781(94)90041-8;
RA Joly E.C., Sevigny G., Todorov I.T., Bibor-Hardy V.;
RT "cDNA encoding a novel TCP1-related protein.";
RL Biochim. Biophys. Acta 1217:224-226(1994).
RN [3]
RP PROTEIN SEQUENCE OF 32-38; 128-138; 150-163; 204-216; 238-248; 428-461;
RP 492-502 AND 508-518, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170 AND SER-252, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 210-386.
RX PubMed=12083524; DOI=10.1016/s0022-2836(02)00190-0;
RA Pappenberger G., Wilsher J.A., Roe S.M., Counsell D.J., Willison K.R.,
RA Pearl L.H.;
RT "Crystal structure of the CCTgamma apical domain: implications for
RT substrate binding to the eukaryotic cytosolic chaperonin.";
RL J. Mol. Biol. 318:1367-1379(2002).
RN [6]
RP INTERACTION WITH DNAAF4.
RX PubMed=23872636; DOI=10.1038/ng.2707;
RA Tarkar A., Loges N.T., Slagle C.E., Francis R., Dougherty G.W.,
RA Tamayo J.V., Shook B., Cantino M., Schwartz D., Jahnke C., Olbrich H.,
RA Werner C., Raidt J., Pennekamp P., Abouhamed M., Hjeij R., Kohler G.,
RA Griese M., Li Y., Lemke K., Klena N., Liu X., Gabriel G., Tobita K.,
RA Jaspers M., Morgan L.C., Shapiro A.J., Letteboer S.J., Mans D.A.,
RA Carson J.L., Leigh M.W., Wolf W.E., Chen S., Lucas J.S., Onoufriadis A.,
RA Plagnol V., Schmidts M., Boldt K., Roepman R., Zariwala M.A., Lo C.W.,
RA Mitchison H.M., Knowles M.R., Burdine R.D., Loturco J.J., Omran H.;
RT "DYX1C1 is required for axonemal dynein assembly and ciliary motility.";
RL Nat. Genet. 45:995-1003(2013).
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 (PubMed:23872636). Interacts with DLEC1 (By
CC similarity). {ECO:0000250|UniProtKB:P49368,
CC ECO:0000269|PubMed:23872636}.
CC -!- INTERACTION:
CC P80318; PRO_0000038598 [P04591]: gag; Xeno; NbExp=3; IntAct=EBI-772361, EBI-10634977;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA19749.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z31556; CAA83431.1; -; mRNA.
DR EMBL; L20509; AAA19749.1; ALT_INIT; mRNA.
DR CCDS; CCDS17468.1; -.
DR PIR; S42723; S42723.
DR PIR; S43062; S43062.
DR RefSeq; NP_033966.1; NM_009836.1.
DR PDB; 1GML; X-ray; 2.20 A; A/B/C/D=210-380.
DR PDB; 1GN1; X-ray; 2.80 A; A/B/C/D/E/F/G/H=210-380.
DR PDBsum; 1GML; -.
DR PDBsum; 1GN1; -.
DR AlphaFoldDB; P80318; -.
DR SMR; P80318; -.
DR BioGRID; 198565; 89.
DR CORUM; P80318; -.
DR DIP; DIP-32344N; -.
DR IntAct; P80318; 60.
DR MINT; P80318; -.
DR STRING; 10090.ENSMUSP00000001452; -.
DR iPTMnet; P80318; -.
DR PhosphoSitePlus; P80318; -.
DR SwissPalm; P80318; -.
DR REPRODUCTION-2DPAGE; IPI00116283; -.
DR REPRODUCTION-2DPAGE; P80318; -.
DR EPD; P80318; -.
DR jPOST; P80318; -.
DR PaxDb; P80318; -.
DR PeptideAtlas; P80318; -.
DR PRIDE; P80318; -.
DR ProteomicsDB; 259364; -.
DR Antibodypedia; 1677; 251 antibodies from 34 providers.
DR DNASU; 12462; -.
DR Ensembl; ENSMUST00000001452; ENSMUSP00000001452; ENSMUSG00000001416.
DR GeneID; 12462; -.
DR KEGG; mmu:12462; -.
DR UCSC; uc008puo.3; mouse.
DR CTD; 7203; -.
DR MGI; MGI:104708; Cct3.
DR VEuPathDB; HostDB:ENSMUSG00000001416; -.
DR eggNOG; KOG0364; Eukaryota.
DR GeneTree; ENSGT00570000079224; -.
DR HOGENOM; CLU_008891_7_3_1; -.
DR InParanoid; P80318; -.
DR OMA; RYCRIEK; -.
DR OrthoDB; 391677at2759; -.
DR PhylomeDB; P80318; -.
DR TreeFam; TF105649; -.
DR BRENDA; 3.6.4.B10; 3474.
DR Reactome; R-MMU-390471; Association of TriC/CCT with target proteins during biosynthesis.
DR Reactome; R-MMU-5620922; BBSome-mediated cargo-targeting to cilium.
DR Reactome; R-MMU-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR BioGRID-ORCS; 12462; 33 hits in 73 CRISPR screens.
DR ChiTaRS; Cct3; mouse.
DR EvolutionaryTrace; P80318; -.
DR PRO; PR:P80318; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P80318; protein.
DR Bgee; ENSMUSG00000001416; Expressed in primitive streak and 263 other tissues.
DR ExpressionAtlas; P80318; baseline and differential.
DR Genevisible; P80318; MM.
DR GO; GO:0044297; C:cell body; IDA:MGI.
DR GO; GO:0005832; C:chaperonin-containing T-complex; IDA:MGI.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0002199; C:zona pellucida receptor complex; IDA:MGI.
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:MGI.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IDA:MGI.
DR GO; GO:0061077; P:chaperone-mediated protein folding; ISO:MGI.
DR GO; GO:0046931; P:pore complex assembly; IMP:MGI.
DR GO; GO:1904851; P:positive regulation of establishment of protein localization to telomere; ISO:MGI.
DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; ISO:MGI.
DR GO; GO:0006457; P:protein folding; ISO:MGI.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR GO; GO:1901998; P:toxin transport; IMP:MGI.
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 3D-structure; Acetylation; ATP-binding; Chaperone; Cytoplasm;
KW Direct protein sequencing; Disulfide bond; Isopeptide bond;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..545
FT /note="T-complex protein 1 subunit gamma"
FT /id="PRO_0000128322"
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:0007744|PubMed:21183079"
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:21183079"
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 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"
FT CONFLICT 124
FT /note="S -> G (in Ref. 2; AAA19749)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="E -> D (in Ref. 2; AAA19749)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="S -> N (in Ref. 2; AAA19749)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="H -> Q (in Ref. 2; AAA19749)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="D -> E (in Ref. 2; AAA19749)"
FT /evidence="ECO:0000305"
FT CONFLICT 474
FT /note="S -> N (in Ref. 2; AAA19749)"
FT /evidence="ECO:0000305"
FT CONFLICT 534
FT /note="N -> S (in Ref. 2; AAA19749)"
FT /evidence="ECO:0000305"
FT CONFLICT 537..538
FT /note="TG -> SS (in Ref. 2; AAA19749)"
FT /evidence="ECO:0000305"
FT CONFLICT 542
FT /note="A -> G (in Ref. 2; AAA19749)"
FT /evidence="ECO:0000305"
FT STRAND 213..221
FT /evidence="ECO:0007829|PDB:1GML"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:1GML"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:1GML"
FT HELIX 264..283
FT /evidence="ECO:0007829|PDB:1GML"
FT STRAND 288..294
FT /evidence="ECO:0007829|PDB:1GML"
FT HELIX 298..306
FT /evidence="ECO:0007829|PDB:1GML"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:1GML"
FT HELIX 317..327
FT /evidence="ECO:0007829|PDB:1GML"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:1GML"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:1GML"
FT HELIX 340..342
FT /evidence="ECO:0007829|PDB:1GML"
FT STRAND 347..355
FT /evidence="ECO:0007829|PDB:1GML"
FT STRAND 358..368
FT /evidence="ECO:0007829|PDB:1GML"
FT STRAND 373..377
FT /evidence="ECO:0007829|PDB:1GML"
SQ SEQUENCE 545 AA; 60630 MW; 492F9743C607FA1D CRC64;
MMGHRPVLVL SQNTKRESGR KVQSGNINAA KTIADIIRTC LGPKSMMKML LDPMGGIVMT
NDGNAILREI QVQHPAAKSM IEISRTQDEE VGDGTTSVII LAGEMLSVAE HFLEQQMHPT
VVISAYRMAL DDMISTLKKI STPVDVNNRE MMLSIINSSI TTKVISRWSS LACNIALDAV
KTVQFEENGR KEIDIKKYAR VEKIPGGIIE DSCVLRGVMI NKDVTHPRMR RYIKNPRIVL
LDSSLEYKKG ESQTDIEITR EEDFTRILQM EEEYIHQLCE DIIQLKPDVV ITEKGISDLA
QHYLMRANVT AIRRVRKTDN NRIARACGAR IVSRPEELRE DDVGTGAGLL EIKKIGDEYF
TFITDCKDPK ACTILLRGAS KEILSEVERN LQDAMQVCRN VLLDPQLVPG GGASEMAVAH
ALTEKSKAMT GVEQWPYRAV AQALEVIPRT LIQNCGASTI RLLTSLRAKH TQESCETWGV
NGETGTLVDM KELGIWEPLA VKLQTYKTAV ETAVLLLRID DIVSGHKKKG DDQNRQTGAP
DAGQE
