TCPH_MOUSE
ID TCPH_MOUSE Reviewed; 544 AA.
AC P80313;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=T-complex protein 1 subunit eta;
DE Short=TCP-1-eta;
DE AltName: Full=CCT-eta;
GN Name=Cct7; Synonyms=Ccth;
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 TISSUE=Testis;
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 [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=10336634; DOI=10.1046/j.1432-1327.1999.00405.x;
RA Kubota H., Yokota S., Yanagi H., Yura T.;
RT "Structures and co-regulated expression of the genes encoding mouse
RT cytosolic chaperonin CCT subunits.";
RL Eur. J. Biochem. 262:492-500(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [4]
RP PROTEIN SEQUENCE OF 11-37; 54-67; 85-106; 199-217; 219-230; 237-247;
RP 293-306; 358-366; 376-397; 402-418 AND 431-447, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-250, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [7]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-536, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
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. The TRiC complex plays a role
CC in the folding of actin and tubulin. {ECO:0000250|UniProtKB:Q99832}.
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 DLEC1 (By similarity). {ECO:0000250|UniProtKB:Q99832}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:7953530}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR EMBL; Z31399; CAA83274.1; -; mRNA.
DR EMBL; AB022160; BAA81878.1; -; Genomic_DNA.
DR EMBL; BC008255; AAH08255.1; -; mRNA.
DR CCDS; CCDS20295.1; -.
DR PIR; S43058; S43058.
DR RefSeq; NP_031664.3; NM_007638.4.
DR AlphaFoldDB; P80313; -.
DR SMR; P80313; -.
DR BioGRID; 198571; 52.
DR CORUM; P80313; -.
DR IntAct; P80313; 30.
DR MINT; P80313; -.
DR STRING; 10090.ENSMUSP00000032078; -.
DR iPTMnet; P80313; -.
DR PhosphoSitePlus; P80313; -.
DR SwissPalm; P80313; -.
DR REPRODUCTION-2DPAGE; P80313; -.
DR EPD; P80313; -.
DR jPOST; P80313; -.
DR PaxDb; P80313; -.
DR PeptideAtlas; P80313; -.
DR PRIDE; P80313; -.
DR ProteomicsDB; 263025; -.
DR Antibodypedia; 1382; 282 antibodies from 31 providers.
DR DNASU; 12468; -.
DR Ensembl; ENSMUST00000032078; ENSMUSP00000032078; ENSMUSG00000030007.
DR GeneID; 12468; -.
DR KEGG; mmu:12468; -.
DR UCSC; uc009cpv.2; mouse.
DR CTD; 10574; -.
DR MGI; MGI:107184; Cct7.
DR VEuPathDB; HostDB:ENSMUSG00000030007; -.
DR eggNOG; KOG0361; Eukaryota.
DR GeneTree; ENSGT00550000074832; -.
DR HOGENOM; CLU_008891_7_1_1; -.
DR InParanoid; P80313; -.
DR OMA; HRKGNTW; -.
DR OrthoDB; 335406at2759; -.
DR PhylomeDB; P80313; -.
DR TreeFam; TF105641; -.
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-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR Reactome; R-MMU-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-MMU-9013422; RHOBTB1 GTPase cycle.
DR BioGRID-ORCS; 12468; 30 hits in 68 CRISPR screens.
DR ChiTaRS; Cct7; mouse.
DR PRO; PR:P80313; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P80313; protein.
DR Bgee; ENSMUSG00000030007; Expressed in floor plate of midbrain and 257 other tissues.
DR ExpressionAtlas; P80313; baseline and differential.
DR Genevisible; P80313; 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:0005739; C:mitochondrion; HDA: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: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; cd03340; TCP1_eta; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR012720; Chap_CCT_eta.
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 PANTHER; PTHR11353:SF22; PTHR11353:SF22; 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; TIGR02345; chap_CCT_eta; 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 Isopeptide bond; Methylation; Nucleotide-binding; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..544
FT /note="T-complex protein 1 subunit eta"
FT /id="PRO_0000128366"
FT REGION 523..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q99832"
FT MOD_RES 67
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99832"
FT MOD_RES 250
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 320
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99832"
FT MOD_RES 536
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CROSSLNK 430
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99832"
SQ SEQUENCE 544 AA; 59652 MW; 0BD7AD35456EE677 CRC64;
MMPTPVILLK EGTDSSQGIP QLVSNISACQ VIAEAVRTTL GPRGMDKLIV DGRGKATISN
DGATILKLLD VVHPAAKTLV DIAKSQDAEV GDGTTSVTLL AAEFLKQVKP YVEEGLHPQI
IIRAFRTATQ LAVNKIKEIA VTVKKQDKVE QRKMLEKCAM TALSSKLISQ QKVFFAKMVV
DAVMMLDELL QLKMIGIKKV QGGALEESQL VAGVAFKKTF SYAGFEMQPK KYKNPKIALL
NVELELKAEK DNAEIRVHTV EDYQAIVDAE WNILYDKLEK IHQSGAKVIL SKLPIGDVAT
QYFADRDMFC AGRVPEEDLK RTMMACGGSI QTSVNALVPD VLGHCQVFEE TQIGGERYNF
FTGCPKAKTC TIILRGGAEQ FMEETERSLH DAIMIVRRAI KNDSVVAGGG AIEMELSKYL
RDYSRTIPGK QQLLIGAYAK ALEIIPRQLC DNAGFDATNI LNKLRARHAQ GGMWYGVDIN
NENIADNFQA FVWEPAMVRI NALTAASEAA CLIVSVDETI KNPRSTVDPP APSAGRGRGQ
ARFH
