TCPD_MOUSE
ID TCPD_MOUSE Reviewed; 539 AA.
AC P80315;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=T-complex protein 1 subunit delta;
DE Short=TCP-1-delta;
DE AltName: Full=A45;
DE AltName: Full=CCT-delta;
GN Name=Cct4; Synonyms=Cctd;
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].
RC TISSUE=Bone marrow;
RX PubMed=7919332;
RA Xie X., Palacios R.;
RT "Cloning and expression of a new mammalian chaperonin gene from a
RT multipotent hematopoietic progenitor clone.";
RL Blood 84:2171-2174(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [5]
RP PROTEIN SEQUENCE OF 60-79; 127-139; 144-206; 246-274; 281-288; 293-302;
RP 307-319; 327-338; 396-403 AND 420-435, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-21 AND LYS-319, AND
RP IDENTIFICATION BY MASS 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 [8]
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).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=23807208; DOI=10.1007/s00018-013-1401-6;
RA Kypri E., Christodoulou A., Maimaris G., Lethan M., Markaki M.,
RA Lysandrou C., Lederer C.W., Tavernarakis N., Geimer S., Pedersen L.B.,
RA Santama N.;
RT "The nucleotide-binding proteins Nubp1 and Nubp2 are negative regulators of
RT ciliogenesis.";
RL Cell. Mol. Life Sci. 71:517-538(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. 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:P50991}.
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:P50991,
CC ECO:0000269|PubMed:23872636}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23807208}.
CC Melanosome {ECO:0000250|UniProtKB:P50991}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:23807208}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000269|PubMed:23807208}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR EMBL; L25913; AAA37418.1; -; mRNA.
DR EMBL; Z31554; CAA83429.1; -; mRNA.
DR EMBL; AB022157; BAA81875.1; -; Genomic_DNA.
DR EMBL; BC054773; AAH54773.1; -; mRNA.
DR CCDS; CCDS24474.1; -.
DR PIR; S43060; S43060.
DR RefSeq; NP_033967.1; NM_009837.1.
DR AlphaFoldDB; P80315; -.
DR SMR; P80315; -.
DR BioGRID; 198567; 82.
DR CORUM; P80315; -.
DR IntAct; P80315; 57.
DR MINT; P80315; -.
DR STRING; 10090.ENSMUSP00000133523; -.
DR iPTMnet; P80315; -.
DR PhosphoSitePlus; P80315; -.
DR SwissPalm; P80315; -.
DR REPRODUCTION-2DPAGE; P80315; -.
DR CPTAC; non-CPTAC-3951; -.
DR EPD; P80315; -.
DR jPOST; P80315; -.
DR PaxDb; P80315; -.
DR PeptideAtlas; P80315; -.
DR PRIDE; P80315; -.
DR ProteomicsDB; 262973; -.
DR Antibodypedia; 15920; 263 antibodies from 32 providers.
DR DNASU; 12464; -.
DR Ensembl; ENSMUST00000173867; ENSMUSP00000133523; ENSMUSG00000007739.
DR GeneID; 12464; -.
DR KEGG; mmu:12464; -.
DR UCSC; uc007ien.1; mouse.
DR CTD; 10575; -.
DR MGI; MGI:104689; Cct4.
DR VEuPathDB; HostDB:ENSMUSG00000007739; -.
DR eggNOG; KOG0358; Eukaryota.
DR GeneTree; ENSGT00550000074956; -.
DR HOGENOM; CLU_008891_9_1_1; -.
DR InParanoid; P80315; -.
DR OMA; HPAANMI; -.
DR OrthoDB; 511484at2759; -.
DR PhylomeDB; P80315; -.
DR TreeFam; TF106332; -.
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; 12464; 33 hits in 73 CRISPR screens.
DR ChiTaRS; Cct4; mouse.
DR PRO; PR:P80315; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P80315; protein.
DR Bgee; ENSMUSG00000007739; Expressed in indifferent gonad and 261 other tissues.
DR ExpressionAtlas; P80315; baseline and differential.
DR Genevisible; P80315; MM.
DR GO; GO:0044297; C:cell body; IDA:MGI.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005832; C:chaperonin-containing T-complex; IDA:MGI.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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:1904851; P:positive regulation of establishment of protein localization to telomere; ISO:MGI.
DR GO; GO:0051973; P:positive regulation of telomerase activity; ISO:MGI.
DR GO; GO:1904874; P:positive regulation of telomerase RNA localization to Cajal body; 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:0090666; P:scaRNA localization to Cajal body; ISO:MGI.
DR GO; GO:1901998; P:toxin transport; IMP:MGI.
DR CDD; cd03338; TCP1_delta; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR012717; Chap_CCT_delta.
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; TIGR02342; chap_CCT_delta; 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; Cell projection; Chaperone; Cilium; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Methylation; Nucleotide-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..539
FT /note="T-complex protein 1 subunit delta"
FT /id="PRO_0000128333"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 19
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P50991"
FT MOD_RES 21
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50991"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50991"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50991"
FT MOD_RES 288
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P50991"
FT MOD_RES 302
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P50991"
FT MOD_RES 319
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 326
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P50991"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50991"
FT CONFLICT 405
FT /note="I -> V (in Ref. 1; AAA37418)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="L -> P (in Ref. 1; AAA37418)"
FT /evidence="ECO:0000305"
FT CONFLICT 453
FT /note="A -> R (in Ref. 1; AAA37418)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 539 AA; 58066 MW; B3EBD470D1C7FABC CRC64;
MPENVASRSG APTAGPGSRG KSAYQDRDKP AQIRFSNISA AKAVADAIRT SLGPKGMDKM
IQDGKGDVTI TNDGATILKQ MQVLHPAARM LVELSKAQDI EAGDGTTSVV IIAGSLLDSC
TKLLQKGIHP TIISESFQKA LEKGLEILTD MSRPVQLSDR ETLLNSATTS LNSKVVSQYS
SLLSPMSVNA VMKVIDPATA TSVDLRDIKI VKKLGGTIDD CELVEGLVLT QKVANSGITR
VEKAKIGLIQ FCLSAPKTDM DNQIVVSDYA QMDRVLREER AYILNLVKQI KKTGCNVLLI
QKSILRDALS DLALHFLNKM KIMVVKDVER EDIEFICKTI GTKPVAHIDQ FTADMLGSAE
LAEEVSLNGS GKLFKITGCT SPGKTVTIVV RGSNKLVIEE AERSIHDALC VIRCLVKKRA
LIAGGGAPEI ELALRLTEYS RTLSGMESYC VRAFADAMEV IPSTLAENAG LNPISTVTEL
RNRHAQGEKT TGINVRKGGI SNILEEMVVQ PLLVSVSALT LATETVRSIL KIDDVVNTR
