TCPQ_MOUSE
ID TCPQ_MOUSE Reviewed; 548 AA.
AC P42932;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=T-complex protein 1 subunit theta;
DE Short=TCP-1-theta;
DE AltName: Full=CCT-theta;
GN Name=Cct8; Synonyms=Cctq;
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].
RX PubMed=7890169; DOI=10.1016/0378-1119(94)00880-2;
RA Kubota H., Hynes G., Willison K.;
RT "The eighth Cct gene, Cctq, encoding the theta subunit of the cytosolic
RT chaperonin containing TCP-1.";
RL Gene 154:231-236(1995).
RN [2]
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 [3]
RP PROTEIN SEQUENCE OF 8-16; 63-74; 156-165; 172-181; 207-224; 261-296;
RP 308-314; 368-400; 408-421; 441-450; 477-504 AND 510-520, AND IDENTIFICATION
RP BY MASS 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND IDENTIFICATION BY
RP 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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-400, 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 [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).
RN [7]
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:P50990}.
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). {ECO:0000250|UniProtKB:P50990,
CC ECO:0000269|PubMed:23872636}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P50990}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:P50990}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000269|PubMed:23807208}.
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z37164; CAA85521.1; -; mRNA.
DR EMBL; BC009007; AAH09007.1; -; mRNA.
DR CCDS; CCDS37384.1; -.
DR PIR; JC4073; JC4073.
DR RefSeq; NP_033970.3; NM_009840.3.
DR AlphaFoldDB; P42932; -.
DR SMR; P42932; -.
DR BioGRID; 198572; 71.
DR CORUM; P42932; -.
DR IntAct; P42932; 48.
DR MINT; P42932; -.
DR STRING; 10090.ENSMUSP00000026704; -.
DR iPTMnet; P42932; -.
DR PhosphoSitePlus; P42932; -.
DR SwissPalm; P42932; -.
DR REPRODUCTION-2DPAGE; P42932; -.
DR EPD; P42932; -.
DR jPOST; P42932; -.
DR PaxDb; P42932; -.
DR PeptideAtlas; P42932; -.
DR PRIDE; P42932; -.
DR ProteomicsDB; 263094; -.
DR Antibodypedia; 6409; 299 antibodies from 32 providers.
DR DNASU; 12469; -.
DR Ensembl; ENSMUST00000026704; ENSMUSP00000026704; ENSMUSG00000025613.
DR GeneID; 12469; -.
DR KEGG; mmu:12469; -.
DR UCSC; uc007zul.1; mouse.
DR CTD; 10694; -.
DR MGI; MGI:107183; Cct8.
DR VEuPathDB; HostDB:ENSMUSG00000025613; -.
DR eggNOG; KOG0362; Eukaryota.
DR GeneTree; ENSGT00550000074783; -.
DR InParanoid; P42932; -.
DR OMA; WGLKYAV; -.
DR OrthoDB; 617040at2759; -.
DR PhylomeDB; P42932; -.
DR TreeFam; TF105699; -.
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-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR BioGRID-ORCS; 12469; 29 hits in 73 CRISPR screens.
DR ChiTaRS; Cct8; mouse.
DR PRO; PR:P42932; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; P42932; protein.
DR Bgee; ENSMUSG00000025613; Expressed in otic placode and 275 other tissues.
DR ExpressionAtlas; P42932; baseline and differential.
DR Genevisible; P42932; 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:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI.
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: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; cd03341; TCP1_theta; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR012721; Chap_CCT_theta.
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; TIGR02346; chap_CCT_theta; 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; Isopeptide bond;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P50990"
FT CHAIN 2..548
FT /note="T-complex protein 1 subunit theta"
FT /id="PRO_0000128374"
FT REGION 529..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P50990"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 30
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P50990"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50990"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50990"
FT MOD_RES 317
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50990"
FT MOD_RES 318
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P50990"
FT MOD_RES 400
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 466
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P50990"
FT MOD_RES 505
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P50990"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50990"
FT CROSSLNK 224
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P50990"
FT CROSSLNK 254
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P50990"
FT CROSSLNK 260
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P50990"
FT CROSSLNK 459
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:P50990"
FT CROSSLNK 534
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P50990"
FT CROSSLNK 539
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P50990"
SQ SEQUENCE 548 AA; 59555 MW; 4B5265250CFF1FE2 CRC64;
MALHVPKAPG FAQMLKDGAK HFSGLEEAVY RNIQACKELA QTTRTAYGPN GMNKMVINRL
EKLFVTNDAA TILRELEVQH PAAKMIVMAS HMQEQEVGDG TNFVLVFAGA LLELAEELLR
IGLSVSEVIS GYEIACKKAH EILPELVCCS AKNLRDVDEV SSLLRTSIMS KQYGSETFLA
KLIAQACVSI FPDSGNFNVD NIRVCKILGS GIYSSSVLHG MVFKKETEGD VTSVKDAKIA
VYSCPFDGMI TETKGTVLIK TAEELMNFSK GEENLMDAQV KAIAGTGANV IVTGGKVADI
ALHYANKYNI MLVRLNSKWD LRRLCKTVGA TALPKLTPPV QEEMGHCDSV YLSEVGDTQV
VVFKHEKEDG AISTIVLRGS TDNLMDDIER AVDDGVNTFK VLTRDKRLVP GGGATEIELA
KQITSYGETC PGLEQYAIKK FAEAFEAIPR ALAENSGVKA NEVISKLYSV HQEGNKNVGL
DIEAEVPAVK DMLEASILDT YLGKYWAIKL ATNAAVTVLR VDQIIMAKPA GGPKPPSGKK
DWDDDQND
