TCPB_MOUSE
ID TCPB_MOUSE Reviewed; 535 AA.
AC P80314; Q9R1U0;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=T-complex protein 1 subunit beta;
DE Short=TCP-1-beta;
DE AltName: Full=CCT-beta;
GN Name=Cct2; Synonyms=Cctb;
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 [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 TISSUE=Eye;
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 26-40; 51-82; 90-131; 139-170; 182-189; 192-203;
RP 205-223; 224-230; 237-248; 264-272; 285-293; 323-342; 348-402; 406-427;
RP 432-441; 445-500 AND 502-516, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., 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).
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:P78371}.
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. Interacts with
CC FLCN (By similarity). Interacts with DLEC1 (By similarity).
CC {ECO:0000250|UniProtKB:P78371}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P78371}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR EMBL; Z31553; CAA83428.1; -; mRNA.
DR EMBL; AB022156; BAA81874.1; -; Genomic_DNA.
DR EMBL; BC007470; AAH07470.1; -; mRNA.
DR EMBL; BC026918; AAH26918.1; -; mRNA.
DR CCDS; CCDS36067.1; -.
DR PIR; S43059; S43059.
DR RefSeq; NP_031662.2; NM_007636.2.
DR RefSeq; XP_006513224.1; XM_006513161.2.
DR AlphaFoldDB; P80314; -.
DR SMR; P80314; -.
DR BioGRID; 198564; 75.
DR CORUM; P80314; -.
DR DIP; DIP-32343N; -.
DR IntAct; P80314; 52.
DR MINT; P80314; -.
DR STRING; 10090.ENSMUSP00000036288; -.
DR iPTMnet; P80314; -.
DR PhosphoSitePlus; P80314; -.
DR SwissPalm; P80314; -.
DR REPRODUCTION-2DPAGE; P80314; -.
DR EPD; P80314; -.
DR jPOST; P80314; -.
DR PaxDb; P80314; -.
DR PeptideAtlas; P80314; -.
DR PRIDE; P80314; -.
DR ProteomicsDB; 263093; -.
DR Antibodypedia; 762; 365 antibodies from 39 providers.
DR DNASU; 12461; -.
DR Ensembl; ENSMUST00000047672; ENSMUSP00000036288; ENSMUSG00000034024.
DR GeneID; 12461; -.
DR KEGG; mmu:12461; -.
DR UCSC; uc007hcs.1; mouse.
DR CTD; 10576; -.
DR MGI; MGI:107186; Cct2.
DR VEuPathDB; HostDB:ENSMUSG00000034024; -.
DR eggNOG; KOG0363; Eukaryota.
DR GeneTree; ENSGT00550000074930; -.
DR HOGENOM; CLU_008891_6_2_1; -.
DR InParanoid; P80314; -.
DR OMA; YCTGGEI; -.
DR OrthoDB; 335406at2759; -.
DR PhylomeDB; P80314; -.
DR TreeFam; TF105645; -.
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 Reactome; R-MMU-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-MMU-9013422; RHOBTB1 GTPase cycle.
DR BioGRID-ORCS; 12461; 30 hits in 76 CRISPR screens.
DR ChiTaRS; Cct2; mouse.
DR PRO; PR:P80314; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P80314; protein.
DR Bgee; ENSMUSG00000034024; Expressed in superior cervical ganglion and 244 other tissues.
DR ExpressionAtlas; P80314; baseline and differential.
DR Genevisible; P80314; MM.
DR GO; GO:0044297; C:cell body; IDA:MGI.
DR GO; GO:0005832; C:chaperonin-containing T-complex; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO: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:0031625; F:ubiquitin protein ligase binding; 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:0051086; P:chaperone mediated protein folding independent of cofactor; ISO:MGI.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; ISO: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; cd03336; TCP1_beta; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR012716; Chap_CCT_beta.
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:SF23; PTHR11353:SF23; 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; TIGR02341; chap_CCT_beta; 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; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P78371"
FT CHAIN 2..535
FT /note="T-complex protein 1 subunit beta"
FT /id="PRO_0000128317"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P78371"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78371"
FT MOD_RES 13
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P78371"
FT MOD_RES 181
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P78371"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78371"
FT MOD_RES 261
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P78371"
FT CROSSLNK 248
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78371"
FT CONFLICT 23
FT /note="T -> I (in Ref. 1; CAA83428)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="V -> G (in Ref. 1; CAA83428)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 535 AA; 57477 MW; 605744DF068BB192 CRC64;
MASLSLAPVN IFKAGADEER AETARLSSFI GAIAIGDLVK STLGPKGMDK ILLSSGRDAA
LMVTNDGATI LKNIGVDNPA AKVLVDMSRV QDDEVGDGTT SVTVLAAELL REAESLIAKK
IHPQTIISGW REATKAAREA LLSSAVDHGS DEARFWQDLM NIAGTTLSSK LLTHHKDHFT
KLAVEAVLRL KGSGNLEAIH VIKKLGGSLA DSYLDEGFLL DKKIGVNQPK RIENAKILIA
NTGMDTDKIK IFGSRVRVDS TAKVAEIEHA EKEKMKEKVE RILKHGINCF INRQLIYNYP
EQLFGAAGVM AIEHADFAGV ERLALVTGGE IASTFDHPEL VKLGSCKLIE EVMIGEDKLI
HFSGVALGEA CTIVLRGATQ QILDEAERSL HDALCVLAQT VKDPRTVYGG GCSEMLMAHA
VTQLANRTPG KEAVAMESFA KALRMLPTII ADNAGYDSAD LVAQLRAAHS EGHITAGLDM
KEGTIGDMAV LGITESFQVK RQVLLSAAEA AEVILRVDNI IKAAPRKRVP DHHPC
