TCPW_MOUSE
ID TCPW_MOUSE Reviewed; 531 AA.
AC Q61390; Q9R1U2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=T-complex protein 1 subunit zeta-2;
DE Short=TCP-1-zeta-2;
DE AltName: Full=CCT-zeta-2;
DE Short=Cctz-2;
GN Name=Cct6b;
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 STRAIN=129/Sv; TISSUE=Testis;
RX PubMed=9013858; DOI=10.1016/s0014-5793(96)01501-3;
RA Kubota H., Hynes G.M., Kerr S.M., Willison K.R.;
RT "Tissue-specific subunit of the mouse cytosolic chaperonin-containing TCP-
RT 1.";
RL FEBS Lett. 402:53-56(1997).
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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. {ECO:0000250|UniProtKB:Q92526}.
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. {ECO:0000250|UniProtKB:Q92526}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q92526}.
CC -!- TISSUE SPECIFICITY: Testis specific.
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR EMBL; Z50192; CAA90574.1; -; mRNA.
DR EMBL; AB022086; BAA81891.1; -; Genomic_DNA.
DR CCDS; CCDS25145.1; -.
DR RefSeq; NP_033969.2; NM_009839.3.
DR AlphaFoldDB; Q61390; -.
DR SMR; Q61390; -.
DR BioGRID; 198570; 7.
DR CORUM; Q61390; -.
DR IntAct; Q61390; 1.
DR STRING; 10090.ENSMUSP00000021040; -.
DR iPTMnet; Q61390; -.
DR PhosphoSitePlus; Q61390; -.
DR EPD; Q61390; -.
DR jPOST; Q61390; -.
DR MaxQB; Q61390; -.
DR PaxDb; Q61390; -.
DR PRIDE; Q61390; -.
DR ProteomicsDB; 263266; -.
DR Antibodypedia; 27366; 131 antibodies from 24 providers.
DR DNASU; 12467; -.
DR Ensembl; ENSMUST00000021040; ENSMUSP00000021040; ENSMUSG00000020698.
DR GeneID; 12467; -.
DR KEGG; mmu:12467; -.
DR UCSC; uc007kmx.3; mouse.
DR CTD; 10693; -.
DR MGI; MGI:1329013; Cct6b.
DR VEuPathDB; HostDB:ENSMUSG00000020698; -.
DR eggNOG; KOG0359; Eukaryota.
DR GeneTree; ENSGT00940000156339; -.
DR HOGENOM; CLU_008891_3_1_1; -.
DR InParanoid; Q61390; -.
DR OMA; KSETDTX; -.
DR OrthoDB; 482152at2759; -.
DR PhylomeDB; Q61390; -.
DR TreeFam; TF106333; -.
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 BioGRID-ORCS; 12467; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Cct6b; mouse.
DR PRO; PR:Q61390; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q61390; protein.
DR Bgee; ENSMUSG00000020698; Expressed in spermatid and 33 other tissues.
DR ExpressionAtlas; Q61390; baseline and differential.
DR Genevisible; Q61390; MM.
DR GO; GO:0005832; C:chaperonin-containing T-complex; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO: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:0006457; P:protein folding; ISO:MGI.
DR GO; GO:1901998; P:toxin transport; IMP:MGI.
DR CDD; cd03342; TCP1_zeta; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR012722; Chap_CCT_zeta.
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; TIGR02347; chap_CCT_zeta; 1.
DR PROSITE; PS00751; TCP1_2; 1.
DR PROSITE; PS00995; TCP1_3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome.
FT CHAIN 1..531
FT /note="T-complex protein 1 subunit zeta-2"
FT /id="PRO_0000128364"
FT CONFLICT 112
FT /note="E -> K (in Ref. 1; CAA90574)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 531 AA; 58185 MW; 5B8C600231A1F6B5 CRC64;
MAAIKIANPG AEVTRSQAAL AVNICAARGL QDVLRPTLGP KGALKMLVSG AGDIKLTKDG
NVLLHEMQIQ HPTASIIAKV AAAQDHVTGD GTTSNVLIIG ELLKQADLYI SEGLHPRIIT
EGFDVAKTKA LEVLDEIKVQ KEMKREILLD VARTSLQTKV HAELADILTE AVVDSVLAIR
RPGVPIDLFM VEIVEMRHKS ETDTQLIRGL VLDHGARHPR MRKQVRDAYI LTCNVSLEYE
KTEVSSGFFY KTVEEKEKLV KAERKFIEDR VQKIIDLKQK VCAESNKGFV VINQKGIDPV
SLEMLAKHNI VALRRAKRRN LERLTLACGG LAVNSFEGLS EECLGHAGLV FEYALGEEKF
TFIEDCVNPL SVTLLVKGPN KHTLIQIKDA LRDGLRAVKN AIEDGCVVPG AGAVEVAIAE
ALVNYKHRVQ GRVRLGIQAF ADALLIIPKV LAQNSGYDLQ ETLIKIQTKH AESKELLGID
LNTGEPMAAA EAGIWDNYCV KKHLLHSCTV IATNILLVDE IMRAGMSSLR D
