ID   TCPZ_MOUSE              Reviewed;         531 AA.
AC   P80317;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   24-JAN-2024, entry version 180.
DE   RecName: Full=T-complex protein 1 subunit zeta;
DE            Short=TCP-1-zeta;
DE   AltName: Full=CCT-zeta-1;
GN   Name=Cct6a; Synonyms=Cct6, Cctz, Cctz1;
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   PROTEIN SEQUENCE OF 16-28; 106-127; 130-138; 160-180; 200-208; 242-251 AND
RP   524-530, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, 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 ALA-2; LYS-5; LYS-199; LYS-287 AND
RP   LYS-365, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], 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).
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:P40227}.
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.
CC       {ECO:0000250|UniProtKB:P40227}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P40227}.
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues examined.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR   EMBL; Z31557; CAA83432.1; -; mRNA.
DR   EMBL; AB022159; BAA81877.1; -; Genomic_DNA.
DR   PIR; S43063; S43063.
DR   RefSeq; NP_033968.1; NM_009838.2.
DR   AlphaFoldDB; P80317; -.
DR   SMR; P80317; -.
DR   BioGRID; 198569; 18.
DR   CORUM; P80317; -.
DR   IntAct; P80317; 10.
DR   MINT; P80317; -.
DR   STRING; 10090.ENSMUSP00000158738; -.
DR   GlyGen; P80317; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P80317; -.
DR   PhosphoSitePlus; P80317; -.
DR   SwissPalm; P80317; -.
DR   REPRODUCTION-2DPAGE; IPI00116281; -.
DR   REPRODUCTION-2DPAGE; P80317; -.
DR   EPD; P80317; -.
DR   jPOST; P80317; -.
DR   MaxQB; P80317; -.
DR   PaxDb; 10090-ENSMUSP00000031402; -.
DR   PeptideAtlas; P80317; -.
DR   ProteomicsDB; 259367; -.
DR   Pumba; P80317; -.
DR   DNASU; 12466; -.
DR   GeneID; 12466; -.
DR   KEGG; mmu:12466; -.
DR   UCSC; uc029voy.2; mouse.
DR   AGR; MGI:107943; -.
DR   CTD; 908; -.
DR   MGI; MGI:107943; Cct6a.
DR   eggNOG; KOG0359; Eukaryota.
DR   InParanoid; P80317; -.
DR   OrthoDB; 1058698at2759; -.
DR   PhylomeDB; P80317; -.
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   BioGRID-ORCS; 12466; 9 hits in 25 CRISPR screens.
DR   ChiTaRS; Cct6a; mouse.
DR   PRO; PR:P80317; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P80317; Protein.
DR   GO; GO:0001669; C:acrosomal vesicle; IDA:MGI.
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: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:0071987; F:WD40-repeat domain binding; ISO:MGI.
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   CDD; cd03342; TCP1_zeta; 1.
DR   Gene3D; 3.50.7.10; GroEL; 1.
DR   Gene3D; 1.10.560.10; GroEL-like equatorial domain; 1.
DR   Gene3D; 3.30.260.10; TCP-1-like chaperonin intermediate domain; 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   NCBIfam; TIGR02347; chap_CCT_zeta; 1.
DR   NCBIfam; NF041083; thermosome_beta; 1.
DR   PANTHER; PTHR11353; CHAPERONIN; 1.
DR   PANTHER; PTHR11353:SF54; T-COMPLEX PROTEIN 1 SUBUNIT ZETA; 1.
DR   Pfam; PF00118; Cpn60_TCP1; 1.
DR   PRINTS; PR00304; TCOMPLEXTCP1.
DR   SUPFAM; SSF52029; GroEL apical domain-like; 1.
DR   SUPFAM; SSF48592; GroEL equatorial domain-like; 1.
DR   SUPFAM; SSF54849; GroEL-intermediate domain like; 1.
DR   PROSITE; PS00750; TCP1_1; 1.
DR   PROSITE; PS00751; TCP1_2; 1.
DR   PROSITE; PS00995; TCP1_3; 1.
DR   UCD-2DPAGE; P80317; -.
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:0007744|PubMed:23806337"
FT   CHAIN           2..531
FT                   /note="T-complex protein 1 subunit zeta"
FT                   /id="PRO_0000128356"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         5
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         199
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         205
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P40227"
FT   MOD_RES         287
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         365
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         377
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P40227"
FT   MOD_RES         388
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P40227"
FT   CROSSLNK        251
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P40227"
SQ   SEQUENCE   531 AA;  58004 MW;  D68C606D67F29642 CRC64;
     MAAVKTLNPK AEVARAQAAL AVNISAARGL QDVLRTNLGP KGTMKMLVSG AGDIKLTKDG
     NVLLHEMQIQ HPTASLIAKV ATAQDDITGD GTTSNVLIIG ELLKQADLYI SEGLHPRIIT
     EGFEAAKEKA LQFLEQVKVS KEMDRETLID VARTSLRTKV HAELADVLTE AVVDSILAIR
     KKDEPIDLFM VEIMEMKHKS ETDTSLIRGL VLDHGARHPD MKKRVENAYI LTCNVSLEYE
     KTEVNSGFFY KSAEEREKLV KAERKFIEDR VKKIIELKKK VCGDSDKGFV VINQKGIDPF
     SLDALAKEGI VALRRAKRRN MERLTLACGG IALNSFDDLN PDCLGHAGLV YEYTLGEEKF
     TFIEKCNNPR SVTLLVKGPN KHTLTQIKDA IRDGLRAVKN AIDDGCVVPG AGAVEVALAE
     ALIKYKPSVK GRAQLGVQAF ADALLIIPKV LAQNSGFDLQ ETLVKVQAEH SESGQLVGVD
     LSTGEPMVAA EMGVWDNYCV KKQLLHSCTV IATNILLVDE IMRAGMSSLK G
//