ID   TCPW_HUMAN              Reviewed;         530 AA.
AC   Q92526; B4DX20; B4DYB0; Q8TC34;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 5.
DT   24-JUL-2024, entry version 201.
DE   RecName: Full=T-complex protein 1 subunit zeta-2;
DE            Short=TCP-1-zeta-2;
DE   AltName: Full=CCT-zeta-2;
DE   AltName: Full=CCT-zeta-like;
DE   AltName: Full=Chaperonin containing T-complex polypeptide 1 subunit 6B;
DE   AltName: Full=TCP-1-zeta-like;
DE   AltName: Full=Testis-specific Tcp20;
DE   AltName: Full=Testis-specific protein TSA303 {ECO:0000303|PubMed:8812458};
GN   Name=CCT6B;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-247, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Testis;
RX   PubMed=8812458; DOI=10.1006/geno.1996.0467;
RA   Ozaki K., Kuroki T., Hayashi S., Nakamura Y.;
RT   "Isolation of three testis-specific genes (TSA303, TSA806, TSA903) by a
RT   differential mRNA display method.";
RL   Genomics 36:316-319(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   TISSUE=Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS GLN-17 AND
RP   ALA-48.
RC   TISSUE=Testis;
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
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:0000305|PubMed:8812458}.
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:0000305|PubMed:8812458}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:8812458}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q92526-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q92526-2; Sequence=VSP_043040;
CC       Name=3;
CC         IsoId=Q92526-3; Sequence=VSP_047129;
CC   -!- TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:8812458}.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR   EMBL; D78333; BAA11347.1; -; mRNA.
DR   EMBL; AK301773; BAG63232.1; -; mRNA.
DR   EMBL; AK302344; BAG63672.1; -; mRNA.
DR   EMBL; AC022903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC026125; AAH26125.1; -; mRNA.
DR   EMBL; BC027591; AAH27591.1; -; mRNA.
DR   CCDS; CCDS32617.1; -. [Q92526-1]
DR   CCDS; CCDS54105.1; -. [Q92526-2]
DR   CCDS; CCDS54106.1; -. [Q92526-3]
DR   RefSeq; NP_001180458.1; NM_001193529.2. [Q92526-3]
DR   RefSeq; NP_001180459.1; NM_001193530.1. [Q92526-2]
DR   RefSeq; NP_006575.2; NM_006584.3. [Q92526-1]
DR   AlphaFoldDB; Q92526; -.
DR   SMR; Q92526; -.
DR   BioGRID; 115932; 224.
DR   DIP; DIP-53269N; -.
DR   IntAct; Q92526; 71.
DR   STRING; 9606.ENSP00000327191; -.
DR   GlyGen; Q92526; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q92526; -.
DR   PhosphoSitePlus; Q92526; -.
DR   SwissPalm; Q92526; -.
DR   BioMuta; CCT6B; -.
DR   DMDM; 327478610; -.
DR   REPRODUCTION-2DPAGE; IPI00220656; -.
DR   jPOST; Q92526; -.
DR   MassIVE; Q92526; -.
DR   PaxDb; 9606-ENSP00000327191; -.
DR   PeptideAtlas; Q92526; -.
DR   ProteomicsDB; 5399; -.
DR   ProteomicsDB; 75285; -. [Q92526-1]
DR   ProteomicsDB; 75286; -. [Q92526-2]
DR   Pumba; Q92526; -.
DR   Antibodypedia; 27366; 136 antibodies from 24 providers.
DR   DNASU; 10693; -.
DR   Ensembl; ENST00000314144.10; ENSP00000327191.5; ENSG00000132141.14. [Q92526-1]
DR   Ensembl; ENST00000421975.7; ENSP00000398044.3; ENSG00000132141.14. [Q92526-3]
DR   Ensembl; ENST00000436961.7; ENSP00000400917.3; ENSG00000132141.14. [Q92526-2]
DR   GeneID; 10693; -.
DR   KEGG; hsa:10693; -.
DR   MANE-Select; ENST00000314144.10; ENSP00000327191.5; NM_006584.4; NP_006575.2.
DR   UCSC; uc002hig.4; human. [Q92526-1]
DR   AGR; HGNC:1621; -.
DR   CTD; 10693; -.
DR   DisGeNET; 10693; -.
DR   GeneCards; CCT6B; -.
DR   HGNC; HGNC:1621; CCT6B.
DR   HPA; ENSG00000132141; Tissue enriched (testis).
DR   MIM; 610730; gene.
DR   neXtProt; NX_Q92526; -.
DR   OpenTargets; ENSG00000132141; -.
DR   PharmGKB; PA26184; -.
DR   VEuPathDB; HostDB:ENSG00000132141; -.
DR   eggNOG; KOG0359; Eukaryota.
DR   GeneTree; ENSGT00940000156339; -.
DR   HOGENOM; CLU_008891_3_1_1; -.
DR   InParanoid; Q92526; -.
DR   OMA; KHTILQI; -.
DR   OrthoDB; 1058698at2759; -.
DR   PhylomeDB; Q92526; -.
DR   TreeFam; TF106333; -.
DR   PathwayCommons; Q92526; -.
DR   Reactome; R-HSA-389957; Prefoldin mediated transfer of substrate to CCT/TriC.
DR   Reactome; R-HSA-389960; Formation of tubulin folding intermediates by CCT/TriC.
DR   Reactome; R-HSA-390450; Folding of actin by CCT/TriC.
DR   Reactome; R-HSA-390471; Association of TriC/CCT with target proteins during biosynthesis.
DR   Reactome; R-HSA-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR   SignaLink; Q92526; -.
DR   BioGRID-ORCS; 10693; 15 hits in 1157 CRISPR screens.
DR   ChiTaRS; CCT6B; human.
DR   GenomeRNAi; 10693; -.
DR   Pharos; Q92526; Tbio.
DR   PRO; PR:Q92526; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q92526; Protein.
DR   Bgee; ENSG00000132141; Expressed in sperm and 129 other cell types or tissues.
DR   ExpressionAtlas; Q92526; baseline and differential.
DR   GO; GO:0005832; C:chaperonin-containing T-complex; IDA:FlyBase.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
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; IDA:FlyBase.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IDA:FlyBase.
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   InterPro; IPR053374; TCP-1_chaperonin.
DR   NCBIfam; TIGR02347; chap_CCT_zeta; 1.
DR   NCBIfam; NF041083; thermosome_beta; 1.
DR   PANTHER; PTHR11353; CHAPERONIN; 1.
DR   PANTHER; PTHR11353:SF58; T-COMPLEX PROTEIN 1 SUBUNIT ZETA-2; 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.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Chaperone; Cytoplasm;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..530
FT                   /note="T-complex protein 1 subunit zeta-2"
FT                   /id="PRO_0000128363"
FT   VAR_SEQ         68..112
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_043040"
FT   VAR_SEQ         206..242
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_047129"
FT   VARIANT         17
FT                   /note="R -> Q (in dbSNP:rs9635769)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_060297"
FT   VARIANT         48
FT                   /note="V -> A (in dbSNP:rs2230552)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_060298"
FT   VARIANT         247
FT                   /note="G -> A (in dbSNP:rs2230553)"
FT                   /evidence="ECO:0000269|PubMed:8812458"
FT                   /id="VAR_057269"
FT   CONFLICT        18..30
FT                   /note="AALAVNICAARGL -> QLWLSIYAPPRV (in Ref. 1; BAA11347)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        86
FT                   /note="D -> G (in Ref. 1; BAA11347)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        94
FT                   /note="S -> T (in Ref. 1; BAA11347)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        176..178
FT                   /note="VLA -> LFP (in Ref. 1; BAA11347)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        183
FT                   /note="G -> P (in Ref. 1; BAA11347)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        529..530
FT                   /note="LK -> QMMIEFKINPSRR (in Ref. 1; BAA11347)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   530 AA;  57821 MW;  AE28A28E3826C196 CRC64;
     MAAIKAVNSK AEVARARAAL AVNICAARGL QDVLRTNLGP KGTMKMLVSG AGDIKLTKDG
     NVLLDEMQIQ HPTASLIAKV ATAQDDVTGD GTTSNVLIIG ELLKQADLYI SEGLHPRIIA
     EGFEAAKIKA LEVLEEVKVT KEMKRKILLD VARTSLQTKV HAELADVLTE VVVDSVLAVR
     RPGYPIDLFM VEIMEMKHKL GTDTKLIQGL VLDHGARHPD MKKRVEDAFI LICNVSLEYE
     KTEVNSGFFY KTAEEKEKLV KAERKFIEDR VQKIIDLKDK VCAQSNKGFV VINQKGIDPF
     SLDSLAKHGI VALRRAKRRN MERLSLACGG MAVNSFEDLT VDCLGHAGLV YEYTLGEEKF
     TFIEECVNPC SVTLLVKGPN KHTLTQVKDA IRDGLRAIKN AIEDGCMVPG AGAIEVAMAE
     ALVTYKNSIK GRARLGVQAF ADALLIIPKV LAQNAGYDPQ ETLVKVQAEH VESKQLVGVD
     LNTGEPMVAA DAGVWDNYCV KKQLLHSCTV IATNILLVDE IMRAGMSSLK
//