Full text data of CCT3
CCT3
(CCTG, TRIC5)
[Confidence: low (only semi-automatic identification from reviews)]
T-complex protein 1 subunit gamma; TCP-1-gamma (CCT-gamma; hTRiC5)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
T-complex protein 1 subunit gamma; TCP-1-gamma (CCT-gamma; hTRiC5)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P49368
ID TCPG_HUMAN Reviewed; 545 AA.
AC P49368; A6NE14; Q5SZY1; Q9BR64;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 24-MAY-2005, sequence version 4.
DT 22-JAN-2014, entry version 144.
DE RecName: Full=T-complex protein 1 subunit gamma;
DE Short=TCP-1-gamma;
DE AltName: Full=CCT-gamma;
DE AltName: Full=hTRiC5;
GN Name=CCT3; Synonyms=CCTG, TRIC5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Cerebellum;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 1-15; 32-38; 49-85; 129-138; 182-191; 238-248;
RP 295-306; 382-389; 428-449 AND 508-528, ACETYLATION AT MET-1, AND MASS
RP SPECTROMETRY.
RC TISSUE=Hepatoma;
RA Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.;
RL Submitted (JUL-2007) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-545.
RC TISSUE=Kidney;
RX PubMed=8573069;
RA Walkley N.A., Demaine A.G., Malik A.N.;
RT "Cloning, structure and mRNA expression of human Cctg, which encodes
RT the chaperonin subunit CCT gamma.";
RL Biochem. J. 313:381-389(1996).
RN [7]
RP PROTEIN SEQUENCE OF 204-216; 331-353 AND 508-518, AND MASS
RP SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Vishwanath V.;
RL Submitted (MAR-2007) to UniProtKB.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 345-544.
RX PubMed=8001976; DOI=10.1006/geno.1994.1438;
RA Sevigny G., Joly E., Bibor-Hardy V., Lemieux N.;
RT "Assignment of the human homologue of the mTRiC-P5 gene (TRIC5) to
RT band 1q23 by fluorescence in situ hybridization.";
RL Genomics 22:634-636(1994).
RN [9]
RP INTERACTION WITH PACRG.
RX PubMed=14532270; DOI=10.1074/jbc.M309655200;
RA Imai Y., Soda M., Murakami T., Shoji M., Abe K., Takahashi R.;
RT "A product of the human gene adjacent to parkin is a component of Lewy
RT bodies and suppresses Pael receptor-induced cell death.";
RL J. Biol. Chem. 278:51901-51910(2003).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-222, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP FUNCTION, AND IDENTIFICATION IN BBS/CCT COMPLEX.
RX PubMed=20080638; DOI=10.1073/pnas.0910268107;
RA Seo S., Baye L.M., Schulz N.P., Beck J.S., Zhang Q., Slusarski D.C.,
RA Sheffield V.C.;
RT "BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family
RT chaperonins and mediate BBSome assembly.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:1488-1493(2010).
RN [14]
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Molecular chaperone; assists the folding of proteins
CC upon ATP hydrolysis. As part of the BBS/CCT complex may play a
CC role in the assembly of BBSome, a complex involved in ciliogenesis
CC regulating transports vesicles to the cilia. Known to play a role,
CC in vitro, in the folding of actin and tubulin.
CC -!- SUBUNIT: Heterooligomeric complex of about 850 to 900 kDa that
CC forms two stacked rings, 12 to 16 nm in diameter. Interacts with
CC PACRG. Component of the BBS/CCT complex composed at least of MKKS,
CC BBS10, BBS12, TCP1, CCT2, CCT3, CCT4, CCT5 AND CCT8.
CC -!- INTERACTION:
CC P04049:RAF1; NbExp=3; IntAct=EBI-356673, EBI-365996;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P49368-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P49368-2; Sequence=VSP_042026;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH08019.1; Type=Erroneous initiation;
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DR EMBL; AK293477; BAG56968.1; -; mRNA.
DR EMBL; AL833197; CAI46192.1; -; mRNA.
DR EMBL; AL589685; CAI14167.1; -; Genomic_DNA.
DR EMBL; BC006501; AAH06501.3; -; mRNA.
DR EMBL; BC008019; AAH08019.1; ALT_INIT; mRNA.
DR EMBL; X74801; CAA52808.1; -; mRNA.
DR EMBL; U17104; AAC50068.1; -; mRNA.
DR PIR; S61529; A38983.
DR RefSeq; NP_001008800.1; NM_001008800.2.
DR RefSeq; NP_005989.3; NM_005998.4.
DR UniGene; Hs.491494; -.
DR ProteinModelPortal; P49368; -.
DR SMR; P49368; 7-526.
DR DIP; DIP-32970N; -.
DR IntAct; P49368; 60.
DR MINT; MINT-260598; -.
DR STRING; 9606.ENSP00000357244; -.
DR PhosphoSite; P49368; -.
DR DMDM; 66774185; -.
DR DOSAC-COBS-2DPAGE; P49368; -.
DR OGP; P49368; -.
DR SWISS-2DPAGE; P49368; -.
DR PaxDb; P49368; -.
DR PRIDE; P49368; -.
DR DNASU; 7203; -.
DR Ensembl; ENST00000295688; ENSP00000295688; ENSG00000163468.
DR Ensembl; ENST00000368259; ENSP00000357242; ENSG00000163468.
DR GeneID; 7203; -.
DR KEGG; hsa:7203; -.
DR UCSC; uc001fol.2; human.
DR CTD; 7203; -.
DR GeneCards; GC01M156278; -.
DR HGNC; HGNC:1616; CCT3.
DR HPA; HPA006543; -.
DR MIM; 600114; gene.
DR neXtProt; NX_P49368; -.
DR PharmGKB; PA26180; -.
DR eggNOG; COG0459; -.
DR HOGENOM; HOG000226732; -.
DR HOVERGEN; HBG104982; -.
DR InParanoid; P49368; -.
DR KO; K09495; -.
DR OMA; GEIEDSR; -.
DR OrthoDB; EOG7DJSKS; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR ChiTaRS; CCT3; human.
DR GeneWiki; CCT3; -.
DR GenomeRNAi; 7203; -.
DR NextBio; 28226; -.
DR PRO; PR:P49368; -.
DR ArrayExpress; P49368; -.
DR Bgee; P49368; -.
DR CleanEx; HS_CCT3; -.
DR Genevestigator; P49368; -.
DR GO; GO:0005832; C:chaperonin-containing T-complex; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0002199; C:zona pellucida receptor complex; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; TAS:ProtInc.
DR GO; GO:0051084; P:'de novo' posttranslational protein folding; TAS:Reactome.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IEA:Ensembl.
DR Gene3D; 1.10.560.10; -; 2.
DR Gene3D; 3.30.260.10; -; 2.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR012719; Chap_CCT_gamma.
DR InterPro; IPR017998; Chaperone_TCP-1.
DR InterPro; IPR002194; Chaperonin_TCP-1_CS.
DR InterPro; IPR002423; Cpn60/TCP-1.
DR InterPro; IPR027409; GroEL-like_apical_dom.
DR InterPro; IPR027413; GROEL-like_equatorial.
DR InterPro; IPR027410; TCP-1-like_intermed.
DR PANTHER; PTHR11353; PTHR11353; 1.
DR PANTHER; PTHR11353:SF24; PTHR11353:SF24; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00304; TCOMPLEXTCP1.
DR SUPFAM; SSF48592; SSF48592; 2.
DR SUPFAM; SSF52029; SSF52029; 1.
DR TIGRFAMs; TIGR02344; chap_CCT_gamma; 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; Alternative splicing; ATP-binding; Chaperone;
KW Complete proteome; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Nucleotide-binding; Phosphoprotein; Polymorphism;
KW Reference proteome.
FT CHAIN 1 545 T-complex protein 1 subunit gamma.
FT /FTId=PRO_0000128321.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 222 222 N6-acetyllysine.
FT MOD_RES 244 244 Phosphoserine.
FT MOD_RES 252 252 Phosphoserine.
FT DISULFID 366 372 By similarity.
FT VAR_SEQ 32 69 Missing (in isoform 2).
FT /FTId=VSP_042026.
FT VARIANT 391 391 L -> F (in dbSNP:rs2230194).
FT /FTId=VAR_052265.
FT CONFLICT 251 251 E -> G (in Ref. 6; CAA52808).
FT CONFLICT 345 345 T -> A (in Ref. 8; AAC50068).
SQ SEQUENCE 545 AA; 60534 MW; 0A528762EF24F36B CRC64;
MMGHRPVLVL SQNTKRESGR KVQSGNINAA KTIADIIRTC LGPKSMMKML LDPMGGIVMT
NDGNAILREI QVQHPAAKSM IEISRTQDEE VGDGTTSVII LAGEMLSVAE HFLEQQMHPT
VVISAYRKAL DDMISTLKKI SIPVDISDSD MMLNIINSSI TTKAISRWSS LACNIALDAV
KMVQFEENGR KEIDIKKYAR VEKIPGGIIE DSCVLRGVMI NKDVTHPRMR RYIKNPRIVL
LDSSLEYKKG ESQTDIEITR EEDFTRILQM EEEYIQQLCE DIIQLKPDVV ITEKGISDLA
QHYLMRANIT AIRRVRKTDN NRIARACGAR IVSRPEELRE DDVGTGAGLL EIKKIGDEYF
TFITDCKDPK ACTILLRGAS KEILSEVERN LQDAMQVCRN VLLDPQLVPG GGASEMAVAH
ALTEKSKAMT GVEQWPYRAV AQALEVIPRT LIQNCGASTI RLLTSLRAKH TQENCETWGV
NGETGTLVDM KELGIWEPLA VKLQTYKTAV ETAVLLLRID DIVSGHKKKG DDQSRQGGAP
DAGQE
//
ID TCPG_HUMAN Reviewed; 545 AA.
AC P49368; A6NE14; Q5SZY1; Q9BR64;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 24-MAY-2005, sequence version 4.
DT 22-JAN-2014, entry version 144.
DE RecName: Full=T-complex protein 1 subunit gamma;
DE Short=TCP-1-gamma;
DE AltName: Full=CCT-gamma;
DE AltName: Full=hTRiC5;
GN Name=CCT3; Synonyms=CCTG, TRIC5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Cerebellum;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 1-15; 32-38; 49-85; 129-138; 182-191; 238-248;
RP 295-306; 382-389; 428-449 AND 508-528, ACETYLATION AT MET-1, AND MASS
RP SPECTROMETRY.
RC TISSUE=Hepatoma;
RA Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.;
RL Submitted (JUL-2007) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-545.
RC TISSUE=Kidney;
RX PubMed=8573069;
RA Walkley N.A., Demaine A.G., Malik A.N.;
RT "Cloning, structure and mRNA expression of human Cctg, which encodes
RT the chaperonin subunit CCT gamma.";
RL Biochem. J. 313:381-389(1996).
RN [7]
RP PROTEIN SEQUENCE OF 204-216; 331-353 AND 508-518, AND MASS
RP SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Vishwanath V.;
RL Submitted (MAR-2007) to UniProtKB.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 345-544.
RX PubMed=8001976; DOI=10.1006/geno.1994.1438;
RA Sevigny G., Joly E., Bibor-Hardy V., Lemieux N.;
RT "Assignment of the human homologue of the mTRiC-P5 gene (TRIC5) to
RT band 1q23 by fluorescence in situ hybridization.";
RL Genomics 22:634-636(1994).
RN [9]
RP INTERACTION WITH PACRG.
RX PubMed=14532270; DOI=10.1074/jbc.M309655200;
RA Imai Y., Soda M., Murakami T., Shoji M., Abe K., Takahashi R.;
RT "A product of the human gene adjacent to parkin is a component of Lewy
RT bodies and suppresses Pael receptor-induced cell death.";
RL J. Biol. Chem. 278:51901-51910(2003).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-222, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP FUNCTION, AND IDENTIFICATION IN BBS/CCT COMPLEX.
RX PubMed=20080638; DOI=10.1073/pnas.0910268107;
RA Seo S., Baye L.M., Schulz N.P., Beck J.S., Zhang Q., Slusarski D.C.,
RA Sheffield V.C.;
RT "BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family
RT chaperonins and mediate BBSome assembly.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:1488-1493(2010).
RN [14]
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Molecular chaperone; assists the folding of proteins
CC upon ATP hydrolysis. As part of the BBS/CCT complex may play a
CC role in the assembly of BBSome, a complex involved in ciliogenesis
CC regulating transports vesicles to the cilia. Known to play a role,
CC in vitro, in the folding of actin and tubulin.
CC -!- SUBUNIT: Heterooligomeric complex of about 850 to 900 kDa that
CC forms two stacked rings, 12 to 16 nm in diameter. Interacts with
CC PACRG. Component of the BBS/CCT complex composed at least of MKKS,
CC BBS10, BBS12, TCP1, CCT2, CCT3, CCT4, CCT5 AND CCT8.
CC -!- INTERACTION:
CC P04049:RAF1; NbExp=3; IntAct=EBI-356673, EBI-365996;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P49368-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P49368-2; Sequence=VSP_042026;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH08019.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
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DR EMBL; AK293477; BAG56968.1; -; mRNA.
DR EMBL; AL833197; CAI46192.1; -; mRNA.
DR EMBL; AL589685; CAI14167.1; -; Genomic_DNA.
DR EMBL; BC006501; AAH06501.3; -; mRNA.
DR EMBL; BC008019; AAH08019.1; ALT_INIT; mRNA.
DR EMBL; X74801; CAA52808.1; -; mRNA.
DR EMBL; U17104; AAC50068.1; -; mRNA.
DR PIR; S61529; A38983.
DR RefSeq; NP_001008800.1; NM_001008800.2.
DR RefSeq; NP_005989.3; NM_005998.4.
DR UniGene; Hs.491494; -.
DR ProteinModelPortal; P49368; -.
DR SMR; P49368; 7-526.
DR DIP; DIP-32970N; -.
DR IntAct; P49368; 60.
DR MINT; MINT-260598; -.
DR STRING; 9606.ENSP00000357244; -.
DR PhosphoSite; P49368; -.
DR DMDM; 66774185; -.
DR DOSAC-COBS-2DPAGE; P49368; -.
DR OGP; P49368; -.
DR SWISS-2DPAGE; P49368; -.
DR PaxDb; P49368; -.
DR PRIDE; P49368; -.
DR DNASU; 7203; -.
DR Ensembl; ENST00000295688; ENSP00000295688; ENSG00000163468.
DR Ensembl; ENST00000368259; ENSP00000357242; ENSG00000163468.
DR GeneID; 7203; -.
DR KEGG; hsa:7203; -.
DR UCSC; uc001fol.2; human.
DR CTD; 7203; -.
DR GeneCards; GC01M156278; -.
DR HGNC; HGNC:1616; CCT3.
DR HPA; HPA006543; -.
DR MIM; 600114; gene.
DR neXtProt; NX_P49368; -.
DR PharmGKB; PA26180; -.
DR eggNOG; COG0459; -.
DR HOGENOM; HOG000226732; -.
DR HOVERGEN; HBG104982; -.
DR InParanoid; P49368; -.
DR KO; K09495; -.
DR OMA; GEIEDSR; -.
DR OrthoDB; EOG7DJSKS; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR ChiTaRS; CCT3; human.
DR GeneWiki; CCT3; -.
DR GenomeRNAi; 7203; -.
DR NextBio; 28226; -.
DR PRO; PR:P49368; -.
DR ArrayExpress; P49368; -.
DR Bgee; P49368; -.
DR CleanEx; HS_CCT3; -.
DR Genevestigator; P49368; -.
DR GO; GO:0005832; C:chaperonin-containing T-complex; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0002199; C:zona pellucida receptor complex; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; TAS:ProtInc.
DR GO; GO:0051084; P:'de novo' posttranslational protein folding; TAS:Reactome.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IEA:Ensembl.
DR Gene3D; 1.10.560.10; -; 2.
DR Gene3D; 3.30.260.10; -; 2.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR012719; Chap_CCT_gamma.
DR InterPro; IPR017998; Chaperone_TCP-1.
DR InterPro; IPR002194; Chaperonin_TCP-1_CS.
DR InterPro; IPR002423; Cpn60/TCP-1.
DR InterPro; IPR027409; GroEL-like_apical_dom.
DR InterPro; IPR027413; GROEL-like_equatorial.
DR InterPro; IPR027410; TCP-1-like_intermed.
DR PANTHER; PTHR11353; PTHR11353; 1.
DR PANTHER; PTHR11353:SF24; PTHR11353:SF24; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00304; TCOMPLEXTCP1.
DR SUPFAM; SSF48592; SSF48592; 2.
DR SUPFAM; SSF52029; SSF52029; 1.
DR TIGRFAMs; TIGR02344; chap_CCT_gamma; 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; Alternative splicing; ATP-binding; Chaperone;
KW Complete proteome; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Nucleotide-binding; Phosphoprotein; Polymorphism;
KW Reference proteome.
FT CHAIN 1 545 T-complex protein 1 subunit gamma.
FT /FTId=PRO_0000128321.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 222 222 N6-acetyllysine.
FT MOD_RES 244 244 Phosphoserine.
FT MOD_RES 252 252 Phosphoserine.
FT DISULFID 366 372 By similarity.
FT VAR_SEQ 32 69 Missing (in isoform 2).
FT /FTId=VSP_042026.
FT VARIANT 391 391 L -> F (in dbSNP:rs2230194).
FT /FTId=VAR_052265.
FT CONFLICT 251 251 E -> G (in Ref. 6; CAA52808).
FT CONFLICT 345 345 T -> A (in Ref. 8; AAC50068).
SQ SEQUENCE 545 AA; 60534 MW; 0A528762EF24F36B CRC64;
MMGHRPVLVL SQNTKRESGR KVQSGNINAA KTIADIIRTC LGPKSMMKML LDPMGGIVMT
NDGNAILREI QVQHPAAKSM IEISRTQDEE VGDGTTSVII LAGEMLSVAE HFLEQQMHPT
VVISAYRKAL DDMISTLKKI SIPVDISDSD MMLNIINSSI TTKAISRWSS LACNIALDAV
KMVQFEENGR KEIDIKKYAR VEKIPGGIIE DSCVLRGVMI NKDVTHPRMR RYIKNPRIVL
LDSSLEYKKG ESQTDIEITR EEDFTRILQM EEEYIQQLCE DIIQLKPDVV ITEKGISDLA
QHYLMRANIT AIRRVRKTDN NRIARACGAR IVSRPEELRE DDVGTGAGLL EIKKIGDEYF
TFITDCKDPK ACTILLRGAS KEILSEVERN LQDAMQVCRN VLLDPQLVPG GGASEMAVAH
ALTEKSKAMT GVEQWPYRAV AQALEVIPRT LIQNCGASTI RLLTSLRAKH TQENCETWGV
NGETGTLVDM KELGIWEPLA VKLQTYKTAV ETAVLLLRID DIVSGHKKKG DDQSRQGGAP
DAGQE
//
MIM
600114
*RECORD*
*FIELD* NO
600114
*FIELD* TI
*600114 CHAPERONIN CONTAINING T-COMPLEX POLYPEPTIDE 1, SUBUNIT 3; CCT3
;;CHAPERONIN CONTAINING TCP1, SUBUNIT 3;;
read moreCCT-GAMMA; CCTG;;
TCP1 RING COMPLEX, POLYPEPTIDE 5; TRIC5
*FIELD* TX
DESCRIPTION
Molecular chaperones are proteins capable of folding or assembling
nascent proteins in a higher order structure. A molecular chaperone
called TCP1 ring complex (TRiC) plays a role in actin and tubulin
folding. TRiC is composed of 2 heteromeric subunits of 6 to 9 different
proteins. The cytoplasmic T-complex protein-1 (TCP1; 186980), an
abundant testicular germ cell protein, has been found in this complex.
Other components of TRiC, such as TRIC5, are TCP1-related proteins
(Sevigny et al., 1994).
CLONING
Joly et al. (1994) cloned a mouse cDNA corresponding to tryptic
fragments of the bovine TRiCP5 subunit described by Frydman et al.
(1992). The mouse TRiCP5 shares 48% nucleotide and 34% amino acid
homology with mouse Tcp1. It is a cytosolic protein also found in the
nuclear matrix of several cultured human cell lines. Furthermore, like
TCP1, it is highly expressed in testis.
Sevigny et al. (1994) cloned a partial human cDNA clone homologous to
mouse TRiCP5.
Walkley et al. (1996) cloned the human cDNA from a kidney library. The
1.9-kb cDNA encodes a predicted 544-amino acid protein that is 98%
similar to the mouse sequence and 75% similar to the yeast gene. The
mRNA is expressed in a variety of human tissues and at high levels in
mouse testis.
Sevigny et al. (1996) cloned the gene coding for the mouse P5 subunit.
GENE FUNCTION
Feldman et al. (1999) demonstrated that the folding and assembly of the
VHL protein (608537) into a complex with its partner proteins, elongin B
(600787) and elongin C (600788), is directly mediated by the chaperonin
TRiC. Their results defined a novel role for TRiC in mediating
oligomerization.
GENE STRUCTURE
Sevigny et al. (1996) determined that the mouse Tric5 gene contains 14
exons distributed within 25 kb of genomic DNA. Sevigny et al. (1996)
used primer extension to demonstrate multiple transcription start points
for the Tric5 gene. This was considered consistent with the lack of any
obvious TATA box upstream of the transcription start points.
MAPPING
Sevigny et al. (1994) mapped the TRIC5 gene to chromosome 1q23 by
fluorescence in situ hybridization. The fact that the human TRIC5 gene
is not on chromosome 6 like other TCP1-related proteins implied to
Sevigny et al. (1994) that the genes coding the TCP1-related proteins
present in the TCP1 ring complex are probably not organized in a cluster
and thus are not synchronously regulated by a cis-acting control region
such as the LCR involved in the regulation of globin synthesis.
Sevigny et al. (1996) showed that the mouse genome contains 1 Tric5 gene
and 1 Tric5 pseudogene located on chromosomes 3F and 5B, respectively.
*FIELD* RF
1. Feldman, D. E.; Thulasiraman, V.; Ferreyra, R. G.; Frydman, J.
: Formation of the VHL-elongin BC tumor suppressor complex is mediated
by the chaperonin TRiC. Molec. Cell 4: 1051-1061, 1999.
2. Frydman, J.; Nimmesgern, E.; Erdjument-Bromage, H.; Wall, J. S.;
Tempst, P.; Hartl, F.-U.: Function in protein folding of TRiC, a
cytosolic ring complex containing TCP-1 and structurally related subunits. EMBO
J. 11: 4767-4778, 1992.
3. Joly, E. C.; Sevigny, G.; Todorov, I. T.; Bibor-Hardy, V.: cDNA
encoding a novel TCP1-related protein. Biochim. Biophys. Acta 1217:
224-226, 1994.
4. Sevigny, G.; Joly, E. C.; Bibor-Hardy, V.; Lemieux, N.: Assignment
of the human homologue of the mTRiC-P5 gene (TRIC5) to band 1q23 by
fluorescence in situ hybridization. Genomics 22: 634-636, 1994.
5. Sevigny, G.; Lemieux, N.; Steyaert, A.; Bibor-Hardy, V.: Structure
of the gene coding for the mouse TRiC-P5 subunit of the cytosolic
chaperonin TRiC. Genomics 31: 107-110, 1996.
6. Walkley, N. A.; Demaine, A. G.; Malik, A. N.: Cloning, structure
and mRNA expression of human Cctg, which encodes the chaperonin subunit
CCT-gamma. Biochem. J. 313: 381-389, 1996.
*FIELD* CN
Stylianos E. Antonarakis - updated: 1/7/2000
Alan F. Scott - updated: 5/20/1996
*FIELD* CD
Victor A. McKusick: 9/14/1994
*FIELD* ED
mgross: 11/21/2006
mgross: 11/20/2006
ckniffin: 3/23/2004
tkritzer: 9/17/2003
mgross: 7/14/2000
mgross: 7/13/2000
mgross: 1/7/2000
alopez: 7/27/1999
alopez: 7/26/1999
mark: 5/20/1996
terry: 5/20/1996
mark: 2/7/1996
terry: 2/2/1996
carol: 9/14/1994
*RECORD*
*FIELD* NO
600114
*FIELD* TI
*600114 CHAPERONIN CONTAINING T-COMPLEX POLYPEPTIDE 1, SUBUNIT 3; CCT3
;;CHAPERONIN CONTAINING TCP1, SUBUNIT 3;;
read moreCCT-GAMMA; CCTG;;
TCP1 RING COMPLEX, POLYPEPTIDE 5; TRIC5
*FIELD* TX
DESCRIPTION
Molecular chaperones are proteins capable of folding or assembling
nascent proteins in a higher order structure. A molecular chaperone
called TCP1 ring complex (TRiC) plays a role in actin and tubulin
folding. TRiC is composed of 2 heteromeric subunits of 6 to 9 different
proteins. The cytoplasmic T-complex protein-1 (TCP1; 186980), an
abundant testicular germ cell protein, has been found in this complex.
Other components of TRiC, such as TRIC5, are TCP1-related proteins
(Sevigny et al., 1994).
CLONING
Joly et al. (1994) cloned a mouse cDNA corresponding to tryptic
fragments of the bovine TRiCP5 subunit described by Frydman et al.
(1992). The mouse TRiCP5 shares 48% nucleotide and 34% amino acid
homology with mouse Tcp1. It is a cytosolic protein also found in the
nuclear matrix of several cultured human cell lines. Furthermore, like
TCP1, it is highly expressed in testis.
Sevigny et al. (1994) cloned a partial human cDNA clone homologous to
mouse TRiCP5.
Walkley et al. (1996) cloned the human cDNA from a kidney library. The
1.9-kb cDNA encodes a predicted 544-amino acid protein that is 98%
similar to the mouse sequence and 75% similar to the yeast gene. The
mRNA is expressed in a variety of human tissues and at high levels in
mouse testis.
Sevigny et al. (1996) cloned the gene coding for the mouse P5 subunit.
GENE FUNCTION
Feldman et al. (1999) demonstrated that the folding and assembly of the
VHL protein (608537) into a complex with its partner proteins, elongin B
(600787) and elongin C (600788), is directly mediated by the chaperonin
TRiC. Their results defined a novel role for TRiC in mediating
oligomerization.
GENE STRUCTURE
Sevigny et al. (1996) determined that the mouse Tric5 gene contains 14
exons distributed within 25 kb of genomic DNA. Sevigny et al. (1996)
used primer extension to demonstrate multiple transcription start points
for the Tric5 gene. This was considered consistent with the lack of any
obvious TATA box upstream of the transcription start points.
MAPPING
Sevigny et al. (1994) mapped the TRIC5 gene to chromosome 1q23 by
fluorescence in situ hybridization. The fact that the human TRIC5 gene
is not on chromosome 6 like other TCP1-related proteins implied to
Sevigny et al. (1994) that the genes coding the TCP1-related proteins
present in the TCP1 ring complex are probably not organized in a cluster
and thus are not synchronously regulated by a cis-acting control region
such as the LCR involved in the regulation of globin synthesis.
Sevigny et al. (1996) showed that the mouse genome contains 1 Tric5 gene
and 1 Tric5 pseudogene located on chromosomes 3F and 5B, respectively.
*FIELD* RF
1. Feldman, D. E.; Thulasiraman, V.; Ferreyra, R. G.; Frydman, J.
: Formation of the VHL-elongin BC tumor suppressor complex is mediated
by the chaperonin TRiC. Molec. Cell 4: 1051-1061, 1999.
2. Frydman, J.; Nimmesgern, E.; Erdjument-Bromage, H.; Wall, J. S.;
Tempst, P.; Hartl, F.-U.: Function in protein folding of TRiC, a
cytosolic ring complex containing TCP-1 and structurally related subunits. EMBO
J. 11: 4767-4778, 1992.
3. Joly, E. C.; Sevigny, G.; Todorov, I. T.; Bibor-Hardy, V.: cDNA
encoding a novel TCP1-related protein. Biochim. Biophys. Acta 1217:
224-226, 1994.
4. Sevigny, G.; Joly, E. C.; Bibor-Hardy, V.; Lemieux, N.: Assignment
of the human homologue of the mTRiC-P5 gene (TRIC5) to band 1q23 by
fluorescence in situ hybridization. Genomics 22: 634-636, 1994.
5. Sevigny, G.; Lemieux, N.; Steyaert, A.; Bibor-Hardy, V.: Structure
of the gene coding for the mouse TRiC-P5 subunit of the cytosolic
chaperonin TRiC. Genomics 31: 107-110, 1996.
6. Walkley, N. A.; Demaine, A. G.; Malik, A. N.: Cloning, structure
and mRNA expression of human Cctg, which encodes the chaperonin subunit
CCT-gamma. Biochem. J. 313: 381-389, 1996.
*FIELD* CN
Stylianos E. Antonarakis - updated: 1/7/2000
Alan F. Scott - updated: 5/20/1996
*FIELD* CD
Victor A. McKusick: 9/14/1994
*FIELD* ED
mgross: 11/21/2006
mgross: 11/20/2006
ckniffin: 3/23/2004
tkritzer: 9/17/2003
mgross: 7/14/2000
mgross: 7/13/2000
mgross: 1/7/2000
alopez: 7/27/1999
alopez: 7/26/1999
mark: 5/20/1996
terry: 5/20/1996
mark: 2/7/1996
terry: 2/2/1996
carol: 9/14/1994