Full text data of PFDN5
PFDN5
(MM1, PFD5)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Prefoldin subunit 5 (C-Myc-binding protein Mm-1; Myc modulator 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Prefoldin subunit 5 (C-Myc-binding protein Mm-1; Myc modulator 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q99471
ID PFD5_HUMAN Reviewed; 154 AA.
AC Q99471; A8K9A8; Q54AA8; Q9C083; Q9C084;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-JAN-2001, sequence version 2.
DT 22-JAN-2014, entry version 123.
DE RecName: Full=Prefoldin subunit 5;
DE AltName: Full=C-Myc-binding protein Mm-1;
DE AltName: Full=Myc modulator 1;
GN Name=PFDN5; Synonyms=MM1, PFD5;
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 [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9792694; DOI=10.1074/jbc.273.45.29794;
RA Mori K., Maeda Y., Kitaura H., Taira T., Iguchi-Ariga S.M., Ariga H.;
RT "MM-1, a novel c-Myc-associating protein that represses
RT transcriptional activity of c-Myc.";
RL J. Biol. Chem. 273:29794-29800(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RC TISSUE=Blood, and Fibroblast;
RX PubMed=11567024; DOI=10.1074/jbc.M106127200;
RA Fujioka Y., Taira T., Maeda Y., Tanaka S., Nishihara H.,
RA Iguchi-Ariga S.M.M., Nagashima K., Ariga H.;
RT "MM-1, a c-Myc-binding protein, is a candidate for a tumor suppressor
RT in leukemia/lymphoma and tongue cancer.";
RL J. Biol. Chem. 276:45137-45144(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), SUBCELLULAR LOCATION,
RP AND ALTERNATIVE SPLICING.
RC TISSUE=B-cell, and Placenta;
RX PubMed=16173081; DOI=10.1002/jcb.20619;
RA Hagio Y., Kimura Y., Taira T., Fujioka Y., Iguchi-Ariga S.M.M.,
RA Ariga H.;
RT "Distinct localizations and repression activities of MM-1 isoforms
RT toward c-Myc.";
RL J. Cell. Biochem. 97:145-155(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Thymus;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [9]
RP FUNCTION.
RX PubMed=9630229; DOI=10.1016/S0092-8674(00)81446-4;
RA Vainberg I.E., Lewis S.A., Rommelaere H., Ampe C., Vandekerckhove J.,
RA Klein H.L., Cowan N.J.;
RT "Prefoldin, a chaperone that delivers unfolded proteins to cytosolic
RT chaperonin.";
RL Cell 93:863-873(1998).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-42, 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 [12]
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).
CC -!- FUNCTION: Binds specifically to cytosolic chaperonin (c-CPN) and
CC transfers target proteins to it. Binds to nascent polypeptide
CC chain and promotes folding in an environment in which there are
CC many competing pathways for nonnative proteins. Represses the
CC transcriptional activity of MYC.
CC -!- SUBUNIT: Heterohexamer of two PFD-alpha type and four PFD-beta
CC type subunits. Binds to MYC; interacts with its N-terminal domain.
CC -!- INTERACTION:
CC Q9DUN1:vIRF-3 (xeno); NbExp=8; IntAct=EBI-357275, EBI-1647907;
CC -!- SUBCELLULAR LOCATION: Isoform 1: Nucleus.
CC -!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm.
CC -!- SUBCELLULAR LOCATION: Isoform 3: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist;
CC Name=1; Synonyms=MM1-alpha;
CC IsoId=Q99471-1; Sequence=Displayed;
CC Name=2; Synonyms=MM1-beta;
CC IsoId=Q99471-2; Sequence=VSP_043104;
CC Note=Does not repress transcription activity of MYC;
CC Name=3; Synonyms=MM1-gamma;
CC IsoId=Q99471-3; Sequence=VSP_043103;
CC -!- TISSUE SPECIFICITY: Highly expressed in pancreas and skeletal
CC muscle and moderately in other tissues.
CC -!- SIMILARITY: Belongs to the prefoldin subunit alpha family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA14006.1; Type=Erroneous initiation;
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DR EMBL; D89667; BAA14006.1; ALT_INIT; mRNA.
DR EMBL; AB055802; BAB32643.1; -; Genomic_DNA.
DR EMBL; AB055803; BAB32644.1; -; mRNA.
DR EMBL; AB055804; BAB32645.1; -; mRNA.
DR EMBL; AB055805; BAB32646.1; -; mRNA.
DR EMBL; BT007195; AAP35859.1; -; mRNA.
DR EMBL; AK292623; BAF85312.1; -; mRNA.
DR EMBL; AC073611; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW96683.1; -; Genomic_DNA.
DR EMBL; CH471054; EAW96685.1; -; Genomic_DNA.
DR EMBL; BC003373; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC062671; AAH62671.1; -; mRNA.
DR RefSeq; NP_002615.2; NM_002624.3.
DR RefSeq; NP_665904.1; NM_145897.2.
DR UniGene; Hs.655327; -.
DR ProteinModelPortal; Q99471; -.
DR SMR; Q99471; 11-149.
DR DIP; DIP-28155N; -.
DR IntAct; Q99471; 14.
DR MINT; MINT-5003456; -.
DR STRING; 9606.ENSP00000334188; -.
DR PhosphoSite; Q99471; -.
DR DMDM; 12231038; -.
DR OGP; Q99471; -.
DR PaxDb; Q99471; -.
DR PeptideAtlas; Q99471; -.
DR PRIDE; Q99471; -.
DR DNASU; 5204; -.
DR Ensembl; ENST00000243040; ENSP00000243040; ENSG00000123349.
DR Ensembl; ENST00000334478; ENSP00000334188; ENSG00000123349.
DR Ensembl; ENST00000351500; ENSP00000266964; ENSG00000123349.
DR Ensembl; ENST00000551018; ENSP00000447942; ENSG00000123349.
DR GeneID; 5204; -.
DR KEGG; hsa:5204; -.
DR UCSC; uc001scl.3; human.
DR CTD; 5204; -.
DR GeneCards; GC12P053689; -.
DR HGNC; HGNC:8869; PFDN5.
DR HPA; HPA008587; -.
DR MIM; 604899; gene.
DR neXtProt; NX_Q99471; -.
DR PharmGKB; PA33210; -.
DR eggNOG; COG1730; -.
DR HOGENOM; HOG000207562; -.
DR HOVERGEN; HBG004539; -.
DR InParanoid; Q99471; -.
DR KO; K04797; -.
DR OMA; YYVKKTR; -.
DR PhylomeDB; Q99471; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR ChiTaRS; PFDN5; human.
DR GeneWiki; PFDN5; -.
DR GenomeRNAi; 5204; -.
DR NextBio; 20126; -.
DR PRO; PR:Q99471; -.
DR ArrayExpress; Q99471; -.
DR Bgee; Q99471; -.
DR CleanEx; HS_PFDN5; -.
DR Genevestigator; Q99471; -.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0016272; C:prefoldin complex; IEA:InterPro.
DR GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
DR GO; GO:0051084; P:'de novo' posttranslational protein folding; TAS:Reactome.
DR GO; GO:0090090; P:negative regulation of canonical Wnt receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; IMP:BHF-UCL.
DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR InterPro; IPR011599; PFD_alpha.
DR InterPro; IPR027236; PFDN5.
DR InterPro; IPR009053; Prefoldin.
DR InterPro; IPR004127; Prefoldin_subunit_alpha.
DR PANTHER; PTHR12674:SF0; PTHR12674:SF0; 1.
DR Pfam; PF02996; Prefoldin; 1.
DR SUPFAM; SSF46579; SSF46579; 1.
DR TIGRFAMs; TIGR00293; TIGR00293; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chaperone; Complete proteome;
KW Cytoplasm; Nucleus; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 154 Prefoldin subunit 5.
FT /FTId=PRO_0000153661.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 42 42 N6-acetyllysine.
FT VAR_SEQ 25 69 Missing (in isoform 3).
FT /FTId=VSP_043103.
FT VAR_SEQ 59 154 GKELLVPLTSSMYVPGKLHDVEHVLIDVGTGYYVEKTAEDA
FT KDFFKRKIDFLTKQMEKIQPALQEKHAMKQAVMEMMSQKIQ
FT QLTALGAAQATAKA -> DVCPWEAA (in isoform
FT 2).
FT /FTId=VSP_043104.
SQ SEQUENCE 154 AA; 17328 MW; 0DA1F3644548CB14 CRC64;
MAQSINITEL NLPQLEMLKN QLDQEVEFLS TSIAQLKVVQ TKYVEAKDCL NVLNKSNEGK
ELLVPLTSSM YVPGKLHDVE HVLIDVGTGY YVEKTAEDAK DFFKRKIDFL TKQMEKIQPA
LQEKHAMKQA VMEMMSQKIQ QLTALGAAQA TAKA
//
ID PFD5_HUMAN Reviewed; 154 AA.
AC Q99471; A8K9A8; Q54AA8; Q9C083; Q9C084;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-JAN-2001, sequence version 2.
DT 22-JAN-2014, entry version 123.
DE RecName: Full=Prefoldin subunit 5;
DE AltName: Full=C-Myc-binding protein Mm-1;
DE AltName: Full=Myc modulator 1;
GN Name=PFDN5; Synonyms=MM1, PFD5;
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 [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9792694; DOI=10.1074/jbc.273.45.29794;
RA Mori K., Maeda Y., Kitaura H., Taira T., Iguchi-Ariga S.M., Ariga H.;
RT "MM-1, a novel c-Myc-associating protein that represses
RT transcriptional activity of c-Myc.";
RL J. Biol. Chem. 273:29794-29800(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RC TISSUE=Blood, and Fibroblast;
RX PubMed=11567024; DOI=10.1074/jbc.M106127200;
RA Fujioka Y., Taira T., Maeda Y., Tanaka S., Nishihara H.,
RA Iguchi-Ariga S.M.M., Nagashima K., Ariga H.;
RT "MM-1, a c-Myc-binding protein, is a candidate for a tumor suppressor
RT in leukemia/lymphoma and tongue cancer.";
RL J. Biol. Chem. 276:45137-45144(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), SUBCELLULAR LOCATION,
RP AND ALTERNATIVE SPLICING.
RC TISSUE=B-cell, and Placenta;
RX PubMed=16173081; DOI=10.1002/jcb.20619;
RA Hagio Y., Kimura Y., Taira T., Fujioka Y., Iguchi-Ariga S.M.M.,
RA Ariga H.;
RT "Distinct localizations and repression activities of MM-1 isoforms
RT toward c-Myc.";
RL J. Cell. Biochem. 97:145-155(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Thymus;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [9]
RP FUNCTION.
RX PubMed=9630229; DOI=10.1016/S0092-8674(00)81446-4;
RA Vainberg I.E., Lewis S.A., Rommelaere H., Ampe C., Vandekerckhove J.,
RA Klein H.L., Cowan N.J.;
RT "Prefoldin, a chaperone that delivers unfolded proteins to cytosolic
RT chaperonin.";
RL Cell 93:863-873(1998).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-42, 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 [12]
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).
CC -!- FUNCTION: Binds specifically to cytosolic chaperonin (c-CPN) and
CC transfers target proteins to it. Binds to nascent polypeptide
CC chain and promotes folding in an environment in which there are
CC many competing pathways for nonnative proteins. Represses the
CC transcriptional activity of MYC.
CC -!- SUBUNIT: Heterohexamer of two PFD-alpha type and four PFD-beta
CC type subunits. Binds to MYC; interacts with its N-terminal domain.
CC -!- INTERACTION:
CC Q9DUN1:vIRF-3 (xeno); NbExp=8; IntAct=EBI-357275, EBI-1647907;
CC -!- SUBCELLULAR LOCATION: Isoform 1: Nucleus.
CC -!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm.
CC -!- SUBCELLULAR LOCATION: Isoform 3: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist;
CC Name=1; Synonyms=MM1-alpha;
CC IsoId=Q99471-1; Sequence=Displayed;
CC Name=2; Synonyms=MM1-beta;
CC IsoId=Q99471-2; Sequence=VSP_043104;
CC Note=Does not repress transcription activity of MYC;
CC Name=3; Synonyms=MM1-gamma;
CC IsoId=Q99471-3; Sequence=VSP_043103;
CC -!- TISSUE SPECIFICITY: Highly expressed in pancreas and skeletal
CC muscle and moderately in other tissues.
CC -!- SIMILARITY: Belongs to the prefoldin subunit alpha family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA14006.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
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CC Distributed under the Creative Commons Attribution-NoDerivs License
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DR EMBL; D89667; BAA14006.1; ALT_INIT; mRNA.
DR EMBL; AB055802; BAB32643.1; -; Genomic_DNA.
DR EMBL; AB055803; BAB32644.1; -; mRNA.
DR EMBL; AB055804; BAB32645.1; -; mRNA.
DR EMBL; AB055805; BAB32646.1; -; mRNA.
DR EMBL; BT007195; AAP35859.1; -; mRNA.
DR EMBL; AK292623; BAF85312.1; -; mRNA.
DR EMBL; AC073611; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW96683.1; -; Genomic_DNA.
DR EMBL; CH471054; EAW96685.1; -; Genomic_DNA.
DR EMBL; BC003373; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC062671; AAH62671.1; -; mRNA.
DR RefSeq; NP_002615.2; NM_002624.3.
DR RefSeq; NP_665904.1; NM_145897.2.
DR UniGene; Hs.655327; -.
DR ProteinModelPortal; Q99471; -.
DR SMR; Q99471; 11-149.
DR DIP; DIP-28155N; -.
DR IntAct; Q99471; 14.
DR MINT; MINT-5003456; -.
DR STRING; 9606.ENSP00000334188; -.
DR PhosphoSite; Q99471; -.
DR DMDM; 12231038; -.
DR OGP; Q99471; -.
DR PaxDb; Q99471; -.
DR PeptideAtlas; Q99471; -.
DR PRIDE; Q99471; -.
DR DNASU; 5204; -.
DR Ensembl; ENST00000243040; ENSP00000243040; ENSG00000123349.
DR Ensembl; ENST00000334478; ENSP00000334188; ENSG00000123349.
DR Ensembl; ENST00000351500; ENSP00000266964; ENSG00000123349.
DR Ensembl; ENST00000551018; ENSP00000447942; ENSG00000123349.
DR GeneID; 5204; -.
DR KEGG; hsa:5204; -.
DR UCSC; uc001scl.3; human.
DR CTD; 5204; -.
DR GeneCards; GC12P053689; -.
DR HGNC; HGNC:8869; PFDN5.
DR HPA; HPA008587; -.
DR MIM; 604899; gene.
DR neXtProt; NX_Q99471; -.
DR PharmGKB; PA33210; -.
DR eggNOG; COG1730; -.
DR HOGENOM; HOG000207562; -.
DR HOVERGEN; HBG004539; -.
DR InParanoid; Q99471; -.
DR KO; K04797; -.
DR OMA; YYVKKTR; -.
DR PhylomeDB; Q99471; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR ChiTaRS; PFDN5; human.
DR GeneWiki; PFDN5; -.
DR GenomeRNAi; 5204; -.
DR NextBio; 20126; -.
DR PRO; PR:Q99471; -.
DR ArrayExpress; Q99471; -.
DR Bgee; Q99471; -.
DR CleanEx; HS_PFDN5; -.
DR Genevestigator; Q99471; -.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0016272; C:prefoldin complex; IEA:InterPro.
DR GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
DR GO; GO:0051084; P:'de novo' posttranslational protein folding; TAS:Reactome.
DR GO; GO:0090090; P:negative regulation of canonical Wnt receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; IMP:BHF-UCL.
DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR InterPro; IPR011599; PFD_alpha.
DR InterPro; IPR027236; PFDN5.
DR InterPro; IPR009053; Prefoldin.
DR InterPro; IPR004127; Prefoldin_subunit_alpha.
DR PANTHER; PTHR12674:SF0; PTHR12674:SF0; 1.
DR Pfam; PF02996; Prefoldin; 1.
DR SUPFAM; SSF46579; SSF46579; 1.
DR TIGRFAMs; TIGR00293; TIGR00293; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chaperone; Complete proteome;
KW Cytoplasm; Nucleus; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 154 Prefoldin subunit 5.
FT /FTId=PRO_0000153661.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 42 42 N6-acetyllysine.
FT VAR_SEQ 25 69 Missing (in isoform 3).
FT /FTId=VSP_043103.
FT VAR_SEQ 59 154 GKELLVPLTSSMYVPGKLHDVEHVLIDVGTGYYVEKTAEDA
FT KDFFKRKIDFLTKQMEKIQPALQEKHAMKQAVMEMMSQKIQ
FT QLTALGAAQATAKA -> DVCPWEAA (in isoform
FT 2).
FT /FTId=VSP_043104.
SQ SEQUENCE 154 AA; 17328 MW; 0DA1F3644548CB14 CRC64;
MAQSINITEL NLPQLEMLKN QLDQEVEFLS TSIAQLKVVQ TKYVEAKDCL NVLNKSNEGK
ELLVPLTSSM YVPGKLHDVE HVLIDVGTGY YVEKTAEDAK DFFKRKIDFL TKQMEKIQPA
LQEKHAMKQA VMEMMSQKIQ QLTALGAAQA TAKA
//
MIM
604899
*RECORD*
*FIELD* NO
604899
*FIELD* TI
*604899 PREFOLDIN 5; PFDN5
;;MM1
*FIELD* TX
Molecular chaperones are proteins that assist in the correct folding of
read moreother proteins in the crowded molecular environment that exists in
living cells. Within this class of proteins, a key role is played by
chaperonins, multisubunit toroidal assemblies that undergo major
ATP-dependent conformational changes as part of the mechanism of
facilitated folding (see 118190).
Using a yeast 2-hybrid screen of a HeLa cell cDNA library with c-myc as
bait, Mori et al. (1998) isolated a cDNA that they designated MM1 (for
myc modulator-1). The MM1 cDNA encodes a deduced 167-amino acid protein
with a putative leucine zipper motif in the N terminus. Northern blot
analysis revealed expression of 4 distinct bands (0.7, 1.15, 2.9 and 4.4
kb); there was strong ubiquitous expression of the 0.7-kb transcript as
well as strong expression of the 1.15-kb transcript in pancreas, weak
expression in kidney, skeletal muscle, and placenta, and faint
expression in liver and lung. Fluorescent microscopy showed MM1
expression primarily in the nucleus, with lower intensity in nucleoli
and cytoplasm. Binding analyses indicated that MM1 and c-myc bind
directly and that all but the N-terminal 13 amino acids of MM1 are
required for binding. MM1 interacts with the myc box-2, a
transcription-activating domain of c-myc.
Vainberg et al. (1998) described the biochemical purification of a
heterohexameric chaperone protein, which they called prefoldin. One of
its subunits, prefoldin-5, is identical to MM1. Vainberg et al. (1998)
found that deletion of PFDN5 from yeast resulted in impaired functions
of the actin and tubulin-based cytoskeleton.
Prefoldin is a hexameric molecular chaperone complex built from 2
related classes of subunits, alpha and beta, and present in all
eukaryotes and archaea. Whereas eukaryotes have 2 related PFD-alpha
subunits and 4 related PFD-beta subunits, archaea have only 1 member of
each class, a PFD-alpha subunit whose closest human homolog is PFD5, and
a PFD-beta subunit whose closest human homolog is PFD6. Prefoldin
interacts with nascent polypeptide chains and, in vitro, can
functionally substitute for the Hsp70 chaperone system in stabilizing
nonnative proteins for subsequent folding in the central cavity of a
chaperonin. Siegert et al. (2000) presented the crystal structure and
characterization of the prefoldin hexamer from the archaeum
Methanobacterium thermoautotrophicum. Prefoldin has the appearance of a
jellyfish: its body consists of a double beta-barrel assembly with 6
long tentacle-like coiled coils protruding from it. The distal regions
of the coiled coils expose hydrophobic patches and are required for
multivalent binding of nonnative proteins.
The International Radiation Hybrid Mapping Consortium mapped the PFDN5
gene to chromosome 12 (TMAP SHGC-31943).
*FIELD* RF
1. Mori, K.; Maeda, Y.; Kitaura, H.; Taira, T.; Iguchi-Ariga, S. M.;
Ariga, H.: MM-1, a novel c-myc associating protein that represses
transcriptional activity of c-myc. J. Biol. Chem. 273: 29794-29800,
1998.
2. Siegert, R.; Leroux, M. R.; Scheufler, C.; Hartl, F. U.; Moarefi,
I.: Structure of the molecular chaperone prefoldin: unique interaction
of multiple coiled coil tentacles with unfolded proteins. Cell 103:
621-632, 2000.
3. Vainberg, I. E.; Lewis, S. A.; Rommelaere, H.; Ampe, C.; Vandekerckhove,
J.; Klein, H. L.; Cowan, N. J.: Prefoldin, a chaperone that delivers
unfolded proteins to cytosolic chaperonin. Cell 93: 863-873, 1998.
*FIELD* CN
Stylianos E. Antonarakis - updated: 11/21/2000
*FIELD* CD
Paul J. Converse: 5/1/2000
*FIELD* ED
mgross: 11/21/2000
carol: 5/1/2000
*RECORD*
*FIELD* NO
604899
*FIELD* TI
*604899 PREFOLDIN 5; PFDN5
;;MM1
*FIELD* TX
Molecular chaperones are proteins that assist in the correct folding of
read moreother proteins in the crowded molecular environment that exists in
living cells. Within this class of proteins, a key role is played by
chaperonins, multisubunit toroidal assemblies that undergo major
ATP-dependent conformational changes as part of the mechanism of
facilitated folding (see 118190).
Using a yeast 2-hybrid screen of a HeLa cell cDNA library with c-myc as
bait, Mori et al. (1998) isolated a cDNA that they designated MM1 (for
myc modulator-1). The MM1 cDNA encodes a deduced 167-amino acid protein
with a putative leucine zipper motif in the N terminus. Northern blot
analysis revealed expression of 4 distinct bands (0.7, 1.15, 2.9 and 4.4
kb); there was strong ubiquitous expression of the 0.7-kb transcript as
well as strong expression of the 1.15-kb transcript in pancreas, weak
expression in kidney, skeletal muscle, and placenta, and faint
expression in liver and lung. Fluorescent microscopy showed MM1
expression primarily in the nucleus, with lower intensity in nucleoli
and cytoplasm. Binding analyses indicated that MM1 and c-myc bind
directly and that all but the N-terminal 13 amino acids of MM1 are
required for binding. MM1 interacts with the myc box-2, a
transcription-activating domain of c-myc.
Vainberg et al. (1998) described the biochemical purification of a
heterohexameric chaperone protein, which they called prefoldin. One of
its subunits, prefoldin-5, is identical to MM1. Vainberg et al. (1998)
found that deletion of PFDN5 from yeast resulted in impaired functions
of the actin and tubulin-based cytoskeleton.
Prefoldin is a hexameric molecular chaperone complex built from 2
related classes of subunits, alpha and beta, and present in all
eukaryotes and archaea. Whereas eukaryotes have 2 related PFD-alpha
subunits and 4 related PFD-beta subunits, archaea have only 1 member of
each class, a PFD-alpha subunit whose closest human homolog is PFD5, and
a PFD-beta subunit whose closest human homolog is PFD6. Prefoldin
interacts with nascent polypeptide chains and, in vitro, can
functionally substitute for the Hsp70 chaperone system in stabilizing
nonnative proteins for subsequent folding in the central cavity of a
chaperonin. Siegert et al. (2000) presented the crystal structure and
characterization of the prefoldin hexamer from the archaeum
Methanobacterium thermoautotrophicum. Prefoldin has the appearance of a
jellyfish: its body consists of a double beta-barrel assembly with 6
long tentacle-like coiled coils protruding from it. The distal regions
of the coiled coils expose hydrophobic patches and are required for
multivalent binding of nonnative proteins.
The International Radiation Hybrid Mapping Consortium mapped the PFDN5
gene to chromosome 12 (TMAP SHGC-31943).
*FIELD* RF
1. Mori, K.; Maeda, Y.; Kitaura, H.; Taira, T.; Iguchi-Ariga, S. M.;
Ariga, H.: MM-1, a novel c-myc associating protein that represses
transcriptional activity of c-myc. J. Biol. Chem. 273: 29794-29800,
1998.
2. Siegert, R.; Leroux, M. R.; Scheufler, C.; Hartl, F. U.; Moarefi,
I.: Structure of the molecular chaperone prefoldin: unique interaction
of multiple coiled coil tentacles with unfolded proteins. Cell 103:
621-632, 2000.
3. Vainberg, I. E.; Lewis, S. A.; Rommelaere, H.; Ampe, C.; Vandekerckhove,
J.; Klein, H. L.; Cowan, N. J.: Prefoldin, a chaperone that delivers
unfolded proteins to cytosolic chaperonin. Cell 93: 863-873, 1998.
*FIELD* CN
Stylianos E. Antonarakis - updated: 11/21/2000
*FIELD* CD
Paul J. Converse: 5/1/2000
*FIELD* ED
mgross: 11/21/2000
carol: 5/1/2000