PFD4_YEAST
ID PFD4_YEAST Reviewed; 129 AA.
AC P53900; D6W130;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Prefoldin subunit 4;
DE AltName: Full=Genes involved in microtubule biogenesis protein 3;
DE AltName: Full=Gim complex subunit 3;
DE Short=GimC subunit 3;
GN Name=GIM3; Synonyms=PFD4; OrderedLocusNames=YNL153C; ORFNames=N1761;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8686380;
RX DOI=10.1002/(sici)1097-0061(199602)12:2<169::aid-yea894>3.0.co;2-b;
RA Nasr F., Becam A.-M., Herbert C.J.;
RT "The sequence of 36.8 kb from the left arm of chromosome XIV reveals 24
RT complete open reading frames: 18 correspond to new genes, one of which
RT encodes a protein similar to the human myotonic dystrophy kinase.";
RL Yeast 12:169-175(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP CHARACTERIZATION.
RX PubMed=9463374; DOI=10.1093/emboj/17.4.952;
RA Geissler S., Siegers K., Schiebel E.;
RT "A novel protein complex promoting formation of functional alpha- and
RT gamma-tubulin.";
RL EMBO J. 17:952-966(1998).
RN [6]
RP IDENTIFICATION IN THE PREFOLDIN COMPLEX.
RX PubMed=9878052; DOI=10.1093/emboj/18.1.75;
RA Siegers K., Waldmann T., Leroux M.R., Grein K., Shevchenko A., Schiebel E.,
RA Hartl F.U.;
RT "Compartmentation of protein folding in vivo: sequestration of non-native
RT polypeptide by the chaperonin-GimC system.";
RL EMBO J. 18:75-84(1999).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Binds specifically to cytosolic chaperonin (c-CPN) and
CC transfers target proteins to it. Binds to nascent polypeptide chain and
CC promotes folding in an environment in which there are many competing
CC pathways for nonnative proteins.
CC -!- SUBUNIT: Heterohexamer of two PFD-alpha type and four PFD-beta type
CC subunits. {ECO:0000269|PubMed:9878052}.
CC -!- INTERACTION:
CC P53900; P48363: PAC10; NbExp=3; IntAct=EBI-13246, EBI-13239;
CC -!- MISCELLANEOUS: Present with 7470 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the prefoldin subunit beta family.
CC {ECO:0000305}.
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DR EMBL; X92517; CAA63286.1; -; Genomic_DNA.
DR EMBL; Z71429; CAA96040.1; -; Genomic_DNA.
DR EMBL; AY692812; AAT92831.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10396.1; -; Genomic_DNA.
DR PIR; S60974; S60974.
DR RefSeq; NP_014246.1; NM_001182991.1.
DR AlphaFoldDB; P53900; -.
DR SMR; P53900; -.
DR BioGRID; 35676; 832.
DR ComplexPortal; CPX-1671; Prefoldin co-chaperone complex.
DR DIP; DIP-3000N; -.
DR IntAct; P53900; 11.
DR MINT; P53900; -.
DR STRING; 4932.YNL153C; -.
DR iPTMnet; P53900; -.
DR MaxQB; P53900; -.
DR PaxDb; P53900; -.
DR PRIDE; P53900; -.
DR EnsemblFungi; YNL153C_mRNA; YNL153C; YNL153C.
DR GeneID; 855569; -.
DR KEGG; sce:YNL153C; -.
DR SGD; S000005097; GIM3.
DR VEuPathDB; FungiDB:YNL153C; -.
DR eggNOG; KOG1760; Eukaryota.
DR GeneTree; ENSGT00390000006696; -.
DR HOGENOM; CLU_130032_0_0_1; -.
DR InParanoid; P53900; -.
DR OMA; KFGRAIN; -.
DR BioCyc; YEAST:G3O-33170-MON; -.
DR PRO; PR:P53900; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53900; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0016272; C:prefoldin complex; IPI:SGD.
DR GO; GO:0015631; F:tubulin binding; IDA:SGD.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0071629; P:cytoplasm protein quality control by the ubiquitin-proteasome system; IMP:SGD.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IMP:SGD.
DR GO; GO:0006457; P:protein folding; IC:ComplexPortal.
DR GO; GO:0007021; P:tubulin complex assembly; IMP:SGD.
DR Gene3D; 1.10.287.370; -; 1.
DR InterPro; IPR002777; PFD_beta-like.
DR InterPro; IPR016661; PFDN4.
DR InterPro; IPR009053; Prefoldin.
DR PANTHER; PTHR21100; PTHR21100; 1.
DR Pfam; PF01920; Prefoldin_2; 1.
DR PIRSF; PIRSF016477; Prefoldin_subunit_4; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Reference proteome.
FT CHAIN 1..129
FT /note="Prefoldin subunit 4"
FT /id="PRO_0000124848"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 129 AA; 15180 MW; 4738F9EA813E04A9 CRC64;
MELLPQGQRN NTQVTFEDQQ KINEFSKLIM RKDAIAQELS LQREEKEYLD DVSLEIELID
EDEPVQYKVG DLFIFMKQSK VTAQLEKDAE RLDNKIETLE DKQRDIDSRL DALKAILYAK
FGDNINLER
