PFD6_YEAST
ID PFD6_YEAST Reviewed; 114 AA.
AC P52553; D6VYK2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Prefoldin subunit 6;
DE AltName: Full=Genes involved in microtubule biogenesis protein 1;
DE AltName: Full=Gim complex subunit 1;
DE Short=GimC subunit 1;
GN Name=YKE2; Synonyms=GIM1, PFD6; OrderedLocusNames=YLR200W;
GN ORFNames=L8167.8;
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=D273-10B/AL;
RX PubMed=7828874; DOI=10.1016/0378-1119(94)90656-4;
RA Shang H.-S., Wong S.-M., Tan H.-M., Wu M.;
RT "YKE2, a yeast nuclear gene encoding a protein showing homology to mouse
RT KE2 and containing a putative leucine-zipper motif.";
RL Gene 151:197-201(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 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 [5]
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 [6]
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 P52553; P43573: BUD27; NbExp=3; IntAct=EBI-13260, EBI-22787;
CC P52553; Q04493: GIM5; NbExp=4; IntAct=EBI-13260, EBI-13253;
CC P52553; P48363: PAC10; NbExp=5; IntAct=EBI-13260, EBI-13239;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 784 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; X76563; CAA54062.1; -; Genomic_DNA.
DR EMBL; U14913; AAB67430.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09518.1; -; Genomic_DNA.
DR PIR; S48552; S48552.
DR RefSeq; NP_013301.1; NM_001182087.1.
DR AlphaFoldDB; P52553; -.
DR SMR; P52553; -.
DR BioGRID; 31469; 732.
DR ComplexPortal; CPX-1671; Prefoldin co-chaperone complex.
DR DIP; DIP-1333N; -.
DR IntAct; P52553; 14.
DR MINT; P52553; -.
DR STRING; 4932.YLR200W; -.
DR iPTMnet; P52553; -.
DR MaxQB; P52553; -.
DR PaxDb; P52553; -.
DR PRIDE; P52553; -.
DR EnsemblFungi; YLR200W_mRNA; YLR200W; YLR200W.
DR GeneID; 850897; -.
DR KEGG; sce:YLR200W; -.
DR SGD; S000004190; YKE2.
DR VEuPathDB; FungiDB:YLR200W; -.
DR eggNOG; KOG3478; Eukaryota.
DR GeneTree; ENSGT00390000010512; -.
DR HOGENOM; CLU_125172_1_1_1; -.
DR InParanoid; P52553; -.
DR OMA; VQTEFAQ; -.
DR BioCyc; YEAST:G3O-32320-MON; -.
DR PRO; PR:P52553; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P52553; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IC:SGD.
DR GO; GO:0016272; C:prefoldin complex; IPI:SGD.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0015631; F:tubulin binding; IDA:SGD.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IBA:GO_Central.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IMP:SGD.
DR GO; GO:0006457; P:protein folding; IMP:SGD.
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; IPR009053; Prefoldin.
DR Pfam; PF01920; Prefoldin_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Nucleus; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..114
FT /note="Prefoldin subunit 6"
FT /id="PRO_0000124855"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 114 AA; 13284 MW; BF66D1A9859E14B8 CRC64;
MSELGAKYQQ LQNELEEFIV ARQKLETQLQ ENKIVNEEFD QLEEDTPVYK LTGNVLLPVE
QSEARTNVDK RLEFIETEIT RCEKNIRDKQ EELEKMRSEL IKLNNTAAST GPGR
