PFD5_YEAST
ID PFD5_YEAST Reviewed; 163 AA.
AC Q04493; D6W0J1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Prefoldin subunit 5;
DE AltName: Full=Genes involved in microtubule biogenesis protein 5;
DE AltName: Full=Gim complex subunit 5;
DE Short=GimC subunit 5;
GN Name=GIM5; Synonyms=PFD5; OrderedLocusNames=YML094W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [2]
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 [3]
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 [4]
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 [5]
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).
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 Q04493; P48363: PAC10; NbExp=5; IntAct=EBI-13253, EBI-13239;
CC Q04493; P52553: YKE2; NbExp=4; IntAct=EBI-13253, EBI-13260;
CC -!- MISCELLANEOUS: Present with 2900 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the prefoldin subunit alpha family.
CC {ECO:0000305}.
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DR EMBL; Z46660; CAA86644.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09805.1; -; Genomic_DNA.
DR PIR; S49633; S49633.
DR RefSeq; NP_013616.1; NM_001182453.1.
DR AlphaFoldDB; Q04493; -.
DR SMR; Q04493; -.
DR BioGRID; 35049; 598.
DR ComplexPortal; CPX-1671; Prefoldin co-chaperone complex.
DR DIP; DIP-1332N; -.
DR IntAct; Q04493; 12.
DR MINT; Q04493; -.
DR STRING; 4932.YML094W; -.
DR iPTMnet; Q04493; -.
DR MaxQB; Q04493; -.
DR PaxDb; Q04493; -.
DR PRIDE; Q04493; -.
DR TopDownProteomics; Q04493; -.
DR EnsemblFungi; YML094W_mRNA; YML094W; YML094W.
DR GeneID; 854879; -.
DR KEGG; sce:YML094W; -.
DR SGD; S000004559; GIM5.
DR VEuPathDB; FungiDB:YML094W; -.
DR eggNOG; KOG3048; Eukaryota.
DR GeneTree; ENSGT00390000008783; -.
DR HOGENOM; CLU_091867_0_2_1; -.
DR InParanoid; Q04493; -.
DR OMA; QAKFKAC; -.
DR BioCyc; YEAST:G3O-32679-MON; -.
DR PRO; PR:Q04493; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q04493; 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:0015631; F:tubulin binding; IDA:SGD.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
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:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0007021; P:tubulin complex assembly; IMP:SGD.
DR Gene3D; 1.10.287.370; -; 1.
DR InterPro; IPR011599; PFD_alpha_archaea.
DR InterPro; IPR009053; Prefoldin.
DR InterPro; IPR004127; Prefoldin_subunit_alpha.
DR PANTHER; PTHR12674; PTHR12674; 1.
DR Pfam; PF02996; Prefoldin; 1.
DR TIGRFAMs; TIGR00293; TIGR00293; 1.
PE 1: Evidence at protein level;
KW Chaperone; Reference proteome.
FT CHAIN 1..163
FT /note="Prefoldin subunit 5"
FT /id="PRO_0000153668"
FT REGION 144..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 163 AA; 18356 MW; 24C71A33885CEE63 CRC64;
MSSQKIDLTK LNPEQLNAVK QQFDQELQHF TQSLQALTMA KGKFTECIDD IKTVSQAGNE
GQKLLVPASA SLYIPGKIVD NKKFMVDIGT GYYVEKSAEA AIAFYQKKVD KLNKESVQIQ
DIIKEKTQYS LSIEAQIRQA AIRQHEAMSK QQQQQQKKES STA
