PCL5_YEAST
ID PCL5_YEAST Reviewed; 229 AA.
AC P38794; D3DL20;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=PHO85 cyclin-5;
DE AltName: Full=G1/S-specific cyclin PCL5;
GN Name=PCL5; OrderedLocusNames=YHR071W; ORFNames=H8025.1;
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=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
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 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 [4]
RP INTERACTION WITH PHO85.
RX PubMed=9032248; DOI=10.1128/mcb.17.3.1212;
RA Measday V., Moore L., Retnakaran R., Lee J., Donoviel M., Neiman A.M.,
RA Andrews B.J.;
RT "A family of cyclin-like proteins that interact with the Pho85 cyclin-
RT dependent kinase.";
RL Mol. Cell. Biol. 17:1212-1223(1997).
RN [5]
RP FUNCTION, INDUCTION, AND PHOSPHORYLATION OF GCN4.
RX PubMed=12101234; DOI=10.1128/mcb.22.15.5395-5404.2002;
RA Shemer R., Meimoun A., Holtzman T., Kornitzer D.;
RT "Regulation of the transcription factor Gcn4 by Pho85 cyclin PCL5.";
RL Mol. Cell. Biol. 22:5395-5404(2002).
CC -!- FUNCTION: Cyclin partner of the cyclin-dependent kinase (CDK) PHO85.
CC Positively controls degradation of transcription factor GCN4 under
CC favorable growth conditions. The PCL5-PHO85 cyclin-CDK holoenzyme
CC phosphorylates GCN4, which is required for its degradation by the E3
CC ubiquitin ligase complex SCF(Cdc4). Amino acid starvation reduces PCL5-
CC PHO85-associated GCN4 kinase activity and leads to stabilization of
CC GCN4. {ECO:0000269|PubMed:12101234}.
CC -!- SUBUNIT: Forms a cyclin-CDK complex with PHO85.
CC -!- INTERACTION:
CC P38794; P17157: PHO85; NbExp=2; IntAct=EBI-4504, EBI-13327;
CC -!- INDUCTION: By transcription factor GCN4. Rapidly degraded under
CC starvation conditions. {ECO:0000269|PubMed:12101234}.
CC -!- SIMILARITY: Belongs to the cyclin family. PCL1,2 subfamily.
CC {ECO:0000305}.
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DR EMBL; U00061; AAB68375.1; -; Genomic_DNA.
DR EMBL; AY558281; AAS56607.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06764.1; -; Genomic_DNA.
DR PIR; S46696; S46696.
DR RefSeq; NP_011938.1; NM_001179201.1.
DR AlphaFoldDB; P38794; -.
DR SMR; P38794; -.
DR BioGRID; 36503; 81.
DR ComplexPortal; CPX-1696; PCL5-PHO85 kinase complex.
DR DIP; DIP-5804N; -.
DR IntAct; P38794; 1.
DR STRING; 4932.YHR071W; -.
DR iPTMnet; P38794; -.
DR PaxDb; P38794; -.
DR PRIDE; P38794; -.
DR EnsemblFungi; YHR071W_mRNA; YHR071W; YHR071W.
DR GeneID; 856468; -.
DR KEGG; sce:YHR071W; -.
DR SGD; S000001113; PCL5.
DR VEuPathDB; FungiDB:YHR071W; -.
DR eggNOG; KOG1674; Eukaryota.
DR HOGENOM; CLU_101101_0_0_1; -.
DR InParanoid; P38794; -.
DR OMA; MERWCLG; -.
DR BioCyc; YEAST:G3O-31121-MON; -.
DR PRO; PR:P38794; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38794; protein.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IPI:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IDA:SGD.
DR GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IMP:SGD.
DR GO; GO:0016242; P:negative regulation of macroautophagy; IMP:SGD.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0031647; P:regulation of protein stability; IMP:SGD.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR006671; Cyclin_N.
DR InterPro; IPR013922; Cyclin_PHO80-like.
DR PANTHER; PTHR15615; PTHR15615; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR SUPFAM; SSF47954; SSF47954; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cyclin; Reference proteome.
FT CHAIN 1..229
FT /note="PHO85 cyclin-5"
FT /id="PRO_0000080501"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 229 AA; 26467 MW; B6839ABB9DB5DD49 CRC64;
MDGNHRFTPD SKEFNTVVKS KESSTGRNPY QTPPLEHNGT HHQTNYSRKK TNLAIIISNF
LSEISRPLSN GKINNSTHNI LKFLNEVLKR SKCSKENAVL ATFYFQKIHQ SRGVRDESSL
PEFSHCSRRI FLCCLILSHK FLNDNTYSMK NWQIISGLHA KDLSLMERWC LGKLNYELAI
PYDEFLLWET NTLMKAKLRV GTPANAPVKR PRESDNDYDA NSWKQIKSC
