PCL7_YEAST
ID PCL7_YEAST Reviewed; 285 AA.
AC P40186; D6VVN1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=PHO85 cyclin-7;
DE AltName: Full=PHO85-associated protein 1;
GN Name=PCL7; Synonyms=PAP1; OrderedLocusNames=YIL050W;
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=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(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 PROTEIN SEQUENCE OF 2-11, AND INTERACTION WITH PHO85.
RX PubMed=12174291;
RA Wu J.S., Xia Z.X., Cao Z., Ao S.Z.;
RT "Cloning and expression of a novel PHO85 associated protein PAP1 gene of
RT Saccharomyces cerevisiae.";
RL Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 30:14-20(1998).
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, INTERACTION WITH PHO81 AND PHO85, ACTIVITY REGULATION, AND
RP INDUCTION.
RX PubMed=11069666; DOI=10.1046/j.1365-2958.2000.02140.x;
RA Lee M., O'Regan S., Moreau J.-L., Johnson A.L., Johnston L.H., Goding C.R.;
RT "Regulation of the Pcl7-Pho85 cyclin-cdk complex by Pho81.";
RL Mol. Microbiol. 38:411-422(2000).
RN [6]
RP FUNCTION.
RX PubMed=11602261; DOI=10.1016/s0014-5793(01)02914-3;
RA Wang Z., Wilson W.A., Fujino M.A., Roach P.J.;
RT "The yeast cyclins Pcl6p and Pcl7p are involved in the control of glycogen
RT storage by the cyclin-dependent protein kinase Pho85p.";
RL FEBS Lett. 506:277-280(2001).
RN [7]
RP FUNCTION, INTERACTION WITH MMR1, AND PHOSPHORYLATION OF MMR1.
RX PubMed=12006994;
RA Shi X.Z., Ao S.Z.;
RT "Phosphorylation of YLR190w by PAP1 PHO85 kinase complex.";
RL Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 34:187-192(2002).
RN [8]
RP FUNCTION, INTERACTION WITH YJL084C, AND PHOSPHORYLATION OF YJL084C.
RX PubMed=12098764;
RA Shi X.Z., Ao S.Z.;
RT "Analysis of phosphorylation of YJL084c, a yeast protein.";
RL Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 34:433-438(2002).
RN [9]
RP FUNCTION, AND PHOSPHORYLATION OF GLC8.
RX PubMed=12407105; DOI=10.1074/jbc.m208058200;
RA Tan Y.S.H., Morcos P.A., Cannon J.F.;
RT "Pho85 phosphorylates the Glc7 protein phosphatase regulator Glc8 in
RT vivo.";
RL J. Biol. Chem. 278:147-153(2003).
RN [10]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [11]
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 [12]
RP FUNCTION.
RX PubMed=15721288; DOI=10.1016/j.bbrc.2005.01.106;
RA Wilson W.A., Wang Z., Roach P.J.;
RT "Regulation of yeast glycogen phosphorylase by the cyclin-dependent protein
RT kinase Pho85p.";
RL Biochem. Biophys. Res. Commun. 329:161-167(2005).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: Cyclin partner of the cyclin-dependent kinase (CDK) PHO85.
CC Together with cyclin PCL6, controls glycogen phosphorylase and glycogen
CC synthase activities in response to nutrient availablility. The PCL7-
CC PHO85 cyclin-CDK holoenzyme has GLC8 kinase activity and phosphorylates
CC and inactivates the phosphatase PP1-2 inhibitor GLC8, causing
CC activation of PP1-2, which then dephosphorylates and activates glycogen
CC phosphorylase. PCL7-PHO85 also phosphorylates MMR1 and YJL084C.
CC {ECO:0000269|PubMed:11069666, ECO:0000269|PubMed:11602261,
CC ECO:0000269|PubMed:12006994, ECO:0000269|PubMed:12098764,
CC ECO:0000269|PubMed:12407105, ECO:0000269|PubMed:15721288}.
CC -!- ACTIVITY REGULATION: The PCL7-PHO85 cyclin-CDK is inhibited by PHO81 in
CC low-phosphate conditions. {ECO:0000269|PubMed:11069666}.
CC -!- SUBUNIT: Forms a cyclin-CDK complex with PHO85. Interacts with the
CC substrate proteins MMR1 and YJL084C. Interacts with the CDK inhibitor
CC (CKI) PHO81. {ECO:0000269|PubMed:11069666, ECO:0000269|PubMed:12006994,
CC ECO:0000269|PubMed:12098764, ECO:0000269|PubMed:12174291,
CC ECO:0000269|PubMed:9032248}.
CC -!- INTERACTION:
CC P40186; P17157: PHO85; NbExp=8; IntAct=EBI-25021, EBI-13327;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: Cell cycle regulated, with a peak in mid to late S phase.
CC {ECO:0000269|PubMed:11069666}.
CC -!- MISCELLANEOUS: Present with 3390 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the cyclin family. PHO80 subfamily.
CC {ECO:0000305}.
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DR EMBL; Z38060; CAA86172.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08497.1; -; Genomic_DNA.
DR PIR; S48429; S48429.
DR RefSeq; NP_012214.3; NM_001179400.3.
DR AlphaFoldDB; P40186; -.
DR SMR; P40186; -.
DR BioGRID; 34940; 60.
DR ComplexPortal; CPX-1690; PCL7-PHO85 kinase complex.
DR DIP; DIP-1508N; -.
DR IntAct; P40186; 4.
DR MINT; P40186; -.
DR STRING; 4932.YIL050W; -.
DR iPTMnet; P40186; -.
DR MaxQB; P40186; -.
DR PaxDb; P40186; -.
DR PRIDE; P40186; -.
DR EnsemblFungi; YIL050W_mRNA; YIL050W; YIL050W.
DR GeneID; 854761; -.
DR KEGG; sce:YIL050W; -.
DR SGD; S000001312; PCL7.
DR VEuPathDB; FungiDB:YIL050W; -.
DR eggNOG; KOG1674; Eukaryota.
DR GeneTree; ENSGT00390000000862; -.
DR HOGENOM; CLU_074159_0_0_1; -.
DR InParanoid; P40186; -.
DR OMA; YCAYLQK; -.
DR BioCyc; YEAST:G3O-31321-MON; -.
DR PRO; PR:P40186; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40186; protein.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IPI:SGD.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:SGD.
DR GO; GO:0005979; P:regulation of glycogen biosynthetic process; IGI:SGD.
DR GO; GO:0005981; P:regulation of glycogen catabolic process; IGI:SGD.
DR GO; GO:0031647; P:regulation of protein stability; IMP:SGD.
DR InterPro; IPR013922; Cyclin_PHO80-like.
DR PANTHER; PTHR15615; PTHR15615; 2.
DR Pfam; PF08613; Cyclin; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cell cycle; Cell division; Cyclin; Cytoplasm;
KW Direct protein sequencing; Glycogen metabolism; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12174291"
FT CHAIN 2..285
FT /note="PHO85 cyclin-7"
FT /id="PRO_0000202991"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 285 AA; 32037 MW; F81EEA8E39BC0FC5 CRC64;
MELSSPSKKT TTSPINIPGG NRDNLIIGPH SHSFKTDPFS SNNSSLLSKI STNPSLESPF
SSKSLLDCSP VQAVKKSLES EAKTHSLDEE TNEQTDVKIL NIADFPTDEL ILMISALLNR
IITANDETTD VSQQVSDETE DELLTPILAF YGKNVPEIAV VQYLERIQKY CPTTNDIFLS
LLVYFDRISK NYGHSSERNG CAKQLFVMDS GNIHRLLITG VTICTKFLSD FFYSNSRYAK
VGGISLQELN HLELQFLILC DFKLLVSVEE MQKYANLLYK FWNDQ
