PCL2_YEAST
ID PCL2_YEAST Reviewed; 308 AA.
AC P25693; D6VRM3; Q07554;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=PHO85 cyclin-2;
DE AltName: Full=Cyclin HCS26 homolog;
DE AltName: Full=G1/S-specific cyclin PCL2;
GN Name=PCL2; Synonyms=CLN4; OrderedLocusNames=YDL127W; ORFNames=D2223;
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].
RX PubMed=1860879; DOI=10.1083/jcb.114.3.443;
RA Froehlich K.-U., Fries H.W., Ruediger M., Erdmann R., Botstein D.,
RA Mecke D.;
RT "Yeast cell cycle protein CDC48p shows full-length homology to the
RT mammalian protein VCP and is a member of a protein family involved in
RT secretion, peroxisome formation, and gene expression.";
RL J. Cell Biol. 114:443-453(1991).
RN [2]
RP SEQUENCE REVISION.
RA Froehlich K.-U.;
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [4]
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 [5]
RP CHARACTERIZATION, INTERACTION WITH PHO85, AND INDUCTION.
RX PubMed=7973731; DOI=10.1126/science.7973731;
RA Measday V., Moore L., Ogas J., Tyers M., Andrews B.J.;
RT "The PCL2 (ORFD)-PHO85 cyclin-dependent kinase complex: a cell cycle
RT regulator in yeast.";
RL Science 266:1391-1395(1994).
RN [6]
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 [7]
RP FUNCTION, INTERACTION WITH RVS167, AND PHOSPHORYLATION OF RVS167.
RX PubMed=9843683; DOI=10.1016/s0960-9822(07)00561-1;
RA Lee J., Colwill K., Aneliunas V., Tennyson C.N., Moore L., Ho Y.,
RA Andrews B.J.;
RT "Interaction of yeast Rvs167 and Pho85 cyclin-dependent kinase complexes
RT may link the cell cycle to the actin cytoskeleton.";
RL Curr. Biol. 8:1310-1321(1998).
RN [8]
RP INDUCTION.
RX PubMed=9529390; DOI=10.1091/mbc.9.4.945;
RA Aerne B.L., Johnson A.L., Toyn J.H., Johnston L.H.;
RT "Swi5 controls a novel wave of cyclin synthesis in late mitosis.";
RL Mol. Biol. Cell 9:945-956(1998).
RN [9]
RP IDENTIFICATION OF FRAMESHIFT.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [10]
RP PHOSPHORYLATION OF RVS167.
RX PubMed=12857883; DOI=10.1091/mbc.e02-09-0613;
RA Friesen H., Murphy K., Breitkreutz A., Tyers M., Andrews B.J.;
RT "Regulation of the yeast amphiphysin homologue Rvs167p by
RT phosphorylation.";
RL Mol. Biol. Cell 14:3027-3040(2003).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14688790; DOI=10.1038/ncb1078;
RA Moffat J., Andrews B.J.;
RT "Late-G1 cyclin-CDK activity is essential for control of cell morphogenesis
RT in budding yeast.";
RL Nat. Cell Biol. 6:59-66(2004).
RN [12]
RP FUNCTION, AND PHOSPHORYLATION OF LCB4.
RX PubMed=15598647; DOI=10.1074/jbc.m410908200;
RA Iwaki S., Kihara A., Sano T., Igarashi Y.;
RT "Phosphorylation by Pho85 cyclin-dependent kinase acts as a signal for the
RT down-regulation of the yeast sphingoid long-chain base kinase Lcb4 during
RT the stationary phase.";
RL J. Biol. Chem. 280:6520-6527(2005).
CC -!- FUNCTION: G1/S-specific cyclin partner of the cyclin-dependent kinase
CC (CDK) PHO85. Essential for the control of the cell cycle at the G1/S
CC (start) transition. Together with cyclin PCL1, positively controls
CC degradation of sphingoid long chain base kinase LCB4. The PCL2-PHO85
CC cyclin-CDK holoenzyme phosphorylates LCB4, which is required for its
CC ubiquitination and degradation. PCL2-PHO85 also phosphorylates RVS167,
CC linking cyclin-CDK activity with organization of the actin
CC cytoskeleton. {ECO:0000269|PubMed:14688790,
CC ECO:0000269|PubMed:15598647, ECO:0000269|PubMed:9843683}.
CC -!- SUBUNIT: Forms a cyclin-CDK complex with PHO85. Interacts with RVS167.
CC {ECO:0000269|PubMed:7973731, ECO:0000269|PubMed:9032248,
CC ECO:0000269|PubMed:9843683}.
CC -!- INTERACTION:
CC P25693; P17157: PHO85; NbExp=8; IntAct=EBI-4499, EBI-13327;
CC P25693; P10591: SSA1; NbExp=3; IntAct=EBI-4499, EBI-8591;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14688790}. Nucleus
CC {ECO:0000269|PubMed:14688790}. Note=Localizes to sites of polarized
CC growth, namely the incipient bud site, the bud tip and the bud neck.
CC -!- INDUCTION: By transcription factors SBF (SWI4-SWI6 cell-cycle box
CC binding factor) and SWI5 in a cell cycle-regulated manner. Peaks in G1
CC phase. {ECO:0000269|PubMed:7973731, ECO:0000269|PubMed:9529390}.
CC -!- SIMILARITY: Belongs to the cyclin family. PCL1,2 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA98695.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X56956; CAA40277.1; -; Genomic_DNA.
DR EMBL; Z74175; CAA98695.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BK006938; DAA11733.1; -; Genomic_DNA.
DR PIR; S67670; S67670.
DR RefSeq; NP_010156.2; NM_001180186.1.
DR AlphaFoldDB; P25693; -.
DR SMR; P25693; -.
DR BioGRID; 31936; 87.
DR ComplexPortal; CPX-1694; PCL2-PHO85 kinase complex.
DR DIP; DIP-1495N; -.
DR IntAct; P25693; 8.
DR MINT; P25693; -.
DR STRING; 4932.YDL127W; -.
DR iPTMnet; P25693; -.
DR PaxDb; P25693; -.
DR PRIDE; P25693; -.
DR EnsemblFungi; YDL127W_mRNA; YDL127W; YDL127W.
DR GeneID; 851430; -.
DR KEGG; sce:YDL127W; -.
DR SGD; S000002285; PCL2.
DR VEuPathDB; FungiDB:YDL127W; -.
DR eggNOG; KOG1674; Eukaryota.
DR GeneTree; ENSGT00390000000862; -.
DR HOGENOM; CLU_018149_0_0_1; -.
DR InParanoid; P25693; -.
DR OMA; HWASYTD; -.
DR BioCyc; YEAST:G3O-29526-MON; -.
DR PRO; PR:P25693; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P25693; protein.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
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:0000131; C:incipient cellular bud site; IDA: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:0044843; P:cell cycle G1/S phase transition; IC:ComplexPortal.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0030952; P:establishment or maintenance of cytoskeleton polarity; IC:ComplexPortal.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; IC:ComplexPortal.
DR GO; GO:0051302; P:regulation of cell division; IC:ComplexPortal.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:SGD.
DR GO; GO:0032878; P:regulation of establishment or maintenance of cell polarity; IGI:SGD.
DR GO; GO:0031106; P:septin ring organization; IGI:SGD.
DR CDD; cd00043; CYCLIN; 1.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR006671; Cyclin_N.
DR InterPro; IPR013922; Cyclin_PHO80-like.
DR InterPro; IPR012104; PHO85_cyclin_1/2/9.
DR PANTHER; PTHR15615; PTHR15615; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR PIRSF; PIRSF016511; Cyclin_Pcl; 1.
DR SMART; SM00385; CYCLIN; 1.
DR SUPFAM; SSF47954; SSF47954; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cyclin; Cytoplasm; Nucleus; Reference proteome.
FT CHAIN 1..308
FT /note="PHO85 cyclin-2"
FT /id="PRO_0000080500"
FT DOMAIN 18..146
FT /note="Cyclin N-terminal"
FT REGION 248..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 308 AA; 35207 MW; 914BE1E2B92858CA CRC64;
MSNYEALLKF NRKAVSKEMV QYLASTTASI IKIKKTNSMI DIALPAPPLT KFINRLIKHS
NVQTPTLMAT SVYLAKLRSI IPSNVYGIET TRHRIFLGCL ILAAKTLNDS SPLNKHWAEY
TDGLLILREV NTIERELLEY FDWDVTISTD DLITCLSPFL KPIKEEQLYK SQRDCRTLKN
FSAQEKDIVN KTSISHSRSS SNMSIPSLAS TSTLSTLESR RSNLSNYSNR IRTLPELHES
NNISDKFSPR TYNIDSKHDN KENRPIPTIK PFNFSKARPV ILKTGLNKQI IKEDTKVKKS
NWSNYFKS
