PCL10_YEAST
ID PCL10_YEAST Reviewed; 433 AA.
AC P53124; D6VU15;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=PHO85 cyclin-10;
GN Name=PCL10; OrderedLocusNames=YGL134W; ORFNames=G2838;
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=ATCC 96604 / S288c / FY1679;
RX PubMed=8840506;
RX DOI=10.1002/(sici)1097-0061(199607)12:9<887::aid-yea971>3.0.co;2-d;
RA Escribano V., Eraso P., Portillo F., Mazon M.J.;
RT "Sequence analysis of a 14.6 kb DNA fragment of Saccharomyces cerevisiae
RT chromosome VII reveals SEC27, SSM1b, a putative S-adenosylmethionine-
RT dependent enzyme and six new open reading frames.";
RL Yeast 12:887-892(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 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, PHOSPHORYLATION OF GSY2, AND INTERACTION WITH GSY2.
RX PubMed=9584169; DOI=10.1128/mcb.18.6.3289;
RA Huang D., Moffat J., Wilson W.A., Moore L., Cheng C., Roach P.J.,
RA Andrews B.J.;
RT "Cyclin partners determine Pho85 protein kinase substrate specificity in
RT vitro and in vivo: control of glycogen biosynthesis by Pcl8 and Pcl10.";
RL Mol. Cell. Biol. 18:3289-3299(1998).
RN [6]
RP FUNCTION, AND INTERACTION WITH GSY2 AND PHO85.
RX PubMed=10490639; DOI=10.1128/mcb.19.10.7020;
RA Wilson W.A., Mahrenholz A.M., Roach P.J.;
RT "Substrate targeting of the yeast cyclin-dependent kinase Pho85p by the
RT cyclin Pcl10p.";
RL Mol. Cell. Biol. 19:7020-7030(1999).
RN [7]
RP FUNCTION.
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 [8]
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 [9]
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: Cyclin partner of the cyclin-dependent kinase (CDK) PHO85.
CC Together with cyclin PCL8, negatively controls glycogen accumulation
CC under favorable growth conditions. The PCL10-PHO85 cyclin-CDK
CC holoenzyme has glycogen synthase kinase activity and phosphorylates and
CC negatively regulates glycogen synthase GSY2. Also has minor GLC8 kinase
CC activity. {ECO:0000269|PubMed:10490639, ECO:0000269|PubMed:12407105,
CC ECO:0000269|PubMed:9584169}.
CC -!- SUBUNIT: Forms a cyclin-CDK complex with PHO85. Interacts with GSY2,
CC independent of the presence of PHO85. {ECO:0000269|PubMed:10490639,
CC ECO:0000269|PubMed:9032248, ECO:0000269|PubMed:9584169}.
CC -!- INTERACTION:
CC P53124; P17157: PHO85; NbExp=6; IntAct=EBI-23973, EBI-13327;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 217 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the cyclin family. PHO80 subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z72656; CAA96845.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07976.1; -; Genomic_DNA.
DR PIR; S64147; S64147.
DR RefSeq; NP_011381.1; NM_001180999.1.
DR PDB; 4KRC; X-ray; 2.60 A; B=227-433.
DR PDB; 4KRD; X-ray; 1.95 A; B=227-433.
DR PDBsum; 4KRC; -.
DR PDBsum; 4KRD; -.
DR AlphaFoldDB; P53124; -.
DR SMR; P53124; -.
DR BioGRID; 33118; 55.
DR ComplexPortal; CPX-1692; PCL10-PHO85 kinase complex.
DR DIP; DIP-1494N; -.
DR IntAct; P53124; 13.
DR MINT; P53124; -.
DR STRING; 4932.YGL134W; -.
DR iPTMnet; P53124; -.
DR MaxQB; P53124; -.
DR PaxDb; P53124; -.
DR PRIDE; P53124; -.
DR EnsemblFungi; YGL134W_mRNA; YGL134W; YGL134W.
DR GeneID; 852743; -.
DR KEGG; sce:YGL134W; -.
DR SGD; S000003102; PCL10.
DR VEuPathDB; FungiDB:YGL134W; -.
DR eggNOG; KOG1674; Eukaryota.
DR GeneTree; ENSGT00390000000862; -.
DR HOGENOM; CLU_043984_0_0_1; -.
DR InParanoid; P53124; -.
DR OMA; DSIFSEC; -.
DR BioCyc; YEAST:G3O-30629-MON; -.
DR PRO; PR:P53124; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53124; 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; IBA:GO_Central.
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:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0045719; P:negative regulation of glycogen biosynthetic process; IMP:SGD.
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; IC:ComplexPortal.
DR InterPro; IPR013922; Cyclin_PHO80-like.
DR PANTHER; PTHR15615; PTHR15615; 1.
DR Pfam; PF08613; Cyclin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cyclin; Cytoplasm;
KW Glycogen metabolism; Reference proteome.
FT CHAIN 1..433
FT /note="PHO85 cyclin-10"
FT /id="PRO_0000202740"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:4KRD"
FT HELIX 262..280
FT /evidence="ECO:0007829|PDB:4KRD"
FT HELIX 291..298
FT /evidence="ECO:0007829|PDB:4KRD"
FT HELIX 310..321
FT /evidence="ECO:0007829|PDB:4KRD"
FT HELIX 325..339
FT /evidence="ECO:0007829|PDB:4KRD"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:4KRD"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:4KRD"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:4KRD"
FT HELIX 359..374
FT /evidence="ECO:0007829|PDB:4KRD"
FT HELIX 381..388
FT /evidence="ECO:0007829|PDB:4KRD"
FT HELIX 392..406
FT /evidence="ECO:0007829|PDB:4KRD"
FT HELIX 415..429
FT /evidence="ECO:0007829|PDB:4KRD"
SQ SEQUENCE 433 AA; 48584 MW; DE6608A34BDBDF99 CRC64;
MDMTKNHTTD TEEFDDGDIR PVSLGIVDDY NASFELPLKP KFLQSENFSD LTSEWDQSRS
NTPGLAEGKT EKAQPCGTTD SSKNRIHVEQ LLESANEMNN YLAQNIENIN NFQVGLLNGG
KGLYSSMGDD SSACINGTNF SSTSNFELSD DELEDTTGCT SSIFDKDLFH QQNGLSIPRR
RSPLFKSPTA SFEIGDATDV EEQDIDDSIF SECSSITSFD MGGLHISLPH DEEEDQEKTK
SESENPLLHG IPVDVEVPHI SVDEALANFK ETIELLLKLS GNRKCTGFNT RVEKKEYSNF
YMKSKPTLSS ADFLKRIQDK CEYQPTVYLV ATFLIDTLFL TRDGNNILQL KLNLQEKEVH
RMIIAAVRLS TKLLEDFVHS HEYFSKVCGI SKRLLTKLEV SLLICVCNTK LMVSNRKLAA
SKLLLNELRS FCV
