KPC1_YEAST
ID KPC1_YEAST Reviewed; 1151 AA.
AC P24583; D6VPP8;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=Protein kinase C-like 1;
DE Short=PKC 1;
DE EC=2.7.11.13;
GN Name=PKC1; Synonyms=HPO2, STT1; OrderedLocusNames=YBL105C;
GN ORFNames=YBL0807;
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 [MRNA].
RC STRAIN=ATCC 204278 / EG123 / SM1058;
RX PubMed=2196995; DOI=10.1016/0092-8674(90)90360-q;
RA Levin D.E., Fields F.O., Kunisawa R., Bishop J.M., Thorner J.;
RT "A candidate protein kinase C gene, PKC1, is required for the S. cerevisiae
RT cell cycle.";
RL Cell 62:213-224(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7502586; DOI=10.1002/yea.320111112;
RA Obermaier B., Gassenhuber J., Piravandi E., Domdey H.;
RT "Sequence analysis of a 78.6 kb segment of the left end of Saccharomyces
RT cerevisiae chromosome II.";
RL Yeast 11:1103-1112(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [4]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 81; 621 AND 789.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-761, AND
RP IDENTIFICATION BY 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).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [7]
RP VARIANTS CLY5 AND CLY7.
RX PubMed=9133734;
RX DOI=10.1002/(sici)1097-0061(19970330)13:4<305::aid-yea91>3.0.co;2-f;
RA Baymiller J., McCullough J.E.;
RT "Saccharomyces cerevisiae cell lysis mutations cly5 and cly7 define
RT temperature-sensitive alleles of PKC1, the gene encoding yeast protein
RT kinase C.";
RL Yeast 13:305-312(1997).
CC -!- FUNCTION: Required for cell growth and for the G2->M transition of the
CC cell division cycle. Mediates a protein kinase cascade; it activates
CC BCK1 which itself activates MKK1/MKK2.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.13;
CC -!- INTERACTION:
CC P24583; P06786: TOP2; NbExp=2; IntAct=EBI-9860, EBI-19352;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PKC subfamily. {ECO:0000305}.
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DR EMBL; M32491; AAA34878.1; -; mRNA.
DR EMBL; X79489; CAA55990.1; -; Genomic_DNA.
DR EMBL; Z35866; CAA84932.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07018.2; -; Genomic_DNA.
DR PIR; S45390; S45390.
DR RefSeq; NP_009445.2; NM_001178345.2.
DR AlphaFoldDB; P24583; -.
DR SMR; P24583; -.
DR BioGRID; 32598; 1105.
DR DIP; DIP-1516N; -.
DR IntAct; P24583; 18.
DR MINT; P24583; -.
DR STRING; 4932.YBL105C; -.
DR CarbonylDB; P24583; -.
DR iPTMnet; P24583; -.
DR MaxQB; P24583; -.
DR PaxDb; P24583; -.
DR PRIDE; P24583; -.
DR EnsemblFungi; YBL105C_mRNA; YBL105C; YBL105C.
DR GeneID; 852169; -.
DR KEGG; sce:YBL105C; -.
DR SGD; S000000201; PKC1.
DR VEuPathDB; FungiDB:YBL105C; -.
DR eggNOG; KOG0694; Eukaryota.
DR GeneTree; ENSGT00940000168328; -.
DR HOGENOM; CLU_000288_54_1_1; -.
DR InParanoid; P24583; -.
DR OMA; NRIYFAM; -.
DR BioCyc; YEAST:G3O-28989-MON; -.
DR BRENDA; 2.7.11.13; 984.
DR Reactome; R-SCE-114508; Effects of PIP2 hydrolysis.
DR Reactome; R-SCE-114516; Disinhibition of SNARE formation.
DR Reactome; R-SCE-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-SCE-1489509; DAG and IP3 signaling.
DR Reactome; R-SCE-202424; Downstream TCR signaling.
DR Reactome; R-SCE-2029485; Role of phospholipids in phagocytosis.
DR Reactome; R-SCE-2179392; EGFR Transactivation by Gastrin.
DR Reactome; R-SCE-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-SCE-399997; Acetylcholine regulates insulin secretion.
DR Reactome; R-SCE-4419969; Depolymerisation of the Nuclear Lamina.
DR Reactome; R-SCE-450520; HuR (ELAVL1) binds and stabilizes mRNA.
DR Reactome; R-SCE-5218921; VEGFR2 mediated cell proliferation.
DR Reactome; R-SCE-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-SCE-5625740; RHO GTPases activate PKNs.
DR Reactome; R-SCE-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR Reactome; R-SCE-5668599; RHO GTPases Activate NADPH Oxidases.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-76005; Response to elevated platelet cytosolic Ca2+.
DR Reactome; R-SCE-8980692; RHOA GTPase cycle.
DR Reactome; R-SCE-9013026; RHOB GTPase cycle.
DR Reactome; R-SCE-9013106; RHOC GTPase cycle.
DR Reactome; R-SCE-9634635; Estrogen-stimulated signaling through PRKCZ.
DR PRO; PR:P24583; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P24583; protein.
DR GO; GO:0005935; C:cellular bud neck; HDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
DR GO; GO:0005856; C:cytoskeleton; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR GO; GO:0032165; C:prospore septin filament array; HDA:SGD.
DR GO; GO:0030427; C:site of polarized growth; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004698; F:calcium-dependent protein kinase C activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004697; F:protein kinase C activity; IDA:SGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0030242; P:autophagy of peroxisome; IMP:SGD.
DR GO; GO:0032186; P:cellular bud neck septin ring organization; IMP:SGD.
DR GO; GO:0009272; P:fungal-type cell wall biogenesis; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IMP:SGD.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0010606; P:positive regulation of cytoplasmic mRNA processing body assembly; IMP:SGD.
DR GO; GO:0060237; P:regulation of fungal-type cell wall organization; IMP:SGD.
DR GO; GO:0060211; P:regulation of nuclear-transcribed mRNA poly(A) tail shortening; IMP:SGD.
DR GO; GO:0007165; P:signal transduction; IMP:SGD.
DR GO; GO:0034063; P:stress granule assembly; IDA:SGD.
DR CDD; cd00029; C1; 2.
DR CDD; cd08689; C2_fungal_Pkc1p; 1.
DR CDD; cd11620; HR1_PKC-like_2_fungi; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037778; C2_fungal_PKC.
DR InterPro; IPR011072; HR1_rho-bd.
DR InterPro; IPR036274; HR1_rpt_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR037312; PKC-like_HR1.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF02185; HR1; 2.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00109; C1; 2.
DR SMART; SM00239; C2; 1.
DR SMART; SM00742; Hr1; 2.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF46585; SSF46585; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57889; SSF57889; 2.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS51860; REM_1; 2.
DR PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Calcium; Cell cycle; Coiled coil; Kinase; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1151
FT /note="Protein kinase C-like 1"
FT /id="PRO_0000055738"
FT DOMAIN 1..67
FT /note="REM-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 106..183
FT /note="REM-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 190..309
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 824..1083
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 1084..1151
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ZN_FING 414..461
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 481..531
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 64..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 649..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 782..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..620
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 949
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 830..838
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 853
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 761
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT VARIANT 958
FT /note="T -> I (in cly5; temperature-sensitive mutation that
FT cause cell lysis at high temperature)"
FT VARIANT 1023
FT /note="P -> S (in cly7; temperature-sensitive mutation that
FT cause cell lysis at high temperature)"
FT CONFLICT 81
FT /note="C -> F (in Ref. 2; CAA55990 and 3; CAA84932)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="T -> S (in Ref. 1; AAA34878)"
FT /evidence="ECO:0000305"
FT CONFLICT 606
FT /note="G -> E (in Ref. 1; AAA34878)"
FT /evidence="ECO:0000305"
FT CONFLICT 621
FT /note="R -> K (in Ref. 1; AAA34878, 2; CAA55990 and 3;
FT CAA84932)"
FT /evidence="ECO:0000305"
FT CONFLICT 623
FT /note="S -> P (in Ref. 1; AAA34878)"
FT /evidence="ECO:0000305"
FT CONFLICT 789
FT /note="A -> P (in Ref. 2; CAA55990 and 3; CAA84932)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1151 AA; 131477 MW; 8200EC2A2C6E649E CRC64;
MSFSQLEQNI KKKIAVEENI IRGASALKKK TSNVMVIQKC NTNIREARQN LEYLEDSLKK
LRLKTAQQSQ GENGSEDNER CNSKEYGFLS TKSPNEHIFS RLDLVKYDCP SLAQRIQYML
QQLEFKLQVE KQYQEANTKL TKLYQIDGDQ RSSSAAEGGA MESKYRIQML NKALKKYQAI
NVDFDQFKHQ PNDIMDNQQP KFRRKQLTGV LTIGITAARD VDHIQSPMFA RKPESYVTIK
IDDTIKARTK PSRNDRWSED FQIPVEKGNE IEITVYDKVN DSLIPVAIMW LLLSDIAEEI
RKKKAGQTNE QQGWVNASNI NGGSSLASEE GSTLTSTYSN SAIQSTSAKN VQGENTSTSQ
ISTNSWFVLE PSGQILLTLG FHKSSQIERK QLMGGLHRHG AIINRKEEIF EQHGHHFVQK
SFYNIMCCAY CGDFLRYTGF QCQDCKFLCH KKCYTNVVTK CIAKTSTDTD PDEAKLNHRI
PHRFLPTSNR GTKWCCHCGY ILPWGRHKVR KCSECGIMCH AQCAHLVPDF CGMSMEMANK
ILKTIQDTKR NQEKKKRTVP SAQLGSSIGT ANGSDLSPSK LAERANAPLP PQPRKHDKTP
SPQKVGRDSP TKQHDPIIDK RISLQTHGRE KLNKFIDENE AYLNFTEGAQ QTAEFSSPEK
TLDPTSNRRS LGLTDLSIEH SQTWESKDDL MRDELELWKA QREEMELEIK QDSGEIQEDL
EVDHIDLETK QKLDWENKND FREADLTIDS THTNPFRDMN SETFQIEQDH ASKEVLQETV
SLAPTSTHAS RTTDQQSPQK SQTSTSAKHK KRAAKRRKVS LDNFVLLKVL GKGNFGKVIL
SKSKNTDRLC AIKVLKKDNI IQNHDIESAR AEKKVFLLAT KTKHPFLTNL YCSFQTENRI
YFAMEFIGGG DLMWHVQNQR LSVRRAKFYA AEVLLALKYF HDNGVIYRDL KLENILLTPE
GHIKIADYGL CKDEMWYGNR TSTFCGTPEF MAPEILKEQE YTKAVDWWAF GVLLYQMLLC
QSPFSGDDED EVFNAILTDE PLYPIDMAGE IVQIFQGLLT KDPEKRLGAG PRDADEVMEE
PFFRNINFDD ILNLRVKPPY IPEIKSPEDT SYFEQEFTSA PPTLTPLPSV LTTSQQEEFR
GFSFMPDDLD L
