RCK2_YEAST
ID RCK2_YEAST Reviewed; 610 AA.
AC P38623; D6VYP6; Q02532; Q06557;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 3.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Serine/threonine-protein kinase RCK2;
DE EC=2.7.11.1;
DE AltName: Full=CAM kinase-like protein kinase CLK1;
GN Name=RCK2; Synonyms=CLK1, CMK3; OrderedLocusNames=YLR248W;
GN ORFNames=L9672.6;
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 204510 / AB320;
RX PubMed=8112585; DOI=10.1016/0378-1119(94)90519-3;
RA Dahlkvist A., Sunnerhagen P.;
RT "Two novel deduced serine/threonine protein kinases from Saccharomyces
RT cerevisiae.";
RL Gene 139:27-33(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=YNN 214;
RX PubMed=8939941; DOI=10.1074/jbc.271.47.29958;
RA Melcher M.L., Thorner J.;
RT "Identification and characterization of the CLK1 gene product, a novel CaM
RT kinase-like protein kinase from the yeast Saccharomyces cerevisiae.";
RL J. Biol. Chem. 271:29958-29968(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 FUNCTION, PHOSPHORYLATION AT SER-520, ACTIVITY REGULATION, AND INTERACTION
RP WITH HOG1.
RX PubMed=10805732; DOI=10.1128/mcb.20.11.3887-3895.2000;
RA Bilsland-Marchesan E., Arino J., Saito H., Sunnerhagen P., Posas F.;
RT "Rck2 kinase is a substrate for the osmotic stress-activated mitogen-
RT activated protein kinase Hog1.";
RL Mol. Cell. Biol. 20:3887-3895(2000).
RN [6]
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 [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-350, 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).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46; SER-50 AND SER-187, AND
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).
CC -!- FUNCTION: Serine/threonine-protein kinase involved in a signal
CC transduction pathway that is activated by changes in the osmolarity of
CC the extracellular environment. {ECO:0000269|PubMed:10805732}.
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=2.7.11.1;
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=2.7.11.1;
CC -!- ACTIVITY REGULATION: Activated by Ser-520 phosphorylation by HOG1.
CC {ECO:0000269|PubMed:10805732}.
CC -!- INTERACTION:
CC P38623; P32485: HOG1; NbExp=4; IntAct=EBI-14885, EBI-8437;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- PTM: Autophosphorylated. Phosphorylated by HOG1 at Ser-520 after
CC osmotic stress. {ECO:0000269|PubMed:10805732}.
CC -!- MISCELLANEOUS: Present with 1790 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CaMK subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA50389.1; Type=Frameshift; Evidence={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; X71065; CAA50389.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U23464; AAA64421.1; -; Genomic_DNA.
DR EMBL; U20865; AAB67392.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09562.1; -; Genomic_DNA.
DR PIR; S59394; S59394.
DR RefSeq; NP_013349.1; NM_001182135.1.
DR AlphaFoldDB; P38623; -.
DR SMR; P38623; -.
DR BioGRID; 31516; 137.
DR DIP; DIP-5079N; -.
DR IntAct; P38623; 11.
DR MINT; P38623; -.
DR STRING; 4932.YLR248W; -.
DR iPTMnet; P38623; -.
DR MaxQB; P38623; -.
DR PaxDb; P38623; -.
DR PRIDE; P38623; -.
DR EnsemblFungi; YLR248W_mRNA; YLR248W; YLR248W.
DR GeneID; 850950; -.
DR KEGG; sce:YLR248W; -.
DR SGD; S000004238; RCK2.
DR VEuPathDB; FungiDB:YLR248W; -.
DR eggNOG; KOG0032; Eukaryota.
DR GeneTree; ENSGT00940000176587; -.
DR HOGENOM; CLU_006421_3_0_1; -.
DR InParanoid; P38623; -.
DR OMA; MAAIQNF; -.
DR BioCyc; YEAST:G3O-32353-MON; -.
DR BRENDA; 2.7.11.1; 984.
DR Reactome; R-SCE-9619229; Activation of RAC1 downstream of NMDARs.
DR PRO; PR:P38623; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P38623; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; HDA:SGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:SGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
DR GO; GO:0007231; P:osmosensory signaling pathway; IMP:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IDA:SGD.
DR GO; GO:0040020; P:regulation of meiotic nuclear division; IMP:SGD.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Calmodulin-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..610
FT /note="Serine/threonine-protein kinase RCK2"
FT /id="PRO_0000086604"
FT DOMAIN 163..478
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..506
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000255"
FT REGION 541..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 313
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 169..177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 350
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10805732"
FT CONFLICT 109
FT /note="S -> N (in Ref. 1; CAA50389 and 2; AAA64421)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="N -> H (in Ref. 1; CAA50389 and 2; AAA64421)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="V -> A (in Ref. 1; CAA50389 and 2; AAA64421)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="R -> P (in Ref. 1; CAA50389 and 2; AAA64421)"
FT /evidence="ECO:0000305"
FT CONFLICT 456
FT /note="A -> S (in Ref. 1; CAA50389 and 2; AAA64421)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 610 AA; 68062 MW; 00DDC674F6723E6A CRC64;
MLKIKALFSK KKPDQADLSQ ESKKPFKGKT RSSGTNNKDV SQITSSPKKS FQDKNIVQYP
SVVADDHHMK SLTDELVTTI DSDSSPSDNI TTENVETVTS VPAIDVHESS EGQLSSDPLI
SDESLSEQSE IISDIQDDST DDDNMEDEIP EKSFLEQKEL IGYKLINKIG EGAFSKVFRA
IPAKNSSNEF LTKNYKAVAI KVIKKADLSS INGDHRKKDK GKDSTKTSSR DQVLKEVALH
KTVSAGCSQI VAFIDFQETD SYYYIIQELL TGGEIFGEIV RLTYFSEDLS RHVIKQLALA
VKHMHSLGVV HRDIKPENLL FEPIEFTRSI KPKLRKSDDP QTKADEGIFT PGVGGGGIGI
VKLADFGLSK QIFSKNTKTP CGTVGYTAPE VVKDEHYSMK VDMWGIGCVL YTMLCGFPPF
YDEKIDTLTE KISRGEYTFL KPWWDEISAG AKNAVAKLLE LEPSKRYDID QFLDDPWLNT
FDCLPKEGES SQKKAGTSER RHPHKKQFQL FQRDSSLLFS PAAVAMRDAF DIGNAVKRTE
EDRMGTRGGL GSLAEDEELE DSYSGAQGDE QLEQNMFQLT LDTSTILQRR KKVQENDVGP
TIPISATIRE
