SMK1_YEAST
ID SMK1_YEAST Reviewed; 388 AA.
AC P41808; D6W460;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Sporulation-specific mitogen-activated protein kinase SMK1;
DE Short=MAP kinase SMK1;
DE EC=2.7.11.24;
GN Name=SMK1; OrderedLocusNames=YPR054W; ORFNames=YP9499.10;
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], AND FUNCTION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7958885; DOI=10.1101/gad.8.18.2151;
RA Krisak L., Strich R., Winters R.S., Hall J.P., Mallory M.J., Kreitzer D.,
RA Tuan R.S., Winter E.;
RT "SMK1, a developmentally regulated MAP kinase, is required for spore wall
RT assembly in Saccharomyces cerevisiae.";
RL Genes Dev. 8:2151-2161(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 FUNCTION, AND INTERACTION WITH GSC2.
RX PubMed=16116083; DOI=10.1073/pnas.0502324102;
RA Huang L.S., Doherty H.K., Herskowitz I.;
RT "The Smk1p MAP kinase negatively regulates Gsc2p, a 1,3-beta-glucan
RT synthase, during spore wall morphogenesis in Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12431-12436(2005).
CC -!- FUNCTION: Required for spore wall assembly. Required for proper
CC deposition of the two outer layers of the spore wall, the chitosan and
CC dityrosine layers. Negatively regulates GSC2, an alternate catalytic
CC subunit of the 1,3-beta-glucan synthase (GS). Participates in a
CC developmentally regulated signal transduction pathway that coordinates
CC cytodifferentiation events with the transcriptional program.
CC {ECO:0000269|PubMed:16116083, ECO:0000269|PubMed:7958885}.
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=2.7.11.24;
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=2.7.11.24;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by tyrosine and threonine
CC phosphorylation. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with GSC2. {ECO:0000269|PubMed:16116083}.
CC -!- INTERACTION:
CC P41808; P02829: HSP82; NbExp=3; IntAct=EBI-17457, EBI-8659;
CC -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC whose phosphorylation activates the MAP kinases.
CC -!- PTM: Dually phosphorylated on Thr-207 and Tyr-209, which activates the
CC enzyme. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. MAP kinase subfamily. {ECO:0000305}.
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DR EMBL; L35047; AAB59325.1; -; Genomic_DNA.
DR EMBL; Z49219; CAA89172.1; -; Genomic_DNA.
DR EMBL; Z71255; CAA94999.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11476.1; -; Genomic_DNA.
DR PIR; S48879; S48879.
DR RefSeq; NP_015379.1; NM_001184151.1.
DR AlphaFoldDB; P41808; -.
DR SMR; P41808; -.
DR BioGRID; 36228; 63.
DR DIP; DIP-1636N; -.
DR IntAct; P41808; 24.
DR MINT; P41808; -.
DR STRING; 4932.YPR054W; -.
DR iPTMnet; P41808; -.
DR PaxDb; P41808; -.
DR PRIDE; P41808; -.
DR EnsemblFungi; YPR054W_mRNA; YPR054W; YPR054W.
DR GeneID; 856167; -.
DR KEGG; sce:YPR054W; -.
DR SGD; S000006258; SMK1.
DR VEuPathDB; FungiDB:YPR054W; -.
DR eggNOG; KOG0660; Eukaryota.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; P41808; -.
DR OMA; GLYCFQE; -.
DR BioCyc; YEAST:G3O-34206-MON; -.
DR BRENDA; 2.7.11.24; 984.
DR Reactome; R-SCE-193648; NRAGE signals death through JNK.
DR Reactome; R-SCE-198765; Signalling to ERK5.
DR Reactome; R-SCE-202670; ERKs are inactivated.
DR Reactome; R-SCE-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-SCE-2871796; FCERI mediated MAPK activation.
DR Reactome; R-SCE-4086398; Ca2+ pathway.
DR Reactome; R-SCE-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
DR Reactome; R-SCE-450341; Activation of the AP-1 family of transcription factors.
DR Reactome; R-SCE-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-SCE-9007892; Interleukin-38 signaling.
DR PRO; PR:P41808; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P41808; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004707; F:MAP kinase 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:0030476; P:ascospore wall assembly; IMP:SGD.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0042174; P:negative regulation of sporulation resulting in formation of a cellular spore; IGI:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
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; Cell shape; Cell wall biogenesis/degradation; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Sporulation; Transferase.
FT CHAIN 1..388
FT /note="Sporulation-specific mitogen-activated protein
FT kinase SMK1"
FT /id="PRO_0000186339"
FT DOMAIN 38..337
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOTIF 207..209
FT /note="TXY"
FT ACT_SITE 166
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 44..52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 388 AA; 44300 MW; 081BD00B9DBC3F23 CRC64;
MNCTLTDNTR AINVASNLGA PQQRTIFAKE RISIPGYYEI IQFLGKGAYG TVCSVKFKGR
SPAARIAVKK ISNIFNKEIL LKRAIRELKF MNFFKGHKNI VNLIDLEIVT SSPYDGLYCY
QELIDYDLAK VIHSSVQLSE FHIKYFLYQI LCGLKYIHSA DVIHRDLKPG NILCTLNGCL
KICDFGLARG IHAGFFKCHS TVQPHITNYV ATRWYRAPEL LLSNQPYSKS VDIWAVGCIL
AEFYARKPVF MGRDSMHQIF EIIKVLGTPD KDILIKFGTI KAWNLGKNSN NPVYKKIPWS
NIFPFASHEA INLIESLLHW DSTHRLNVEQ AISHPFLNEV RKPDDEPVCL QGPFDFTYES
ELNSMSKLRD YLVEEVKNFK TDLSSSSL
