MPS1_MAGO7
ID MPS1_MAGO7 Reviewed; 415 AA.
AC G4N374;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Mitogen-activated protein kinase MPS1 {ECO:0000303|PubMed:9770551};
DE Short=MAPK MPS1 {ECO:0000303|PubMed:9770551};
DE EC=2.7.11.24 {ECO:0000269|PubMed:9770551};
GN Name=MPS1 {ECO:0000303|PubMed:9770551}; ORFNames=MGG_04943;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9770551; DOI=10.1073/pnas.95.21.12713;
RA Xu J.R., Staiger C.J., Hamer J.E.;
RT "Inactivation of the mitogen-activated protein kinase Mps1 from the rice
RT blast fungus prevents penetration of host cells but allows activation of
RT plant defense responses.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:12713-12718(1998).
RN [3]
RP FUNCTION, AND INTERACTION WITH MIG1.
RX PubMed=18344407; DOI=10.1128/ec.00009-08;
RA Mehrabi R., Ding S., Xu J.R.;
RT "MADS-box transcription factor mig1 is required for infectious growth in
RT Magnaporthe grisea.";
RL Eukaryot. Cell 7:791-799(2008).
RN [4]
RP FUNCTION, AND INTERACTION WITH SWI6.
RX PubMed=22321443; DOI=10.1111/j.1364-3703.2011.00779.x;
RA Qi Z., Wang Q., Dou X., Wang W., Zhao Q., Lv R., Zhang H., Zheng X.,
RA Wang P., Zhang Z.;
RT "MoSwi6, an APSES family transcription factor, interacts with MoMps1 and is
RT required for hyphal and conidial morphogenesis, appressorial function and
RT pathogenicity of Magnaporthe oryzae.";
RL Mol. Plant Pathol. 13:677-689(2012).
RN [5]
RP FUNCTION.
RX PubMed=28799700; DOI=10.1111/1462-2920.13884;
RA Zhang X., Liu W., Li Y., Li G., Xu J.R.;
RT "Expression of HopAI interferes with MAP kinase signalling in Magnaporthe
RT oryzae.";
RL Environ. Microbiol. 19:4190-4204(2017).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28424497; DOI=10.1038/s41598-017-01006-w;
RA Zhou T., Dagdas Y.F., Zhu X., Zheng S., Chen L., Cartwright Z.,
RA Talbot N.J., Wang Z.;
RT "The glycogen synthase kinase MoGsk1, regulated by Mps1 MAP kinase, is
RT required for fungal development and pathogenicity in Magnaporthe oryzae.";
RL Sci. Rep. 7:945-945(2017).
RN [7]
RP ERRATUM OF PUBMED:28424497.
RX PubMed=31959847; DOI=10.1038/s41598-020-58148-7;
RA Zhou T., Dagdas Y.F., Zhu X., Zheng S., Chen L., Cartwright Z.,
RA Talbot N.J., Wang Z.;
RT "Publisher correction: The glycogen synthase kinase MoGsk1, regulated by
RT Mps1 MAP kinase, is required for fungal development and pathogenicity in
RT Magnaporthe oryzae.";
RL Sci. Rep. 10:1187-1187(2020).
RN [8] {ECO:0007744|PDB:5Z33}
RP X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS).
RA Zhou F., Peng J.B., Zhao Y.X., Chen X., Zhang Y.Y., Peng Y.L., Liu J.F.,
RA Zhang G.Z.;
RT "Crystal structure of Mitogen-activated Protein Kinase Mps1 in Magnaporthe
RT oryzae.";
RL Submitted (JAN-2018) to the PDB data bank.
CC -!- FUNCTION: Mitogen-activated protein kinase; part of the MCK1-MKK2-MPS1
CC MAP kinase (MAPK) signal transduction cascade that is essential for
CC cell wall integrity and plant infection, but not for plant defense
CC responses (PubMed:9770551, PubMed:18344407, PubMed:22321443,
CC PubMed:28799700, PubMed:28424497). Beside its role in pathogenesis, the
CC MPS1 cascade is active in conidiation and cellular stress responses
CC (PubMed:9770551). Targets downstream of the MPS1-MAPK pathway include
CC transcription factors MIG1 and SWI6, as well as GSK1 and MPG1
CC (PubMed:18344407, PubMed:22321443, PubMed:28424497).
CC {ECO:0000269|PubMed:18344407, ECO:0000269|PubMed:22321443,
CC ECO:0000269|PubMed:28424497, ECO:0000269|PubMed:28799700,
CC ECO:0000269|PubMed:9770551}.
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 Evidence={ECO:0000305|PubMed:9770551};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000305|PubMed:9770551};
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; Evidence={ECO:0000305|PubMed:9770551};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000305|PubMed:9770551};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|RuleBase:RU361165};
CC -!- SUBUNIT: Interacts with transcription factor MIG1 (PubMed:18344407).
CC Interacts with transcription factor SWI6 (PubMed:22321443).
CC {ECO:0000269|PubMed:18344407, ECO:0000269|PubMed:22321443}.
CC -!- DISRUPTION PHENOTYPE: Leads to sensitivity to cell-wall-digesting
CC enzymes, as well as reduced sporulation and fertility (PubMed:9770551).
CC Abolishes pathogenicity by blocking the penetration of appressoria into
CC plant cell surfaces (PubMed:9770551). Does not affect the ability to
CC trigger early plant-cell defense responses (PubMed:9770551). Affects
CC the expression of MPG1 and GSK1 (PubMed:28424497).
CC {ECO:0000269|PubMed:28424497, ECO:0000269|PubMed:9770551}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. MAP kinase subfamily. {ECO:0000305}.
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DR EMBL; CM001233; EHA52630.1; -; Genomic_DNA.
DR RefSeq; XP_003712437.1; XM_003712389.1.
DR PDB; 5Z33; X-ray; 1.99 A; A=1-415.
DR PDBsum; 5Z33; -.
DR AlphaFoldDB; G4N374; -.
DR SMR; G4N374; -.
DR STRING; 318829.MGG_04943T0; -.
DR EnsemblFungi; MGG_04943T0; MGG_04943T0; MGG_04943.
DR GeneID; 2675515; -.
DR KEGG; mgr:MGG_04943; -.
DR VEuPathDB; FungiDB:MGG_04943; -.
DR eggNOG; KOG0660; Eukaryota.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; G4N374; -.
DR OMA; MDIPRPE; -.
DR OrthoDB; 741207at2759; -.
DR Proteomes; UP000009058; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004707; F:MAP kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0000196; P:cell wall integrity MAPK cascade; IEA:EnsemblFungi.
DR GO; GO:1902660; P:negative regulation of glucose mediated signaling pathway; IEA:EnsemblFungi.
DR GO; GO:1902413; P:negative regulation of mitotic cytokinesis; IEA:EnsemblFungi.
DR GO; GO:1905665; P:positive regulation of calcium ion import across plasma membrane; IEA:EnsemblFungi.
DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IEA:EnsemblFungi.
DR GO; GO:0051094; P:positive regulation of developmental process; IEA:UniProt.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003527; MAP_kinase_CS.
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; PS01351; MAPK; 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 3D-structure; ATP-binding; Kinase; Magnesium; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Virulence.
FT CHAIN 1..415
FT /note="Mitogen-activated protein kinase MPS1"
FT /id="PRO_0000453093"
FT DOMAIN 23..314
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 363..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 29..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:5Z33"
FT STRAND 15..20
FT /evidence="ECO:0007829|PDB:5Z33"
FT STRAND 23..31
FT /evidence="ECO:0007829|PDB:5Z33"
FT STRAND 33..42
FT /evidence="ECO:0007829|PDB:5Z33"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:5Z33"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:5Z33"
FT HELIX 61..76
FT /evidence="ECO:0007829|PDB:5Z33"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:5Z33"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:5Z33"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:5Z33"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:5Z33"
FT HELIX 111..117
FT /evidence="ECO:0007829|PDB:5Z33"
FT HELIX 123..142
FT /evidence="ECO:0007829|PDB:5Z33"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:5Z33"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:5Z33"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:5Z33"
FT HELIX 179..183
FT /evidence="ECO:0007829|PDB:5Z33"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:5Z33"
FT HELIX 197..200
FT /evidence="ECO:0007829|PDB:5Z33"
FT HELIX 209..224
FT /evidence="ECO:0007829|PDB:5Z33"
FT HELIX 234..245
FT /evidence="ECO:0007829|PDB:5Z33"
FT HELIX 250..254
FT /evidence="ECO:0007829|PDB:5Z33"
FT HELIX 259..267
FT /evidence="ECO:0007829|PDB:5Z33"
FT HELIX 276..279
FT /evidence="ECO:0007829|PDB:5Z33"
FT HELIX 285..294
FT /evidence="ECO:0007829|PDB:5Z33"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:5Z33"
FT HELIX 305..309
FT /evidence="ECO:0007829|PDB:5Z33"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:5Z33"
FT TURN 315..317
FT /evidence="ECO:0007829|PDB:5Z33"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:5Z33"
FT HELIX 333..336
FT /evidence="ECO:0007829|PDB:5Z33"
FT HELIX 340..358
FT /evidence="ECO:0007829|PDB:5Z33"
FT HELIX 396..408
FT /evidence="ECO:0007829|PDB:5Z33"
SQ SEQUENCE 415 AA; 46993 MW; F149D7258145E2EA CRC64;
MSDLQGRKIF KVFNQDFIVD ERYTVTKELG QGAYGIVCAA VNNQTSEGVA IKKVTNVFSK
KILAKRALRE IKLLQHFRGH RNITCLYDMD IPRPDNFNET YLYEELMECD LAAIIRSGQP
LTDAHFQSFI YQILCGLKYI HSANVLHRDL KPGNLLVNAD CELKICDFGL ARGFSVDPEE
NAGYMTEYVA TRWYRAPEIM LSFQSYTKAI DVWSVGCILA ELLGGRPFFK GRDYVDQLNQ
ILHILGTPNE ETLSRIGSPR AQEYVRNLPF MAKKPFPTLF PNANPDALDL LDRMLAFDPS
SRISVEQALE HPYLHIWHDA SDEPDCPTTF NFDFEVVEDV GEMRKMILDE VYRFRQLVRT
APGAGGHGAP HAPQVPIPAG AGQGQWKAED PRPQEYVGQM NDLEAELAGG LDQRR
