MPS1_MAGOR
ID MPS1_MAGOR Reviewed; 415 AA.
AC O13352;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 151.
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; ORFNames=PgNI_01373;
OS Magnaporthe oryzae (Rice blast fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=318829;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Guyane 11;
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NI907;
RX PubMed=30835262; DOI=10.1093/molbev/msz045;
RA Gomez Luciano L.B., Tsai I.J., Chuma I., Tosa Y., Chen Y.H., Li J.Y.,
RA Li M.Y., Lu M.J., Nakayashiki H., Li W.H.;
RT "Blast fungal genomes show frequent chromosomal changes, gene gains and
RT losses, and effector gene turnover.";
RL Mol. Biol. Evol. 36:1148-1161(2019).
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).
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; AF020316; AAC63682.1; -; Genomic_DNA.
DR AlphaFoldDB; O13352; -.
DR SMR; O13352; -.
DR OMA; MDIPRPE; -.
DR PHI-base; PHI:113; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004707; F:MAP kinase activity; IEA:UniProtKB-EC.
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 ATP-binding; Kinase; Magnesium; Nucleotide-binding;
KW Serine/threonine-protein kinase; Transferase; Virulence.
FT CHAIN 1..415
FT /note="Mitogen-activated protein kinase MPS1"
FT /id="PRO_0000453094"
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"
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
