HOG1_MAGO7
ID HOG1_MAGO7 Reviewed; 357 AA.
AC Q9UV51; G4MW71;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Mitogen-activated protein kinase HOG1;
DE Short=MAP kinase HOG1;
DE EC=2.7.11.24;
DE AltName: Full=Osmotic stress MAP kinase;
GN Name=HOG1; Synonyms=OSM1; ORFNames=MGG_01822;
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 [GENOMIC DNA], AND FUNCTION.
RC STRAIN=Guyane 11;
RX PubMed=10521531; DOI=10.2307/3871096;
RA Dixon K.P., Xu J.-R., Smirnoff N., Talbot N.J.;
RT "Independent signaling pathways regulate cellular turgor during
RT hyperosmotic stress and appressorium-mediated plant infection by
RT Magnaporthe grisea.";
RL Plant Cell 11:2045-2058(1999).
RN [2]
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).
CC -!- FUNCTION: Mitogen-activated protein kinase involved in a signal
CC transduction pathway that is activated by changes in the osmolarity of
CC the extracellular environment. Controls osmotic regulation of
CC transcription of target genes (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:10521531}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC whose phosphorylation activates the MAP kinases.
CC -!- PTM: Dually phosphorylated on Thr-171 and Tyr-173, which activates the
CC enzyme. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. MAP kinase subfamily. HOG1 sub-subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00159}.
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; AF184980; AAF09475.1; -; Genomic_DNA.
DR EMBL; CM001232; EHA55031.1; -; Genomic_DNA.
DR RefSeq; XP_003714838.1; XM_003714790.1.
DR AlphaFoldDB; Q9UV51; -.
DR SMR; Q9UV51; -.
DR STRING; 318829.MGG_01822T0; -.
DR EnsemblFungi; MGG_01822T0; MGG_01822T0; MGG_01822.
DR GeneID; 2679641; -.
DR KEGG; mgr:MGG_01822; -.
DR VEuPathDB; FungiDB:MGG_01822; -.
DR eggNOG; KOG0660; Eukaryota.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; Q9UV51; -.
DR OMA; YTDLNPV; -.
DR OrthoDB; 683132at2759; -.
DR PHI-base; PHI:153; -.
DR Proteomes; UP000009058; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0051094; P:positive regulation of developmental process; IEA:UniProt.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0051403; P:stress-activated MAPK cascade; IEA:InterPro.
DR CDD; cd07856; STKc_Sty1_Hog1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003527; MAP_kinase_CS.
DR InterPro; IPR008352; MAPK_p38-like.
DR InterPro; IPR038783; MAPK_Sty1/Hog1.
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 PRINTS; PR01773; P38MAPKINASE.
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 3: Inferred from homology;
KW Activator; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transcription; Transcription regulation; Transferase.
FT CHAIN 1..357
FT /note="Mitogen-activated protein kinase HOG1"
FT /id="PRO_0000289695"
FT DOMAIN 20..299
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOTIF 171..173
FT /note="TXY"
FT ACT_SITE 141
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 26..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 171
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 173
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 357 AA; 41145 MW; 130F823ADF084F89 CRC64;
MAEFVRAQIF GTTFEITSRY SDLQPVGMGA FGLVCSARDQ LTNQNVAIKK IMKPFSTPVL
AKRTYRELKL LKHLKHENVI SLSDIFISPL EDIYFVTELL GTDLHRLLTS RPLEKQFIQY
FLYQIMRGLK YVHSAGVVHR DLKPSNILVN ENCDLKICDF GLARIQDPQM TGYVSTRYYR
APEIMLTWQK YDVEVDIWSA GCIFAEMLEG KPLFPGKDHV NQFSIITELL GTPPDDVINT
IASENTLRFV KSLPKRERQP LKNKFKNADP SAIDLLERML VFDPKKRITA TEALAHEYLT
PYHDPTDEPI AEEKFDWSFN DADLPVDTWK IMMYSEILDY HNAEAGMQQM DDQFTGQ
