HOG1_EMENI
ID HOG1_EMENI Reviewed; 379 AA.
AC Q9P419; C8VU47; Q5BEL3; Q9P454;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Mitogen-activated protein kinase hog1;
DE Short=MAP kinase hog1;
DE EC=2.7.11.24;
GN Name=hog1; Synonyms=hogA, sakA; ORFNames=AN1017;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Han K., Prade R.A.;
RT "The Aspergillus nidulans hogA MAP kinase gene, homologous to the yeast
RT HOG1 gene, is regulated by salt stress.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PHOSPHORYLATION.
RX PubMed=12180932; DOI=10.1046/j.1365-2958.2002.03087.x;
RA Kawasaki L., Sanchez O., Shiozaki K., Aguirre J.;
RT "SakA MAP kinase is involved in stress signal transduction, sexual
RT development and spore viability in Aspergillus nidulans.";
RL Mol. Microbiol. 45:1153-1163(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [5]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=15882418; DOI=10.1111/j.1365-2958.2005.04605.x;
RA Furukawa K., Hoshi Y., Maeda T., Nakajima T., Abe K.;
RT "Aspergillus nidulans HOG pathway is activated only by two-component
RT signalling pathway in response to osmotic stress.";
RL Mol. Microbiol. 56:1246-1261(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. {ECO:0000269|PubMed:12180932,
CC ECO:0000269|PubMed:15882418}.
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 (By similarity). Phosphorylated by pbsB in response to osmotic
CC and oxidative stresses. {ECO:0000250, ECO:0000269|PubMed:12180932,
CC ECO:0000269|PubMed:15882418}.
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}.
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DR EMBL; AF270498; AAF81523.1; -; Genomic_DNA.
DR EMBL; AF282891; AAF97243.1; -; Genomic_DNA.
DR EMBL; AACD01000015; EAA65585.1; -; Genomic_DNA.
DR EMBL; BN001308; CBF88327.1; -; Genomic_DNA.
DR RefSeq; XP_658621.1; XM_653529.1.
DR AlphaFoldDB; Q9P419; -.
DR SMR; Q9P419; -.
DR STRING; 162425.CADANIAP00001630; -.
DR EnsemblFungi; CBF88327; CBF88327; ANIA_01017.
DR EnsemblFungi; EAA65585; EAA65585; AN1017.2.
DR GeneID; 2876793; -.
DR KEGG; ani:AN1017.2; -.
DR VEuPathDB; FungiDB:AN1017; -.
DR eggNOG; KOG0660; Eukaryota.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; Q9P419; -.
DR OMA; YTDLNPV; -.
DR OrthoDB; 683132at2759; -.
DR Proteomes; UP000000560; Chromosome VIII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:AspGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004707; F:MAP kinase activity; ISA:AspGD.
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:0071474; P:cellular hyperosmotic response; IMP:AspGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IDA:AspGD.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:AspGD.
DR GO; GO:0006972; P:hyperosmotic response; ISA:AspGD.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0007231; P:osmosensory signaling pathway; IMP:AspGD.
DR GO; GO:0006468; P:protein phosphorylation; ISA:AspGD.
DR GO; GO:0051403; P:stress-activated MAPK cascade; IBA:GO_Central.
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 Activator; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transcription; Transcription regulation; Transferase.
FT CHAIN 1..379
FT /note="Mitogen-activated protein kinase hog1"
FT /id="PRO_0000289687"
FT DOMAIN 20..313
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"
FT CONFLICT 132
FT /note="V -> C (in Ref. 1; AAF81523)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 379 AA; 43183 MW; 93DB6A450ECAB8E5 CRC64;
MAEFVRAQIF GTTFEITSRY TDLQPVGMGA FGLVCSARDQ LTAQPVAVKK IMKPFSTPVL
SKRTYRELKL LKHLRHENII SLSDIFISPL EDIYFVTELL GTDLHRLISS RPLEKQFIQY
FLYQIMRGLK YVHSAGVVHR DLKPSNILIN ENCDLKICDF GLARIQDPQM TGYVSTRYYR
APEIMLTWQK YDAKVDVWSA ACIFAEMLLG APLFPGKDHV NQFSIITELL GTPPDDVIQT
ICSENTLRFV KSLPKREPQD LAKLPKFLAL VHPDKKPEED EDYKNTINLL KAMLVYNPKD
RISAEAALAA PYLAPYHDET DEPVAEEKFD WSFNDADLPV DTWKIMMYSE ILDFHNIDQG
GDINPALVEG AGLNQQGFQ
