ID HOG1_YARLI Reviewed; 386 AA. AC Q6C4M9; DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2004, sequence version 1. DT 27-MAR-2024, entry version 124. DE RecName: Full=Mitogen-activated protein kinase HOG1; DE Short=MAP kinase HOG1; DE EC=2.7.11.24; GN Name=HOG1; OrderedLocusNames=YALI0E25135g; OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Dipodascaceae; Yarrowia. OX NCBI_TaxID=284591; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CLIB 122 / E 150; RX PubMed=15229592; DOI=10.1038/nature02579; RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S., RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., RA Weissenbach J., Wincker P., Souciet J.-L.; RT "Genome evolution in yeasts."; RL Nature 430:35-44(2004). 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 -!- 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; CR382131; CAG79982.1; -; Genomic_DNA. DR RefSeq; XP_504383.1; XM_504383.1. DR AlphaFoldDB; Q6C4M9; -. DR SMR; Q6C4M9; -. DR STRING; 284591.Q6C4M9; -. DR EnsemblFungi; CAG79982; CAG79982; YALI0_E25135g. DR GeneID; 2912707; -. DR KEGG; yli:YALI0E25135g; -. DR VEuPathDB; FungiDB:YALI0_E25135g; -. DR HOGENOM; CLU_000288_181_1_1; -. DR InParanoid; Q6C4M9; -. DR OMA; NRYTDLN; -. DR OrthoDB; 158564at2759; -. DR Proteomes; UP000001300; Chromosome E. DR GO; GO:0000785; C:chromatin; IEA:EnsemblFungi. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:EnsemblFungi. 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; IEA:UniProtKB-EC. 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:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IEA:EnsemblFungi. DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central. DR GO; GO:1990625; P:negative regulation of cytoplasmic translational initiation in response to stress; IEA:EnsemblFungi. DR GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; IEA:EnsemblFungi. DR GO; GO:0010515; P:negative regulation of induction of conjugation with cellular fusion; IEA:EnsemblFungi. DR GO; GO:0007231; P:osmosensory signaling pathway; IBA:GO_Central. DR GO; GO:0038066; P:p38MAPK cascade; IEA:EnsemblFungi. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IEA:EnsemblFungi. DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IEA:EnsemblFungi. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:EnsemblFungi. DR GO; GO:1903715; P:regulation of aerobic respiration; IEA:EnsemblFungi. DR GO; GO:0051445; P:regulation of meiotic cell cycle; IEA:EnsemblFungi. DR GO; GO:0010520; P:regulation of reciprocal meiotic recombination; IEA:EnsemblFungi. DR GO; GO:0051403; P:stress-activated MAPK cascade; IBA:GO_Central. DR CDD; cd07856; STKc_Sty1_Hog1; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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 PANTHER; PTHR24055; MITOGEN-ACTIVATED PROTEIN KINASE; 1. DR PANTHER; PTHR24055:SF158; MITOGEN-ACTIVATED PROTEIN KINASE P38A-RELATED; 1. DR Pfam; PF00069; Pkinase; 1. DR PRINTS; PR01773; P38MAPKINASE. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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..386 FT /note="Mitogen-activated protein kinase HOG1" FT /id="PRO_0000289709" FT DOMAIN 20..299 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 349..386 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 171..173 FT /note="TXY" FT COMPBIAS 349..365 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" 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 386 AA; 44482 MW; D7026B1E6774CDB2 CRC64; MADFIRTQIF GTCFEITSRY VDLNPVGMGA FGLVCSAKDQ LTDQNVAIKK IMKPFGTPVL SKRTYRELKL LKHLRHENLI CLSDIFISPL EDIYFVTELL GTDLHRLLMT RPLEKQFIQY FLYQILRGLK YVHSAGVVHR DLKPSNILVN ENCDLKICDF GLARIQDTQM TGYVSTRYYR APEIMLTWQK YDVEVDIWST GCIFAEMLEG KPLFPGKDHV HQFSIITELL GSPPEDVIHT ICSENTLRFV RTLPRRERIP LASKFRNADP EAIDLMEKML VFDPKKRITA AEALAHPYLA PYHDPSDEPV AEERFDWSFN DADLPVDTWK VMMYSEILDF HNVDIDVNGQ PPQGQFEQVH AQAQAAVAQN EAARAREQEQ QQQEQQ //