ID   HOG2_ZYGRO              Reviewed;         420 AA.
AC   O59853;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   RecName: Full=Mitogen-activated protein kinase HOG2;
DE            Short=MAP kinase HOG2;
DE            EC=2.7.11.24;
DE   AltName: Full=ZrHOG2;
GN   Name=HOG2;
OS   Zygosaccharomyces rouxii (Candida mogii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX   NCBI_TaxID=4956;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 42981 / IAM 12879 / JCM 22060 / S-96;
RX   PubMed=10206704; DOI=10.1099/13500872-145-1-241;
RA   Iwaki T., Tamai Y., Watanabe Y.;
RT   "Two putative MAP kinase genes, ZrHOG1 and ZrHOG2, cloned from the salt-
RT   tolerant yeast Zygosaccharomyces rouxii are functionally homologous to the
RT   Saccharomyces cerevisiae HOG1 gene.";
RL   Microbiology 145:241-248(1999).
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:10206704}.
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-174 and Tyr-176, 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}.
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DR   EMBL; AB012088; BAA25143.1; -; Genomic_DNA.
DR   AlphaFoldDB; O59853; -.
DR   SMR; O59853; -.
DR   eggNOG; KOG0660; Eukaryota.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0051403; P:stress-activated MAPK cascade; IEA:InterPro.
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; 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   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; Serine/threonine-protein kinase; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN           1..420
FT                   /note="Mitogen-activated protein kinase HOG2"
FT                   /id="PRO_0000289711"
FT   REGION          372..394
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           174..176
FT                   /note="TXY"
FT   COMPBIAS        373..394
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        144
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
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   MOD_RES         174
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         176
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   420 AA;  47593 MW;  C24E97A8EBD3EBAA CRC64;
     MATHEEFIRT QVFGTVFEIT NRYTDLNPVG MGAFGLVCSA TDTLVGQPVA IKKIMKPFST
     AVLAKRTYRE LKLLKHLRHE NLICLQDIFL SPLEDIYFVT ELQGTDLHRL LQTRPLEKQF
     VQYFLYQILR GLKYVHSAGV IHRDLKPSNI LINENCDLKI CDFGLARIQD PQMTGYVSTR
     YYRAPEIMLT WQKYDVEVDI WSAGCIFSEM IEGKPLFPGK DHVHQFSIIT DLLGSPPRDV
     INTICSENTL KFVTSLPHRD PVPFQERFKT VEPDAVDLLR RMLVFVPKKR ITAADALVHP
     YLAPYHDPTD EPTAEAQFDW DFNDADLPVD TWRVMMYSEI LDFHKIGGGD GQIDTNAAFD
     DQVAAAHAAA MAQHHHQTQQ QSSGKHTNPT TSSSAATITV TVPIAITMPS LIMVIKRFTT
//