HOG1_CANGA
ID HOG1_CANGA Reviewed; 447 AA.
AC Q6FIU2;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Mitogen-activated protein kinase HOG1;
DE Short=MAP kinase HOG1;
DE EC=2.7.11.24;
GN Name=HOG1; OrderedLocusNames=CAGL0M11748g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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-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; CR380959; CAG62832.1; -; Genomic_DNA.
DR RefSeq; XP_449852.1; XM_449852.1.
DR AlphaFoldDB; Q6FIU2; -.
DR SMR; Q6FIU2; -.
DR STRING; 5478.XP_449852.1; -.
DR EnsemblFungi; CAG62832; CAG62832; CAGL0M11748g.
DR GeneID; 2891247; -.
DR KEGG; cgr:CAGL0M11748g; -.
DR CGD; CAL0136993; HOG1.
DR VEuPathDB; FungiDB:CAGL0M11748g; -.
DR eggNOG; KOG0660; Eukaryota.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; Q6FIU2; -.
DR OMA; YTDLNPV; -.
DR PHI-base; PHI:4625; -.
DR PHI-base; PHI:8395; -.
DR Proteomes; UP000002428; Chromosome M.
DR GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:EnsemblFungi.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IDA:CGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:EnsemblFungi.
DR GO; GO:0003682; F:chromatin binding; IEA:EnsemblFungi.
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:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IEA:EnsemblFungi.
DR GO; GO:0043966; P:histone H3 acetylation; IEA:EnsemblFungi.
DR GO; GO:0006972; P:hyperosmotic response; IEA:EnsemblFungi.
DR GO; GO:1990625; P:negative regulation of cytoplasmic translational initiation in response to stress; IEA:EnsemblFungi.
DR GO; GO:0001100; P:negative regulation of exit from mitosis; 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; IEA:EnsemblFungi.
DR GO; GO:0038066; P:p38MAPK cascade; IEA:EnsemblFungi.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IEA:EnsemblFungi.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IEA:EnsemblFungi.
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:0036091; P:positive regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IEA:EnsemblFungi.
DR GO; GO:1903715; P:regulation of aerobic respiration; IEA:EnsemblFungi.
DR GO; GO:0016241; P:regulation of macroautophagy; IEA:EnsemblFungi.
DR GO; GO:0051445; P:regulation of meiotic cell cycle; IEA:EnsemblFungi.
DR GO; GO:0033262; P:regulation of nuclear cell cycle DNA replication; IEA:EnsemblFungi.
DR GO; GO:0010520; P:regulation of reciprocal meiotic recombination; IEA:EnsemblFungi.
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..447
FT /note="Mitogen-activated protein kinase HOG1"
FT /id="PRO_0000186329"
FT DOMAIN 23..302
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 394..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 174..176
FT /note="TXY"
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 447 AA; 50111 MW; 9721E7EC5C05EF4F CRC64;
MATNEEFIRT QIFGTVFEIT NRYSDLNPVG MGAFGLVCSA TDTLTNQQVA IKKIMKPFAT
AVLAKRTYRE LKLLKHLRHE NLICLQDIFL SPLEDIYFVT ELQGTDLHRL LQTRPLEKQF
VQYFHYQILR GLKYVHSAGV VHRDLKPSNI LINENCDLKI CDFGLARIQD PQMTGYVSTR
YYRAPEIMLT WQKYDVEVDI WSAGCIFAEM IEGKPLFPGK DHVHQFSIIT DLLGSPPSDV
IDTICSENTL KFVTSLPHRD PIPFSERFKT VEPDAVDLLE KMLVFDPKKR ITAADALAHP
YLAPYHDPTD EPVAEAKFDW HFNDADLPVD TWRVMMYSEI LDFHKIGGTD GQIDTSATFD
DQVAAATVAA AQAQAHALAQ AQMSQNMIDP NQLLNEDGTP VSGSIAENSS NSATTNLNGA
AAGMNSASDT INEYANQAVH FANEFQQ
