HOG1_DEBHA
ID HOG1_DEBHA Reviewed; 387 AA.
AC Q9UV50; Q6BNK7;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 3.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Mitogen-activated protein kinase HOG1;
DE Short=MAP kinase HOG1;
DE EC=2.7.11.24;
GN Name=HOG1; OrderedLocusNames=DEHA2E20944g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=MTCC 234;
RX PubMed=10620778;
RX DOI=10.1002/(sici)1097-0061(20000115)16:1<81::aid-yea510>3.0.co;2-i;
RA Bansal P.K., Mondal A.K.;
RT "Isolation and sequence of the HOG1 homolog from Debaryomyces hansenii by
RT complementation of hog1 Delta strain of Saccharomyces cerevisiae.";
RL Yeast 16:81-88(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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).
RN [3]
RP FUNCTION, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=16091960; DOI=10.1007/s00294-005-0010-9;
RA Sharma P., Meena N., Aggarwal M., Mondal A.K.;
RT "Debaryomyces hansenii, a highly osmo-tolerant and halo-tolerant yeast,
RT maintains activated Dhog1p in the cytoplasm during its growth under severe
RT osmotic stress.";
RL Curr. Genet. 48:162-170(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:10620778,
CC ECO:0000269|PubMed:16091960}.
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16091960}. Nucleus
CC {ECO:0000269|PubMed:16091960}. Note=In contrast to other yeasts, the
CC nuclear translocation is delayed under severe osmotic conditions
CC although it is activated rapidly.
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 (By similarity). Phosphorylated in response of osmotic stress,
CC oxidative stress and UV stress, but not heat stress. {ECO:0000250,
CC ECO:0000269|PubMed:16091960}.
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; AF185278; AAF24231.2; -; Genomic_DNA.
DR EMBL; CR382137; CAG88486.2; -; Genomic_DNA.
DR RefSeq; XP_460213.2; XM_460213.1.
DR AlphaFoldDB; Q9UV50; -.
DR SMR; Q9UV50; -.
DR STRING; 4959.XP_460213.2; -.
DR EnsemblFungi; CAG88486; CAG88486; DEHA2E20944g.
DR GeneID; 2902985; -.
DR KEGG; dha:DEHA2E20944g; -.
DR VEuPathDB; FungiDB:DEHA2E20944g; -.
DR eggNOG; KOG0660; Eukaryota.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; Q9UV50; -.
DR OMA; YTDLNPV; -.
DR OrthoDB; 683132at2759; -.
DR Proteomes; UP000000599; Chromosome E.
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: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; 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 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..387
FT /note="Mitogen-activated protein kinase HOG1"
FT /id="PRO_0000186330"
FT DOMAIN 23..305
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 360..387
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"
FT CONFLICT 272
FT /note="S -> T (in Ref. 1; AAF24231)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 387 AA; 44357 MW; 710908EC58AA0828 CRC64;
MVSDGEFTRT QIFGTVFEIT NRYTDLNPVG MGAFGLVCSA IDKLTGQNVA VKKIMKPFST
SVLAKRTYRE LKLLKHLRHE NLITLDDIFL SPLEDIYFVT ELQGTDLHRL LTSRPLEKQF
IQYFTYQILR GLKYVHSAGV IHRDLKPSNI LINENCDLKI CDFGLARIQD PQMTGYVSTR
YYRAPEIMLT WQKYDTEVDL WSVGCILSEM IEGKPLFPGK DHVHQFSIIT ELLGSPPPDV
IETICSENTL RFVQSLPHRD PIPFSERFAQ CSHVEPEAID LLAKMLIFDP KKRISALDAL
SHPYMEPYHD PTDEPVCEVK FDWSFNDADL PVDTWRVMMY SEILDFHQII GAGANGTTQE
QMAQIQQEGI QAPSSQYQQT NQEQKVE
