HOG1_KLULA
ID HOG1_KLULA Reviewed; 444 AA.
AC Q6CJA8;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Mitogen-activated protein kinase HOG1;
DE Short=MAP kinase HOG1;
DE EC=2.7.11.24;
GN Name=HOG1; OrderedLocusNames=KLLA0F20053g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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-173 and Tyr-175, 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; CR382126; CAG98689.1; -; Genomic_DNA.
DR RefSeq; XP_455981.1; XM_455981.1.
DR AlphaFoldDB; Q6CJA8; -.
DR SMR; Q6CJA8; -.
DR STRING; 28985.XP_455981.1; -.
DR EnsemblFungi; CAG98689; CAG98689; KLLA0_F20053g.
DR GeneID; 2895492; -.
DR KEGG; kla:KLLA0_F20053g; -.
DR eggNOG; KOG0660; Eukaryota.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; Q6CJA8; -.
DR OMA; YTDLNPV; -.
DR Proteomes; UP000000598; Chromosome F.
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; IEA:UniProtKB-SubCell.
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; PS00221; MIP; 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..444
FT /note="Mitogen-activated protein kinase HOG1"
FT /id="PRO_0000289694"
FT DOMAIN 22..301
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 371..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 173..175
FT /note="TXY"
FT ACT_SITE 143
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 28..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 173
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 175
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 444 AA; 50298 MW; CEA1CB7A1849891D CRC64;
MSNEEFIRTQ IFGTVFEITN RYTNLNPVGM GAFGLVCSAT DTLTSQPVAI KKIMKPFSTS
VLAKRTYREL KLLKHLRHEN LICLEDIFLS PLEDIYFVTE LQGTDLHRLL QTRPLEKQFV
QYFLYQILRG LKYVHSAGVI HRDLKPSNIL INENCDLKIC DFGLARIQDP QMTGYVSTRY
YRAPEIMLTW QKYNVEVDIW SAGCIFAEMI EGKPLFPGKD HVHQFSIITD LLGSPPKDVI
DTICSENTLK FVTSLPHRDP VPFSSRFQNL EPDAIDLLEK MLVFDPKKRI TAADALAHPY
LSPYHDPTDE PIAEAKFDWN FNDADLPVDT WRVMMYSEIL DFHQIGDPQI NTNATFDDQV
AAATVAAAEA ASKQQQQQQH QTEEQTQQTI ASTPPQAQVT PQQLESGANS NSNSNPSFSI
GPDPANETLT NFANQADQYV SKFK
