HOG1_CRYNH
ID HOG1_CRYNH Reviewed; 365 AA.
AC Q56R42; J9VTY4;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Mitogen-activated protein kinase HOG1;
DE Short=MAP kinase HOG1;
DE EC=2.7.11.24;
GN Name=HOG1; ORFNames=CNAG_01523;
OS Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=235443;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PHOSPHORYLATION, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487;
RX PubMed=15728721; DOI=10.1091/mbc.e04-11-0987;
RA Bahn Y.-S., Kojima K., Cox G.M., Heitman J.;
RT "Specialization of the HOG pathway and its impact on differentiation and
RT virulence of Cryptococcus neoformans.";
RL Mol. Biol. Cell 16:2285-2300(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487;
RX PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA Janbon G., Ormerod K.L., Paulet D., Byrnes E.J. III, Yadav V.,
RA Chatterjee G., Mullapudi N., Hon C.-C., Billmyre R.B., Brunel F.,
RA Bahn Y.-S., Chen W., Chen Y., Chow E.W.L., Coppee J.-Y., Floyd-Averette A.,
RA Gaillardin C., Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S.,
RA Hamlin J.L., Hsueh Y.-P., Ianiri G., Jones S., Kodira C.D., Kozubowski L.,
RA Lam W., Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K.,
RA Proux C., Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A.,
RA Zeng Q., Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA Cuomo C.A., Dietrich F.S.;
RT "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT grubii reveals complex RNA expression and microevolution leading to
RT virulence attenuation.";
RL PLoS Genet. 10:E1004261-E1004261(2014).
RN [3]
RP FUNCTION, PHOSPHORYLATION, AND MUTAGENESIS OF LYS-49; LYS-50; THR-171 AND
RP TYR-173.
RX PubMed=16514140; DOI=10.1099/mic.0.28571-0;
RA Kojima K., Bahn Y.-S., Heitman J.;
RT "Calcineurin, Mpk1 and Hog1 MAPK pathways independently control fludioxonil
RT antifungal sensitivity in Cryptococcus neoformans.";
RL Microbiology 152:591-604(2006).
RN [4]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=16672377; DOI=10.1091/mbc.e06-02-0113;
RA Bahn Y.-S., Kojima K., Cox G.M., Heitman J.;
RT "A unique fungal two-component system regulates stress responses, drug
RT sensitivity, sexual development, and virulence of Cryptococcus
RT neoformans.";
RL Mol. Biol. Cell 17:3122-3135(2006).
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. Also involved in response to UV
CC radiations, heat stress and oxidative stress. Mediates the sensitivity
CC to fludioxonil, an agricultural fungicide.
CC {ECO:0000269|PubMed:15728721, ECO:0000269|PubMed:16514140,
CC ECO:0000269|PubMed:16672377}.
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 dephosphorylation after osmotic
CC stress or in presence of the fludioxonil fungicide.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15728721}. Nucleus
CC {ECO:0000269|PubMed:15728721}. Note=Concentration into the nucleus in
CC response to hyperosmotic conditions is transient and moderate.
CC -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC whose phosphorylation activates the MAP kinases.
CC -!- PTM: Contrary to what happens in most fungi, is constitutively
CC phosphorylated during non-stress conditions and dephosphorylated after
CC osmotic stress or in presence of the fludioxonil fungicide.
CC {ECO:0000269|PubMed:15728721, ECO:0000269|PubMed:16514140,
CC ECO:0000269|PubMed:16672377}.
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; AY775548; AAX08139.1; -; Genomic_DNA.
DR EMBL; CP003830; AFR97728.1; -; Genomic_DNA.
DR RefSeq; XP_012052578.1; XM_012197188.1.
DR AlphaFoldDB; Q56R42; -.
DR SMR; Q56R42; -.
DR SwissPalm; Q56R42; -.
DR EnsemblFungi; AAW42642; AAW42642; CNC06590.
DR EnsemblFungi; AFR97728; AFR97728; CNAG_01523.
DR GeneID; 23885222; -.
DR VEuPathDB; FungiDB:CNAG_01523; -.
DR HOGENOM; CLU_000288_181_1_1; -.
DR PHI-base; PHI:497; -.
DR Proteomes; UP000010091; Chromosome 11.
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; 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 1: Evidence at protein level;
KW Activator; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Serine/threonine-protein kinase; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..365
FT /note="Mitogen-activated protein kinase HOG1"
FT /id="PRO_0000289685"
FT DOMAIN 20..299
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOTIF 171..173
FT /note="TXY"
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"
FT MUTAGEN 49
FT /note="K->S: Confers resistance to fludioxonil; when
FT associated with N-50."
FT /evidence="ECO:0000269|PubMed:16514140"
FT MUTAGEN 50
FT /note="K->N: Confers resistance to fludioxonil; when
FT associated with S-49."
FT /evidence="ECO:0000269|PubMed:16514140"
FT MUTAGEN 171
FT /note="T->A: Confers resistance to fludioxonil; when
FT associated with A-173."
FT /evidence="ECO:0000269|PubMed:16514140"
FT MUTAGEN 173
FT /note="Y->A: Confers resistance to fludioxonil; when
FT associated with A-171."
FT /evidence="ECO:0000269|PubMed:16514140"
SQ SEQUENCE 365 AA; 41213 MW; F28E2E95B6DAD6B5 CRC64;
MADFVKLSIF GTVFEVTTRY VDLQPVGMGA FGLVCSAKDQ LSGTSVAIKK IMKPFSTPVL
SKRTYRELKL LKHLRHENII SLSDIFISPL EDIYFVTELL GTDLHRLLTS RPLEKQFIQY
FLYQILRGLK YVHSAGVVHR DLKPSNILVN ENCDLKICDF GLARIQDPQM TGYVSTRYYR
APEIMLTWQK YDVAVDIWST GCIFAEMLEG KPLFPGKDHV NQFSIITELL GTPPDDVIQT
IASENTLRFV QSLPKREKVP FSTKFPNADP VSLDLLEKML VFDPRTRISA AEGLAHEYLA
PYHDPTDEPV AAEVFDWSFN DADLPVDTWK VMMYSEILDF HNLGDISQNE AEGPVTGEVP
AAPAS
