ID   HOG1_CRYNJ              Reviewed;         365 AA.
AC   P0CP68; Q55WS9; Q5KJG8; Q8NKG4;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=Mitogen-activated protein kinase HOG1;
DE            Short=MAP kinase HOG1;
DE            EC=2.7.11.24;
GN   Name=HOG1; OrderedLocusNames=CNC06590;
OS   Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS   MYA-565) (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=214684;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Saha S.K., Chaturvedi V.;
RT   "Functional characterization of Cryptococcus neoformans mitogen-activated
RT   protein kinase homolog HOG1.";
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEC21 / ATCC MYA-565;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
RN   [3]
RP   FUNCTION, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RC   STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487, and JEC21 / ATCC
RC   MYA-565;
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   [4]
RP   FUNCTION, AND PHOSPHORYLATION.
RC   STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487, and JEC21 / ATCC
RC   MYA-565;
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).
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 UV radiations
CC       and mediates the sensitivity to fludioxonil, an agricultural fungicide.
CC       {ECO:0000269|PubMed:15728721, ECO:0000269|PubMed:16514140}.
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:0000269|PubMed:15728721}. Nucleus
CC       {ECO:0000269|PubMed:15728721}. Note=Predominantly cytoplasmic in
CC       unstressed cells but rapidly concentrates within the nucleus in
CC       response to hyperosmotic conditions and phosphorylation.
CC   -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC       whose phosphorylation activates the MAP kinases.
CC   -!- PTM: Dually phosphorylated on Thr-171 and Tyr-173, which activates the
CC       enzyme (By similarity). Phosphorylated by PBS2 after osmotic stress.
CC       {ECO:0000250, ECO:0000269|PubMed:15728721,
CC       ECO:0000269|PubMed:16514140}.
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; AF243531; AAM26267.1; -; mRNA.
DR   EMBL; AE017343; AAW42642.1; -; Genomic_DNA.
DR   RefSeq; XP_569949.1; XM_569949.1.
DR   AlphaFoldDB; P0CP68; -.
DR   SMR; P0CP68; -.
DR   STRING; 214684.P0CP68; -.
DR   PaxDb; 214684-P0CP68; -.
DR   EnsemblFungi; AAW42642; AAW42642; CNC06590.
DR   GeneID; 3256363; -.
DR   KEGG; cne:CNC06590; -.
DR   VEuPathDB; FungiDB:CNC06590; -.
DR   eggNOG; KOG0660; Eukaryota.
DR   HOGENOM; CLU_000288_181_1_1; -.
DR   InParanoid; P0CP68; -.
DR   OMA; NRYTDLN; -.
DR   OrthoDB; 158564at2759; -.
DR   Proteomes; UP000002149; Chromosome 3.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR   GO; GO:0007231; P:osmosensory signaling pathway; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0051403; P:stress-activated MAPK cascade; IBA:GO_Central.
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; 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   PANTHER; PTHR24055; MITOGEN-ACTIVATED PROTEIN KINASE; 1.
DR   PANTHER; PTHR24055:SF158; MITOGEN-ACTIVATED PROTEIN KINASE P38A-RELATED; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR01773; P38MAPKINASE.
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   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..365
FT                   /note="Mitogen-activated protein kinase HOG1"
FT                   /id="PRO_0000289684"
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   CONFLICT        195
FT                   /note="V -> G (in Ref. 1; AAM26267)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        247
FT                   /note="L -> I (in Ref. 1; AAM26267)"
FT                   /evidence="ECO:0000305"
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
//