ID   HOG1A_WALI9             Reviewed;         365 AA.
AC   A3EZ55; M1S3C2; R9AIJ2;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   14-MAY-2014, sequence version 2.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=Mitogen-activated protein kinase HOG1A;
DE            Short=MAP kinase HOG1A;
DE            EC=2.7.11.24;
DE   AltName: Full=WiHog1A;
GN   Name=HOG1A; ORFNames=J056_003708;
OS   Wallemia ichthyophaga (strain EXF-994 / CBS 113033).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC   Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX   NCBI_TaxID=1299270;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PHOSPHORYLATION, AND
RP   INDUCTION.
RC   STRAIN=EXF-994 / CBS 113033;
RX   PubMed=23712906; DOI=10.1007/s00792-013-0546-4;
RA   Konte T., Plemenitas A.;
RT   "The HOG signal transduction pathway in the halophilic fungus Wallemia
RT   ichthyophaga: identification and characterisation of MAP kinases WiHog1A
RT   and WiHog1B.";
RL   Extremophiles 17:623-636(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EXF-994 / CBS 113033;
RX   PubMed=24034603; DOI=10.1186/1471-2164-14-617;
RA   Zajc J., Liu Y., Dai W., Yang Z., Hu J., Gostincar C., Gunde-Cimerman N.;
RT   "Genome and transcriptome sequencing of the halophilic fungus Wallemia
RT   ichthyophaga: haloadaptations present and absent.";
RL   BMC Genomics 14:617-617(2013).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 76-338.
RC   STRAIN=EXF-994 / CBS 113033;
RX   PubMed=17349032; DOI=10.1186/1746-1448-3-3;
RA   Lenassi M., Vaupotic T., Gunde-Cimerman N., Plemenitas A.;
RT   "The MAP kinase HwHog1 from the halophilic black yeast Hortaea werneckii:
RT   coping with stresses in solar salterns.";
RL   Saline Syst. 3:3-3(2007).
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:23712906}.
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   -!- INDUCTION: By hyperosmotic and hypo-osmotic stress. Less induced than
CC       isoform HOG1B under the same conditions. {ECO:0000269|PubMed:23712906}.
CC   -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC       whose phosphorylation activates the MAP kinases.
CC   -!- PTM: Phosphorylated. Dually phosphorylated on Thr-175 and Tyr-177,
CC       which activates the enzyme (By similarity). Rapidly dephosphorylated
CC       upon either hypo- or hyperosmotic shock. {ECO:0000250,
CC       ECO:0000269|PubMed:23712906}.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABN54705.1; Type=Miscellaneous discrepancy; Note=Contains vector sequence in the N- and C-terminal part.; Evidence={ECO:0000305};
CC       Sequence=EOR02032.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JX573532; AGG39582.1; -; Genomic_DNA.
DR   EMBL; KE007228; EOR02032.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; EF158006; ABN54705.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_009267199.1; XM_009268924.1.
DR   AlphaFoldDB; A3EZ55; -.
DR   SMR; A3EZ55; -.
DR   STRING; 1299270.A3EZ55; -.
DR   GeneID; 20376660; -.
DR   KEGG; wic:J056_003708; -.
DR   eggNOG; KOG0660; Eukaryota.
DR   HOGENOM; CLU_521951_0_0_1; -.
DR   OrthoDB; 158564at2759; -.
DR   Proteomes; UP000014064; Unassembled WGS sequence.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; 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 HOG1A"
FT                   /id="PRO_0000289706"
FT   DOMAIN          24..303
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOTIF           175..177
FT                   /note="TXY"
FT   ACT_SITE        145
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         30..38
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         53
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         175
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         177
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        184
FT                   /note="R -> K (in Ref. 3; ABN54705)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   365 AA;  41633 MW;  387C630BB77C6734 CRC64;
     MSQEDSSFVK LSVFGNIFQV TTRYTDLQPV GMGAFGLLCS STDQKSGGPV AIKKVMKPFS
     APVLAKRTYR ELKLLKHLRH ENIISLLDVF ISPGEDIYFI TELLGTDLHR LLSSRPLERQ
     FVQYFLYQML RALKFVHPAG VVHRDLKPSN ILINENCDLK ICDFGLARLQ DPQMTGYVST
     RYYRAPEIML TWQEYDSAVD IWSVGCIFAE MIDGRPIFPG KDHVHQLTVI TELLGSPPED
     VINTITSENT RRFVDALPKR HKISFADRFP NANAEEIDLL EKMLDFNPKK RITAADALAH
     PYLAPYHDPE DEPTANERFD WSFNDADLPT DQWKVMMYSE ILDFHNVDVK SEKDMTPSTT
     TAGAH
//