HOG1A_WALI9
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 03-AUG-2022, entry version 65.
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};
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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 EnsemblFungi; EOR02032; EOR02032; J056_003708.
DR GeneID; 20376660; -.
DR KEGG; wic:J056_003708; -.
DR eggNOG; KOG0660; Eukaryota.
DR HOGENOM; CLU_521951_0_0_1; -.
DR OrthoDB; 683132at2759; -.
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:0006468; P:protein phosphorylation; IEA:InterPro.
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 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; 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
