HOG1_CANAL
ID HOG1_CANAL Reviewed; 377 AA.
AC Q92207; A0A1D8PGU7; Q5AHA1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Mitogen-activated protein kinase HOG1;
DE Short=MAP kinase HOG1;
DE EC=2.7.11.24;
GN Name=HOG1; OrderedLocusNames=CAALFM_C203330CA;
GN ORFNames=CaO19.8514, CaO19.895;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 64385 / 1001;
RX PubMed=8824643; DOI=10.1128/jb.178.19.5850-5852.1996;
RA San Jose C., Monge R.A., Perez-Diaz R., Pla J., Nombela C.;
RT "The mitogen-activated protein kinase homolog HOG1 gene controls glycerol
RT accumulation in the pathogenic fungus Candida albicans.";
RL J. Bacteriol. 178:5850-5852(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [5]
RP FUNCTION.
RX PubMed=10322006; DOI=10.1128/jb.181.10.3058-3068.1999;
RA Alonso-Monge R., Navarro-Garcia F., Molero G., Diez-Orejas R., Gustin M.C.,
RA Pla J., Sanchez M., Nombela C.;
RT "Role of the mitogen-activated protein kinase Hog1p in morphogenesis and
RT virulence of Candida albicans.";
RL J. Bacteriol. 181:3058-3068(1999).
RN [6]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=12684384; DOI=10.1128/ec.2.2.351-361.2003;
RA Alonso-Monge R., Navarro-Garcia F., Roman E., Negredo A.I., Eisman B.,
RA Nombela C., Pla J.;
RT "The Hog1 mitogen-activated protein kinase is essential in the oxidative
RT stress response and chlamydospore formation in Candida albicans.";
RL Eukaryot. Cell 2:351-361(2003).
RN [7]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=14555484; DOI=10.1128/ec.2.5.1018-1024.2003;
RA Chauhan N., Inglis D., Roman E., Pla J., Li D., Calera J.A., Calderone R.;
RT "Candida albicans response regulator gene SSK1 regulates a subset of genes
RT whose functions are associated with cell wall biosynthesis and adaptation
RT to oxidative stress.";
RL Eukaryot. Cell 2:1018-1024(2003).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=15229284; DOI=10.1091/mbc.e04-03-0181;
RA Smith D.A., Nicholls S., Morgan B.A., Brown A.J.P., Quinn J.;
RT "A conserved stress-activated protein kinase regulates a core stress
RT response in the human pathogen Candida albicans.";
RL Mol. Biol. Cell 15:4179-4190(2004).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15817773; DOI=10.1099/mic.0.27723-0;
RA Arana D.M., Nombela C., Alonso-Monge R., Pla J.;
RT "The Pbs2 MAP kinase kinase is essential for the oxidative-stress response
RT in the fungal pathogen Candida albicans.";
RL Microbiology 151:1033-1049(2005).
RN [10]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=16079350; DOI=10.1099/mic.0.28038-0;
RA Navarro-Garcia F., Eisman B., Fiuza S.M., Nombela C., Pla J.;
RT "The MAP kinase Mkc1p is activated under different stress conditions in
RT Candida albicans.";
RL Microbiology 151:2737-2749(2005).
RN [11]
RP FUNCTION.
RX PubMed=16151209; DOI=10.1099/mic.0.28040-0;
RA Kayingo G., Wong B.;
RT "The MAP kinase Hog1p differentially regulates stress-induced production
RT and accumulation of glycerol and D-arabitol in Candida albicans.";
RL Microbiology 151:2987-2999(2005).
RN [12]
RP FUNCTION.
RX PubMed=16467475; DOI=10.1128/ec.5.2.347-358.2006;
RA Eisman B., Alonso-Monge R., Roman E., Arana D.M., Nombela C., Pla J.;
RT "The Cek1 and Hog1 mitogen-activated protein kinases play complementary
RT roles in cell wall biogenesis and chlamydospore formation in the fungal
RT pathogen Candida albicans.";
RL Eukaryot. Cell 5:347-358(2006).
RN [13]
RP FUNCTION.
RX PubMed=16339080; DOI=10.1091/mbc.e05-06-0501;
RA Enjalbert B., Smith D.A., Cornell M.J., Alam I., Nicholls S., Brown A.J.P.,
RA Quinn J.;
RT "Role of the Hog1 stress-activated protein kinase in the global
RT transcriptional response to stress in the fungal pathogen Candida
RT albicans.";
RL Mol. Biol. Cell 17:1018-1032(2006).
RN [14]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=17038117; DOI=10.1111/j.1365-2958.2006.05438.x;
RA Menon V., Li D., Chauhan N., Rajnarayanan R., Dubrovska A., West A.H.,
RA Calderone R.;
RT "Functional studies of the Ssk1p response regulator protein of Candida
RT albicans as determined by phenotypic analysis of receiver domain point
RT mutants.";
RL Mol. Microbiol. 62:997-1013(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. Regulates stress-induced production and
CC accumulation of glycerol and D-arabitol. HOG1 is also involved in
CC virulence, morphogenesis and oxidative stress response especially
CC through its role in chlamydospore formation, an oxygen-dependent
CC morphogenetic program. {ECO:0000269|PubMed:10322006,
CC ECO:0000269|PubMed:12684384, ECO:0000269|PubMed:14555484,
CC ECO:0000269|PubMed:15229284, ECO:0000269|PubMed:15817773,
CC ECO:0000269|PubMed:16079350, ECO:0000269|PubMed:16151209,
CC ECO:0000269|PubMed:16339080, ECO:0000269|PubMed:16467475,
CC ECO:0000269|PubMed:8824643}.
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. Nucleus. Note=Predominantly
CC cytoplasmic in unstressed cells but rapidly concentrates within the
CC nucleus in 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-174 and Tyr-176, which activates the
CC enzyme (By similarity). Phosphorylated in response to oxidative and
CC salt stress. {ECO:0000250, ECO:0000269|PubMed:12684384,
CC ECO:0000269|PubMed:14555484, ECO:0000269|PubMed:15229284,
CC ECO:0000269|PubMed:16079350, ECO:0000269|PubMed:17038117}.
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; X90586; CAA62214.1; -; Genomic_DNA.
DR EMBL; CP017624; AOW27369.1; -; Genomic_DNA.
DR RefSeq; XP_721016.1; XM_715923.1.
DR AlphaFoldDB; Q92207; -.
DR SMR; Q92207; -.
DR BioGRID; 1220364; 7.
DR STRING; 237561.Q92207; -.
DR PRIDE; Q92207; -.
DR GeneID; 3637393; -.
DR KEGG; cal:CAALFM_C203330CA; -.
DR CGD; CAL0000197240; HOG1.
DR VEuPathDB; FungiDB:C2_03330C_A; -.
DR eggNOG; KOG0660; Eukaryota.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; Q92207; -.
DR OrthoDB; 683132at2759; -.
DR BRENDA; 2.7.11.24; 1096.
DR PHI-base; PHI:149; -.
DR PRO; PR:Q92207; -.
DR Proteomes; UP000000559; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IDA:CGD.
DR GO; GO:0005634; C:nucleus; IDA:CGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004707; F:MAP kinase activity; ISS:CGD.
DR GO; GO:0004672; F:protein kinase activity; IDA:CGD.
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:0071276; P:cellular response to cadmium ion; IMP:CGD.
DR GO; GO:0034605; P:cellular response to heat; IMP:CGD.
DR GO; GO:0071500; P:cellular response to nitrosative stress; IMP:CGD.
DR GO; GO:0071470; P:cellular response to osmotic stress; IMP:CGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:CGD.
DR GO; GO:0071467; P:cellular response to pH; IMP:CGD.
DR GO; GO:0001410; P:chlamydospore formation; IMP:CGD.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0044182; P:filamentous growth of a population of unicellular organisms; IMP:CGD.
DR GO; GO:0036180; P:filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
DR GO; GO:0036168; P:filamentous growth of a population of unicellular organisms in response to heat; IMP:CGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:CGD.
DR GO; GO:0006973; P:intracellular accumulation of glycerol; IMP:CGD.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:1900429; P:negative regulation of filamentous growth of a population of unicellular organisms; IMP:CGD.
DR GO; GO:1900444; P:negative regulation of filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
DR GO; GO:1900432; P:negative regulation of filamentous growth of a population of unicellular organisms in response to heat; IMP:CGD.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IMP:CGD.
DR GO; GO:0007231; P:osmosensory signaling pathway; IBA:GO_Central.
DR GO; GO:0046173; P:polyol biosynthetic process; IMP:CGD.
DR GO; GO:0006468; P:protein phosphorylation; IDA:CGD.
DR GO; GO:1900443; P:regulation of filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
DR GO; GO:0009651; P:response to salt stress; IMP:CGD.
DR GO; GO:0009636; P:response to toxic substance; IMP:CGD.
DR GO; GO:0051403; P:stress-activated MAPK cascade; IDA:CGD.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003527; MAP_kinase_CS.
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 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..377
FT /note="Mitogen-activated protein kinase HOG1"
FT /id="PRO_0000186328"
FT DOMAIN 23..305
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 354..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 174..176
FT /note="TXY"
FT ACT_SITE 144
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 29..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 174
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 176
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT CONFLICT 298
FT /note="E -> Q (in Ref. 1; CAA62214)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 377 AA; 42947 MW; 8DB21BD497A4F52E CRC64;
MSADGEFTRT QIFGTVFEIT NRYTELNPVG MGAFGLVCSA VDRLTGQNVA VKKVMKPFST
SVLAKRTYRE LKLLKHLKHE NLITLDDIFI SPLEDIYFVN ELQGTDLHRL LNSRPLEKQF
IQYFTYQIMR GLKYIHSAGV IHRDLKPSNI LINENCDLKI CDFGLARLQD PQMTGYVSTR
YYRAPEIMLT WQKYDTEVDL WSVGCILAEM IEGKPLFPGK DHVHQFSIIT ELLGSPPADV
IDTICSENTL RFVQSLPHRD PIPFSERFAS CTHVEPEAID LLAKLLVFDP KKRISAVEGL
THPYMEAYHD PTDEPVCESK FDWSFNDADL PVDTWRVMMY SEILDFHQTV GVANETEGSE
QPDSQVEQNN LDSANGA
