Reviewed, UniProtKB/Swiss-Prot Q92207 (HOG1_CANAL)

Names and origin

Protein names

Recommended name:
    Mitogen-activated protein kinase HOG1
      Short name=MAP kinase HOG1
    EC=2.7.11.24

Gene names

Name:	HOG1
ORF Names:	CaO19.895, CaO19.8514

Organism

Candida albicans (Yeast)

Taxonomic identifier

5476 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	377 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Mitogen-activated protein kinase involved in a signal transduction pathway that is activated by changes in the osmolarity of the extracellular environment. Controls osmotic regulation of transcription of target genes. Regulates stress-induced production and accumulation of glycerol and D-arabitol. HOG1 is also involved in virulence, morphogenesis and oxidative stress response especially through its role in chlamydospore formation, an oxygen-dependent morphogenetic program. Ref.1 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium By similarity.
Enzyme regulation	Activated by tyrosine and threonine phosphorylation By similarity.
Subcellular location	Cytoplasm. Nucleus. Note: Predominantly cytoplasmic in unstressed cells but rapidly concentrates within the nucleus in response to hyperosmotic conditions and phosphorylation. Ref.6 Ref.7 Ref.12
Domain	The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.
Post-translational modification	Dually phosphorylated on Thr-174 and Tyr-176, which activates the enzyme By similarity. Phosphorylated in response to oxidative and salt stress.
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. MAP kinase subfamily. HOG1 sub-subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Activator Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro regulation of transcription Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW MAP kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 377	377	Mitogen-activated protein kinase HOG1		PRO_0000186328
Regions
	Domain	23 – 305	283	Protein kinase
	Nucleotide binding	29 – 37	9	ATP By similarity
	Motif	174 – 176	3	TXY
Sites
	Active site	144	1	Proton acceptor By similarity
	Binding site	52	1	ATP By similarity
Amino acid modifications
	Modified residue	174	1	Phosphothreonine By similarity
	Modified residue	176	1	Phosphotyrosine By similarity
Experimental info
	Sequence conflict	298	1	E → Q in CAA62214. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q92207-1 [UniParc]. Last modified May 29, 2007. Version 2. Checksum: 8DB21BD497A4F52E	FASTA	377	42,947
	10 20 30 40 50 60 MSADGEFTRT QIFGTVFEIT NRYTELNPVG MGAFGLVCSA VDRLTGQNVA VKKVMKPFST 70 80 90 100 110 120 SVLAKRTYRE LKLLKHLKHE NLITLDDIFI SPLEDIYFVN ELQGTDLHRL LNSRPLEKQF 130 140 150 160 170 180 IQYFTYQIMR GLKYIHSAGV IHRDLKPSNI LINENCDLKI CDFGLARLQD PQMTGYVSTR 190 200 210 220 230 240 YYRAPEIMLT WQKYDTEVDL WSVGCILAEM IEGKPLFPGK DHVHQFSIIT ELLGSPPADV 250 260 270 280 290 300 IDTICSENTL RFVQSLPHRD PIPFSERFAS CTHVEPEAID LLAKLLVFDP KKRISAVEGL 310 320 330 340 350 360 THPYMEAYHD PTDEPVCESK FDWSFNDADL PVDTWRVMMY SEILDFHQTV GVANETEGSE 370 QPDSQVEQNN LDSANGA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The mitogen-activated protein kinase homolog HOG1 gene controls glycerol accumulation in the pathogenic fungus Candida albicans." San Jose C., Monge R.A., Perez-Diaz R., Pla J., Nombela C. J. Bacteriol. 178:5850-5852(1996) [PubMed: 8824643] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION. Strain: ATCC 64385 / 1001.
[2]	"The diploid genome sequence of Candida albicans." Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S. Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed: 15123810] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SC5314.
[3]	"Role of the mitogen-activated protein kinase Hog1p in morphogenesis and virulence of Candida albicans." Alonso-Monge R., Navarro-Garcia F., Molero G., Diez-Orejas R., Gustin M.C., Pla J., Sanchez M., Nombela C. J. Bacteriol. 181:3058-3068(1999) [PubMed: 10322006] [Abstract] Cited for: FUNCTION.
[4]	"The Hog1 mitogen-activated protein kinase is essential in the oxidative stress response and chlamydospore formation in Candida albicans." Alonso-Monge R., Navarro-Garcia F., Roman E., Negredo A.I., Eisman B., Nombela C., Pla J. Eukaryot. Cell 2:351-361(2003) [PubMed: 12684384] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION.
[5]	"Candida albicans response regulator gene SSK1 regulates a subset of genes whose functions are associated with cell wall biosynthesis and adaptation to oxidative stress." Chauhan N., Inglis D., Roman E., Pla J., Li D., Calera J.A., Calderone R. Eukaryot. Cell 2:1018-1024(2003) [PubMed: 14555484] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION.
[6]	"A conserved stress-activated protein kinase regulates a core stress response in the human pathogen Candida albicans." Smith D.A., Nicholls S., Morgan B.A., Brown A.J.P., Quinn J. Mol. Biol. Cell 15:4179-4190(2004) [PubMed: 15229284] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION.
[7]	"The Pbs2 MAP kinase kinase is essential for the oxidative-stress response in the fungal pathogen Candida albicans." Arana D.M., Nombela C., Alonso-Monge R., Pla J. Microbiology 151:1033-1049(2005) [PubMed: 15817773] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[8]	"The MAP kinase Mkc1p is activated under different stress conditions in Candida albicans." Navarro-Garcia F., Eisman B., Fiuza S.M., Nombela C., Pla J. Microbiology 151:2737-2749(2005) [PubMed: 16079350] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION.
[9]	"The MAP kinase Hog1p differentially regulates stress-induced production and accumulation of glycerol and D-arabitol in Candida albicans." Kayingo G., Wong B. Microbiology 151:2987-2999(2005) [PubMed: 16151209] [Abstract] Cited for: FUNCTION.
[10]	"The Cek1 and Hog1 mitogen-activated protein kinases play complementary roles in cell wall biogenesis and chlamydospore formation in the fungal pathogen Candida albicans." Eisman B., Alonso-Monge R., Roman E., Arana D.M., Nombela C., Pla J. Eukaryot. Cell 5:347-358(2006) [PubMed: 16467475] [Abstract] Cited for: FUNCTION.
[11]	"Role of the Hog1 stress-activated protein kinase in the global transcriptional response to stress in the fungal pathogen Candida albicans." Enjalbert B., Smith D.A., Cornell M.J., Alam I., Nicholls S., Brown A.J.P., Quinn J. Mol. Biol. Cell 17:1018-1032(2006) [PubMed: 16339080] [Abstract] Cited for: FUNCTION.
[12]	"Functional studies of the Ssk1p response regulator protein of Candida albicans as determined by phenotypic analysis of receiver domain point mutants." Menon V., Li D., Chauhan N., Rajnarayanan R., Dubrovska A., West A.H., Calderone R. Mol. Microbiol. 62:997-1013(2006) [PubMed: 17038117] [Abstract] Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X90586 Genomic DNA. Translation: CAA62214.1. AACQ01000018 Genomic DNA. Translation: EAL02326.1. AACQ01000019 Genomic DNA. Translation: EAL02199.1.
RefSeq	XP_721016.1. XP_721137.1.
3D structure databases
HSSP	HSSP built from PDB template 1KV1 based on UniProtKB Q16539.
ModBase	Search...
Genome annotation databases
GeneID	3637270. 3637393.
KEGG	cal:CaO19.8514. cal:CaO19.895.
Organism-specific databases
CGD	CAL0002931. HOG1.
Phylogenomic databases
OMA	SEILDFH.
Enzyme and pathway databases
BRENDA	2.7.11.24. 1124.
Family and domain databases
InterPro	IPR003527. MAP_kinase_CS. IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. IPR002290. Ser_thr_pkinase. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS01351. MAPK. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HOG1_CANAL

Accession

Primary (citable) accession number: Q92207
Secondary accession number(s): Q5AHA1

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 29, 2007
Last modified:	November 3, 2009
This is version 63 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)