Q39023 (MPK3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Mitogen-activated protein kinase 3
Short name=AtMPK3
Short name=MAP kinase 3
EC=2.7.11.24

Gene names

Name:	MPK3
Ordered Locus Names:	At3g45640
ORF Names:	F9K21.220, T6D9.4

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › Mesangiospermae › eudicotyledons › Gunneridae › Pentapetalae › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	370 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in oxidative stress-mediated signaling cascade (such as ozone). Involved in the innate immune MAP kinase signaling cascade (MEKK1, MKK4/MKK5 and MPK3/MPK6) downstream of bacterial flagellin receptor FLS2. May be involved in hypersensitive response (HR)-mediated signaling cascade. May phosphorylate regulators of WRKY transcription factors. Mediates the phosphorylation of VIP1 and subsequent stress genes transcription in response to Agrobacterium. MKK9-MPK3/MPK6 module phosphorylates and activates EIN3, leading to the promotion of EIN3-mediated transcription in ethylene signaling. MPK3/MPK6 cascade regulates camalexin synthesis through transcriptional regulation of the biosynthetic genes after pathogen infection. YDA-MKK4/MKK5-MPK3/MPK6 module regulates stomatal cell fate before the guard mother cell (GMC) is specified. This MAPK cascade also functions downstream of the ER receptor in regulating coordinated local cell proliferation, which shapes the morphology of plant organs. Ref.9 Ref.13 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21 Ref.22
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Activated by threonine and tyrosine phosphorylation. Activated by MAP kinase kinases MKK4, MKK5, MKK7 and MKK9. Activated in response to hydrogen peroxide, ozone, salt stress and flagellin bacterial elicitor. Triggered by Agrobacterium upon T-DNA transfer. Repressed by DSPTP1B/MKP2-mediated dephosphorylation. Ref.6 Ref.7 Ref.9 Ref.12 Ref.15 Ref.17 Ref.18 Ref.21
Subunit structure	Interacts with DSPTP1B/MKP2, NDPK2 and VIP1. The interaction with DSPTP1B/MKP2 is repressed by fungal elicitation. Ref.11 Ref.17 Ref.20
Subcellular location	Cytoplasm. Nucleus. Note: Translocated into the nucleus in response to phosphorylation Probable. Ref.12
Induction	By touch, cold, salinity stress and ozone. Ref.5 Ref.6 Ref.7 Ref.9 Ref.12 Ref.15 Ref.17 Ref.18 Ref.21
Domain	The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.
Post-translational modification	Dually phosphorylated on Thr-196 and Tyr-198, which activates the enzyme By similarity. Dephosphorylated by DSPTP1B/MKP2. Ref.8 Ref.15
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Hypersensitive response Plant defense Stress response
Cellular component	Cytoplasm Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	abscisic acid-activated signaling pathway Traceable author statement PubMed 12434021. Source: TAIR activation of MAPK activity involved in osmosensory signaling pathway Inferred from direct assay Ref.7. Source: TAIR camalexin biosynthetic process Inferred from mutant phenotype Ref.19. Source: TAIR inflorescence development Inferred from genetic interaction Ref.22. Source: TAIR ovule development Inferred from genetic interaction PubMed 18364464. Source: TAIR plant-type hypersensitive response Inferred from electronic annotation. Source: UniProtKB-KW priming of cellular response to stress Inferred from mutant phenotype PubMed 19318610. Source: TAIR regulation of stomatal complex development Inferred from genetic interaction Ref.16. Source: TAIR regulation of stomatal complex patterning Inferred from genetic interaction Ref.16. Source: TAIR response to UV-B Inferred from mutant phenotype PubMed 21790814. Source: TAIR response to bacterium Inferred from expression pattern PubMed 19318610. Source: TAIR response to chitin Inferred from expression pattern PubMed 15923325. Source: TAIR response to cold Inferred from expression pattern Ref.5. Source: TAIR response to osmotic stress Inferred from direct assay Ref.7. Source: TAIR response to oxidative stress Inferred from expression pattern Ref.6. Source: TAIR response to wounding Inferred from expression pattern PubMed 17953483. Source: TAIR
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: UniProtKB-EC protein kinase activity Inferred from direct assay PubMed 22631074. Source: TAIR
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
At2g47060	O80719	2	EBI-349526,EBI-4436376
NDPK2	O64903	4	EBI-349526,EBI-349517

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 370	370	Mitogen-activated protein kinase 3		PRO_0000186312
Regions
	Domain	38 – 324	287	Protein kinase
	Nucleotide binding	44 – 52	9	ATP By similarity
	Motif	196 – 198	3	TXY
Sites
	Active site	164	1	Proton acceptor By similarity
	Binding site	67	1	ATP By similarity
Amino acid modifications
	Modified residue	196	1	Phosphothreonine By similarity
	Modified residue	198	1	Phosphotyrosine By similarity
	Modified residue	201	1	Phosphothreonine By similarity
Experimental info
	Sequence conflict	15	1	E → D in BAA04866. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q39023 [UniParc]. Last modified June 6, 2002. Version 2. Checksum: 6992A7D97F3C9841	FASTA	370	42,717
	10 20 30 40 50 60 MNTGGGQYTD FPAVETHGGQ FISYDIFGSL FEITSKYRPP IIPIGRGAYG IVCSVLDTET 70 80 90 100 110 120 NELVAMKKIA NAFDNHMDAK RTLREIKLLR HLDHENIIAI RDVVPPPLRR QFSDVYISTE 130 140 150 160 170 180 LMDTDLHQII RSNQSLSEEH CQYFLYQLLR GLKYIHSANI IHRDLKPSNL LLNANCDLKI 190 200 210 220 230 240 CDFGLARPTS ENDFMTEYVV TRWYRAPELL LNSSDYTAAI DVWSVGCIFM ELMNRKPLFP 250 260 270 280 290 300 GKDHVHQMRL LTELLGTPTE SDLGFTHNED AKRYIRQLPN FPRQPLAKLF SHVNPMAIDL 310 320 330 340 350 360 VDRMLTFDPN RRITVEQALN HQYLAKLHDP NDEPICQKPF SFEFEQQPLD EEQIKEMIYQ 370 EAIALNPTYG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"ATMPKs: a gene family of plant MAP kinases in Arabidopsis thaliana." Mizoguchi T., Hayashida N., Yamaguchi-Shinozaki K., Kamada H., Shinozaki K. FEBS Lett. 336:440-444(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana." Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"A gene encoding a mitogen-activated protein kinase kinase kinase is induced simultaneously with genes for a mitogen-activated protein kinase and an S6 ribosomal protein kinase by touch, cold, and water stress in Arabidopsis thaliana." Mizoguchi T., Irie K., Hirayama T., Hayashida N., Yamaguchi-Shinozaki K., Matsumoto K., Shinozaki K. Proc. Natl. Acad. Sci. U.S.A. 93:765-769(1996) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
[6]	"Functional analysis of oxidative stress-activated mitogen-activated protein kinase cascade in plants." Kovtun Y., Chiu W.-L., Tena G., Sheen J. Proc. Natl. Acad. Sci. U.S.A. 97:2940-2945(2000) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION.
[7]	"Different protein kinase families are activated by osmotic stresses in Arabidopsis thaliana cell suspensions. Involvement of the MAP kinases AtMPK3 and AtMPK6." Droillard M.-J., Boudsocq M., Barbier-Brygoo H., Lauriere C. FEBS Lett. 527:43-50(2002) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION.
[8]	"Activation of AtMEK1, an Arabidopsis mitogen-activated protein kinase kinase, in vitro and in vivo: analysis of active mutants expressed in E. coli and generation of the active form in stress response in seedlings." Matsuoka D., Nanmori T., Sato K., Fukami Y., Kikkawa U., Yasuda T. Plant J. 29:637-647(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION.
[9]	"MAP kinase signalling cascade in Arabidopsis innate immunity." Asai T., Tena G., Plotnikova J., Willmann M.R., Chiu W.-L., Gomez-Gomez L., Boller T., Ausubel F.M., Sheen J. Nature 415:977-983(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ENZYME REGULATION.
[10]	"Mitogen-activated protein kinase cascades in plants: a new nomenclature." MAPK group Trends Plant Sci. 7:301-308(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE.
[11]	"NDP kinase 2 interacts with two oxidative stress-activated MAPKs to regulate cellular redox state and enhances multiple stress tolerance in transgenic plants." Moon H., Lee B., Choi G., Shin D., Prasad D.T., Lee O., Kwak S.-S., Kim D.H., Nam J., Bahk J., Hong J.C., Lee S.Y., Cho M.J., Lim C.O., Yun D.-J. Proc. Natl. Acad. Sci. U.S.A. 100:358-363(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NDPK2.
[12]	"Stress hormone-independent activation and nuclear translocation of mitogen-activated protein kinases in Arabidopsis thaliana during ozone exposure." Ahlfors R., Macioszek V., Rudd J., Brosche M., Schlichting R., Scheel D., Kangasjarvi J. Plant J. 40:512-522(2004) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION, SUBCELLULAR LOCATION, INDUCTION.
[13]	"RNA interference-based (RNAi) suppression of AtMPK6, an Arabidopsis mitogen-activated protein kinase, results in hypersensitivity to ozone and misregulation of AtMPK3." Miles G.P., Samuel M.A., Zhang Y., Ellis B.E. Environ. Pollut. 138:230-237(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[14]	"Ancient signals: comparative genomics of plant MAPK and MAPKK gene families." Hamel L.P., Nicole M.C., Sritubtim S., Morency M.J., Ellis M., Ehlting J., Beaudoin N., Barbazuk B., Klessig D., Lee J., Martin G., Mundy J., Ohashi Y., Scheel D., Sheen J., Xing T., Zhang S., Seguin A., Ellis B.E. Trends Plant Sci. 11:192-198(2006) [PubMed] [Europe PMC] [Abstract] Cited for: GENE FAMILY.
[15]	"Arabidopsis MAPK phosphatase 2 (MKP2) positively regulates oxidative stress tolerance and inactivates the MPK3 and MPK6 MAPKs." Lee J.S., Ellis B.E. J. Biol. Chem. 282:25020-25029(2007) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION, DEPHOSPHORYLATION.
[16]	"Stomatal development and patterning are regulated by environmentally responsive mitogen-activated protein kinases in Arabidopsis." Wang H., Ngwenyama N., Liu Y., Walker J.C., Zhang S. Plant Cell 19:63-73(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[17]	"Trojan horse strategy in Agrobacterium transformation: abusing MAPK defense signaling." Djamei A., Pitzschke A., Nakagami H., Rajh I., Hirt H. Science 318:453-456(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ENZYME REGULATION, INTERACTION WITH VIP1.
[18]	"Dual control of nuclear EIN3 by bifurcate MAPK cascades in C2H4 signalling." Yoo S.D., Cho Y.H., Tena G., Xiong Y., Sheen J. Nature 451:789-795(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ENZYME REGULATION.
[19]	"A fungal-responsive MAPK cascade regulates phytoalexin biosynthesis in Arabidopsis." Ren D., Liu Y., Yang K.Y., Han L., Mao G., Glazebrook J., Zhang S. Proc. Natl. Acad. Sci. U.S.A. 105:5638-5643(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[20]	"MAPK phosphatase MKP2 mediates disease responses in Arabidopsis and functionally interacts with MPK3 and MPK6." Lumbreras V., Vilela B., Irar S., Sole M., Capellades M., Valls M., Coca M., Pages M. Plant J. 63:1017-1030(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DSPTP1B/MKP2.
[21]	"Arabidopsis MKK4 mediates osmotic-stress response via its regulation of MPK3 activity." Kim S.H., Woo D.H., Kim J.M., Lee S.Y., Chung W.S., Moon Y.H. Biochem. Biophys. Res. Commun. 412:150-154(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ENZYME REGULATION.
[22]	"A MAPK cascade downstream of ERECTA receptor-like protein kinase regulates Arabidopsis inflorescence architecture by promoting localized cell proliferation." Meng X., Wang H., He Y., Liu Y., Walker J.C., Torii K.U., Zhang S. Plant Cell 24:4948-4960(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D21839 mRNA. Translation: BAA04866.1. AL138657 Genomic DNA. Translation: CAB75493.1. AL157735 Genomic DNA. No translation available. CP002686 Genomic DNA. Translation: AEE78054.1. AF386961 mRNA. Translation: AAK62406.1. BT000007 mRNA. Translation: AAN15326.1.
PIR	S40469. T47504.
RefSeq	NP_190150.1. NM_114433.2.
UniGene	At.263.
3D structure databases
ProteinModelPortal	Q39023.
SMR	Q39023. Positions 31-361.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
BioGrid	9026. 29 interactions.
DIP	DIP-768N.
IntAct	Q39023. 18 interactions.
MINT	MINT-8086190.
Proteomic databases
PaxDb	Q39023.
PRIDE	Q39023.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT3G45640.1; AT3G45640.1; AT3G45640.
GeneID	823706.
KEGG	ath:AT3G45640.
Organism-specific databases
GeneFarm	828. 89.
TAIR	AT3G45640.
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000233024.
InParanoid	Q39023.
KO	K04371.
OMA	PFDHTMF.
PhylomeDB	Q39023.
ProtClustDB	CLSN2684763.
Enzyme and pathway databases
BioCyc	ARA:AT3G45640-MONOMER.
BRENDA	2.7.11.24. 399.
Gene expression databases
ArrayExpress	Q39023.
Genevestigator	Q39023.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR003527. MAP_kinase_CS. IPR000719. Prot_kinase_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. SSF56112. 1 hit.
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...
Other
PRO	Q39023.

Entry information

Entry name

MPK3_ARATH

Accession

Primary (citable) accession number: Q39023
Secondary accession number(s): Q9M1E3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	June 6, 2002
Last modified:	April 16, 2014
This is version 132 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program