MPK4A_PHYPA
ID MPK4A_PHYPA Reviewed; 375 AA.
AC A9T142;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Mitogen-activated protein kinase 4a {ECO:0000303|PubMed:27268428};
DE EC=2.7.11.24 {ECO:0000255, ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|RuleBase:RU361165, ECO:0000269|PubMed:27268428};
DE AltName: Full=MAP kinase 4a {ECO:0000303|PubMed:27268428};
DE Short=PpMPK4a {ECO:0000303|PubMed:27268428};
GN Name=MPK4a; ORFNames=PHYPADRAFT_217865 {ECO:0000312|EMBL:EDQ62847.1};
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION,
RP PHOSPHORYLATION AT THR-197 AND TYR-199, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Gransden 2004 {ECO:0000303|PubMed:27268428};
RX PubMed=27268428; DOI=10.1105/tpc.15.00774;
RA Bressendorff S., Azevedo R., Kenchappa C.S., Ponce de Leon I., Olsen J.V.,
RA Rasmussen M.W., Erbs G., Newman M.A., Petersen M., Mundy J.;
RT "An innate immunity pathway in the Moss Physcomitrella patens.";
RL Plant Cell 28:1328-1342(2016).
RN [2] {ECO:0000312|EMBL:EDQ62847.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004;
RX PubMed=18079367; DOI=10.1126/science.1150646;
RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA Boore J.L.;
RT "The Physcomitrella genome reveals evolutionary insights into the conquest
RT of land by plants.";
RL Science 319:64-69(2008).
CC -!- FUNCTION: The CERK1, MEKK1a/b, MKK1a/b/c and MPK4a/b proteins are
CC involved in pathogen defense. The pathway induces rapid growth
CC inhibition, cell wall depositions and accumulation of defense-related
CC transcripts. This protein is required for innate immunity triggered by
CC pathogen-associated molecular patterns (PAMPs). Involved in resistance
CC to necrotrophic fungi B.cinerea and A.brassicicola. Involved in the
CC transduction of signals from chitosan perception to the activation of
CC defense genes. {ECO:0000269|PubMed:27268428}.
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 Evidence={ECO:0000255|RuleBase:RU361165,
CC ECO:0000269|PubMed:27268428};
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; Evidence={ECO:0000255|RuleBase:RU361165,
CC ECO:0000269|PubMed:27268428};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|RuleBase:RU361165};
CC -!- ACTIVITY REGULATION: Activated by threonine and tyrosine
CC phosphorylation. Activated in response to bacterial and fungal
CC pathogen-associated molecular patterns (PAMPs) including chitin,
CC chitosan and peptidyl glycans (PGNs). Activation in response to chitin
CC requires the CERK1, MEKK1a/b, MKK1a/b/c and MPK4a/b signaling pathway.
CC Activated in response to necrotrophic fungus B.cinerea spores. Not
CC activated in response to osmotic stress. {ECO:0000269|PubMed:27268428}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27268428}. Nucleus
CC {ECO:0000269|PubMed:27268428}. Note=Localization to the cytoplasm and
CC nucleus does not change significantly following chitin treatment.
CC {ECO:0000269|PubMed:27268428}.
CC -!- TISSUE SPECIFICITY: Expressed strongly in the apical cells of
CC caulonemal air filaments and rhizoids in fully developed plants and
CC less strongly, but readily detectable in filamentous protonemal tissue
CC at the edge of the plant consisting of both chloronema and caulonema.
CC When filamentous growth of protonema is promoted, the expression is
CC strongest in newly formed apical tip cells of protonemal tissue.
CC {ECO:0000269|PubMed:27268428}.
CC -!- INDUCTION: Up-regulated in response to chitosan within 15 min, peaks 8-
CC fold at 2 h, and returns to basal levels by 8 h.
CC {ECO:0000269|PubMed:27268428}.
CC -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC whose phosphorylation activates the MAP kinases. {ECO:0000305}.
CC -!- PTM: Dually phosphorylated on Thr-197 and Tyr-199, which activates the
CC enzyme. Phosphorylated in response to pathogen-associated molecular
CC pattern (PAMP) chitin and in response to necrotrophic fungus B.cinerea
CC spores. Not phosphorylated in response to osmotic stress.
CC {ECO:0000269|PubMed:27268428}.
CC -!- DISRUPTION PHENOTYPE: Significantly reduced chitin-induced cell wall-
CC associated depositions. Reduced accumulation of PAL4, CHS, ERF2, alpha-
CC DOX and LOX7 transcripts in response to chitin or chitosan. Susceptible
CC to necrotrophic fungus B.cinerea, characterized by the symptoms of
CC browning protonema and stems becoming visible 2 days after the
CC infection leading to host cell death. Reactive oxygen species (ROS)
CC production is detected in infected tissues, and phenolic compounds are
CC incorporated in cell walls in contact with B.cinerea hyphae, especially
CC around the point of hyphal penetration, but there are no clear
CC differences compared to wild-type. Susceptible also to necrotrophic
CC fungus A.brassicicola characterized by the production of significantly
CC more spores 4 days after the infection compared to wild-type.
CC Transcript levels of SnRK2 proteins respond similarly to wild-type in
CC response to NaCl treatment. {ECO:0000269|PubMed:27268428}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. MAP kinase subfamily. {ECO:0000305}.
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DR EMBL; DS545038; EDQ62847.1; -; Genomic_DNA.
DR RefSeq; XP_001772376.1; XM_001772324.1.
DR AlphaFoldDB; A9T142; -.
DR SMR; A9T142; -.
DR STRING; 3218.PP1S149_39V6.3; -.
DR iPTMnet; A9T142; -.
DR EnsemblPlants; Pp3c26_400V3.1; Pp3c26_400V3.1; Pp3c26_400.
DR EnsemblPlants; Pp3c26_400V3.2; Pp3c26_400V3.2; Pp3c26_400.
DR Gramene; Pp3c26_400V3.1; Pp3c26_400V3.1; Pp3c26_400.
DR Gramene; Pp3c26_400V3.2; Pp3c26_400V3.2; Pp3c26_400.
DR eggNOG; KOG0660; Eukaryota.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; A9T142; -.
DR OrthoDB; 741207at2759; -.
DR Proteomes; UP000006727; Chromosome 26.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004707; F:MAP kinase activity; IDA:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0002221; P:pattern recognition receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0010468; P:regulation of gene expression; IMP:UniProtKB.
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 ATP-binding; Cytoplasm; Immunity; Innate immunity; Kinase; Magnesium;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Plant defense;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..375
FT /note="Mitogen-activated protein kinase 4a"
FT /id="PRO_0000443378"
FT DOMAIN 39..325
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOTIF 197..199
FT /note="TXY"
FT /evidence="ECO:0000305"
FT ACT_SITE 165
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 45..53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 68
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 197
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:27268428"
FT MOD_RES 199
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:27268428"
SQ SEQUENCE 375 AA; 42832 MW; 51F086D6CC5C4F58 CRC64;
METSSGTPEL KVISTPTYGG HYVKYVVAGT DFEVTARYKP PLRPIGRGAY GIVCSLFDTV
TGEEVAVKKI GNAFDNRIDA KRTLREIKLL RHMDHENVVA ITDIIRPPTR ENFNDVYIVY
ELMDTDLHQI IRSNQALTED HCQYFLYQIL RGLKYIHSAN VLHRDLKPTN LLVNANCDLK
IADFGLARTL SETDFMTEYV VTRWYRAPEL LLNCSAYTAA IDIWSVGCIF MELLNRSALF
PGRDYVHQLR LITELIGTPE DRDLGFLRSD NARRYIKHLP RQSPIPLTQK FRGINRSALD
LVEKMLVFDP AKRITVEAAL AHPYLASLHD INDEPASVSP FEFDFEEPSI SEEHIKDLIW
REALDCSLGP DDMVQ
