MPK4B_PHYPA
ID MPK4B_PHYPA Reviewed; 380 AA.
AC A9S9Q8;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Mitogen-activated protein kinase 4b {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 4b {ECO:0000303|PubMed:27268428};
DE Short=PpMPK4b {ECO:0000303|PubMed:27268428};
GN Name=MPK4b {ECO:0000303|PubMed:27268428};
GN ORFNames=PHYPADRAFT_126277 {ECO:0000312|EMBL:EDQ72109.1};
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 {ECO:0000312|EMBL:EDQ72109.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, INDUCTION, AND PHOSPHORYLATION AT THR-201 AND TYR-203.
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:EDQ72109.1}
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 may act redundantly with MPK4a in innate
CC immunity triggered by pathogen-associated molecular patterns (PAMPs).
CC May also be involved in resistance to necrotrophic fungi B.cinerea.
CC {ECO:0000305|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 Slightly activated in response to necrotrophic fungus B.cinerea spores.
CC Not activated in response to osmotic stress.
CC {ECO:0000269|PubMed:27268428}.
CC -!- INDUCTION: Up-regulated only marginally in response to chitosan.
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-201 and Tyr-203, which activates the
CC enzyme. Phosphorylated in response to pathogen-associated molecular
CC pattern (PAMP) chitin and to a lot lesser extent in response to
CC necrotrophic fungus B.cinerea spores. Not phosphorylated in response to
CC osmotic stress. {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; DS544948; EDQ72109.1; -; Genomic_DNA.
DR RefSeq; XP_001763232.1; XM_001763180.1.
DR AlphaFoldDB; A9S9Q8; -.
DR SMR; A9S9Q8; -.
DR STRING; 3218.PP1S59_325V6.1; -.
DR iPTMnet; A9S9Q8; -.
DR EnsemblPlants; Pp3c1_22480V3.1; Pp3c1_22480V3.1; Pp3c1_22480.
DR EnsemblPlants; Pp3c1_22480V3.2; Pp3c1_22480V3.2; Pp3c1_22480.
DR Gramene; Pp3c1_22480V3.1; Pp3c1_22480V3.1; Pp3c1_22480.
DR Gramene; Pp3c1_22480V3.2; Pp3c1_22480V3.2; Pp3c1_22480.
DR eggNOG; KOG0660; Eukaryota.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; A9S9Q8; -.
DR OMA; TERCIFR; -.
DR OrthoDB; 741207at2759; -.
DR Proteomes; UP000006727; Chromosome 1.
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 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; Immunity; Innate immunity; Kinase; Magnesium;
KW Nucleotide-binding; Phosphoprotein; Plant defense; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..380
FT /note="Mitogen-activated protein kinase 4b"
FT /id="PRO_0000443379"
FT DOMAIN 43..329
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOTIF 201..203
FT /note="TXY"
FT /evidence="ECO:0000305"
FT ACT_SITE 169
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 49..57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 201
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:27268428"
FT MOD_RES 203
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:27268428"
SQ SEQUENCE 380 AA; 43488 MW; 03783C0DAA66E4FC CRC64;
MDVAGAGGGG AADGNIQGVP THNGEYTQYN IFGNLFEVSR KYVPPIRPIG RGAYGIVCSA
VNSETGEEVA IKKIGNAFDN RIDAKRTLRE IKLLRHMDHE NIVAIRDIIR PPTRENFNDV
YIVYELMDTD LHQIIRSNQP LTEDHCQYFL YQLLRGLKYI HSAKVLHRDL KPSNLLLNAN
CDLKICDFGL ARTTSETDFM TEYVVTRWYR APELLLNCSE YTAAIDVWSV GCIFMELLNR
EPLFPGRDYV QQLRLITELI GSPEDHDLGF LRSDNARRYI RQLPRFARQP LDRKFPNMGP
AAIDLVEHML RFDPARRITV EEALAHPYLA TLHDINDEPI CHSPFEFDFE QPSFTEEHIK
ELIMMEAIAF NPGNVGDMMS
