M2K1A_PHYPA
ID M2K1A_PHYPA Reviewed; 352 AA.
AC A9RWC9;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Mitogen-activated protein kinase kinase 1a {ECO:0000303|PubMed:27268428};
DE EC=2.7.12.2 {ECO:0000250|UniProtKB:Q9S7U9};
DE AltName: Full=MAP kinase kinase 1a {ECO:0000303|PubMed:27268428};
DE Short=PpMKK1a {ECO:0000303|PubMed:27268428};
GN Name=MKK1a {ECO:0000303|PubMed:27268428};
GN ORFNames=PHYPADRAFT_206232 {ECO:0000312|EMBL:EDQ76757.1};
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, INDUCTION, AND DISRUPTION
RP 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:EDQ76757.1}
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 full defense response to
CC fungal pathogen chitin. {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=2.7.12.2;
CC Evidence={ECO:0000250|UniProtKB:Q9S7U9};
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=2.7.12.2; Evidence={ECO:0000250|UniProtKB:Q9S7U9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.2;
CC Evidence={ECO:0000250|UniProtKB:Q9S7U9};
CC -!- INDUCTION: Slightly induced in response to chitosan.
CC {ECO:0000269|PubMed:27268428}.
CC -!- DISRUPTION PHENOTYPE: Slighty reduced chitin-induced cell wall
CC modification compared to wild-type. Modest reduction in chitin-induced
CC MPK phosphorylation. The levels of mRNAs of the defense-related PAL4
CC and CHS are being less induced following chitin treatment.
CC {ECO:0000269|PubMed:27268428}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
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DR EMBL; DS544921; EDQ76757.1; -; Genomic_DNA.
DR RefSeq; XP_001758355.1; XM_001758303.1.
DR AlphaFoldDB; A9RWC9; -.
DR SMR; A9RWC9; -.
DR STRING; 3218.PP1S32_219V6.1; -.
DR EnsemblPlants; Pp3c10_22760V3.1; Pp3c10_22760V3.1; Pp3c10_22760.
DR EnsemblPlants; Pp3c10_22760V3.2; Pp3c10_22760V3.2; Pp3c10_22760.
DR Gramene; Pp3c10_22760V3.1; Pp3c10_22760V3.1; Pp3c10_22760.
DR Gramene; Pp3c10_22760V3.2; Pp3c10_22760V3.2; Pp3c10_22760.
DR eggNOG; KOG0581; Eukaryota.
DR HOGENOM; CLU_000288_63_23_1; -.
DR InParanoid; A9RWC9; -.
DR OMA; ATQELPW; -.
DR OrthoDB; 688282at2759; -.
DR Proteomes; UP000006727; Chromosome 10.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004708; F:MAP kinase kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:RHEA.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0010200; P:response to chitin; IMP:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Plant defense; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..352
FT /note="Mitogen-activated protein kinase kinase 1a"
FT /id="PRO_0000443373"
FT DOMAIN 69..331
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 193
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 75..83
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 352 AA; 38952 MW; 464909AD03951916 CRC64;
MRRARGKFKG GNSALRVNVP KENAISDYVT ASGTFQDGDI MLNKEGIRVV SQTQTSTPAA
NGNISLSDLE TVKVLGKGSG GVVQLVRHKW TNETYALKVI HMNIEETTRK QIVQELKINH
ASQCPYVVIC YHAFYNNGLI SIVLEYMDGG SLADIMKELE PKCIKEPNLG VVCKQVLLGL
MYLHQTRHII HRDIKPSNLL VNHKGEVKIS DFGVSAVLAN SMAVRDTFVG TCTYMSPERV
LGGTYGFDSD IWSLGLTLLE CALGKYPYQP PGSEEGWMNF YELLQTIVDQ PPPVAPADQF
SPEFCSFISA CLQKDPKCRP TAAELLNHPF VNKYDEEEYG LAKLLPPLVP LA
