M2K1C_PHYPA
ID M2K1C_PHYPA Reviewed; 346 AA.
AC A9S5R3;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Mitogen-activated protein kinase kinase 1c {ECO:0000303|PubMed:27268428};
DE EC=2.7.12.2 {ECO:0000250|UniProtKB:Q9S7U9};
DE AltName: Full=MAP kinase kinase 1c {ECO:0000303|PubMed:27268428};
DE AltName: Full=PpMKK1c {ECO:0000303|PubMed:27268428};
GN Name=MKK1c {ECO:0000303|PubMed:27268428};
GN ORFNames=PHYPADRAFT_181532 {ECO:0000312|EMBL:EDQ73493.1};
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, 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:EDQ73493.1}
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 -!- DISRUPTION PHENOTYPE: Slighty reduced chitin-induced cell wall
CC modification compared to wild-type. Significantly reduced chitin-
CC induced MPK phosphorylation. The levels of mRNAs of the defense-related
CC PAL4 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS544939; EDQ73493.1; -; Genomic_DNA.
DR RefSeq; XP_001761737.1; XM_001761685.1.
DR AlphaFoldDB; A9S5R3; -.
DR SMR; A9S5R3; -.
DR STRING; 3218.PP1S50_83V6.1; -.
DR EnsemblPlants; Pp3c25_9020V3.1; Pp3c25_9020V3.1; Pp3c25_9020.
DR EnsemblPlants; Pp3c25_9020V3.2; Pp3c25_9020V3.2; Pp3c25_9020.
DR EnsemblPlants; Pp3c25_9020V3.3; Pp3c25_9020V3.3; Pp3c25_9020.
DR Gramene; Pp3c25_9020V3.1; Pp3c25_9020V3.1; Pp3c25_9020.
DR Gramene; Pp3c25_9020V3.2; Pp3c25_9020V3.2; Pp3c25_9020.
DR Gramene; Pp3c25_9020V3.3; Pp3c25_9020V3.3; Pp3c25_9020.
DR eggNOG; KOG0581; Eukaryota.
DR InParanoid; A9S5R3; -.
DR OMA; RILMEVM; -.
DR OrthoDB; 688282at2759; -.
DR Proteomes; UP000006727; Chromosome 25.
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 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Plant defense; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..346
FT /note="Mitogen-activated protein kinase kinase 1c"
FT /id="PRO_0000443375"
FT DOMAIN 70..332
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 194
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 76..84
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 346 AA; 39138 MW; D59A6CC195834DD0 CRC64;
MSRRVRRGGL RVAVPKQETP VSKFLTASGT FQDDDIKLNH TGLRVVSSEP NLPTQTQSSS
PDGQLSIADL ELVRFLGKGA GGTVQLVRHK WTNVNYALKA IQMNINETVR KQIVQELKIN
QVTHQQCPYI VECFHSFYHN GVISMILEYM DRGSLSDIIK QQKQIPEPYL AVIASQVLKG
LEYLHQVRHI IHRDIKPSNL LINHKGEVKI SDFGVSAVLV HSLAQRDTFV GTCTYMSPER
LQGRSYAYDS DLWSLGLTLL ECALGTFPYK PAGMEEGWQN FFILMECIVN QPPAAASPDK
FSPEFCSFIE SCIRKCPSER PSTTDLLKHP FLQKYNEEEY HLSKIL
