M2K1B_PHYPA
ID M2K1B_PHYPA Reviewed; 342 AA.
AC A9SR33;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2018, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Mitogen-activated protein kinase kinase 1b {ECO:0000303|PubMed:27268428};
DE EC=2.7.12.2 {ECO:0000250|UniProtKB:Q9S7U9};
DE AltName: Full=MAP kinase kinase 1b {ECO:0000303|PubMed:27268428};
DE AltName: Full=PpMKK1b {ECO:0000303|PubMed:27268428};
GN Name=MKK1b {ECO:0000303|PubMed:27268428};
GN ORFNames=PHYPADRAFT_230484 {ECO:0000312|EMBL:EDQ66344.1};
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:EDQ66344.1}
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: No change in 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 induced similarly to wild-type.
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 -!- SEQUENCE CAUTION:
CC Sequence=EDQ66344.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DS544995; EDQ66344.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001768791.1; XM_001768739.1.
DR AlphaFoldDB; A9SR33; -.
DR SMR; A9SR33; -.
DR STRING; 3218.PP1S106_83V6.1; -.
DR EnsemblPlants; Pp3c16_11030V3.1; Pp3c16_11030V3.1; Pp3c16_11030.
DR EnsemblPlants; Pp3c16_11030V3.2; Pp3c16_11030V3.2; Pp3c16_11030.
DR Gramene; Pp3c16_11030V3.1; Pp3c16_11030V3.1; Pp3c16_11030.
DR Gramene; Pp3c16_11030V3.2; Pp3c16_11030V3.2; Pp3c16_11030.
DR eggNOG; KOG0581; Eukaryota.
DR HOGENOM; CLU_000288_63_23_1; -.
DR InParanoid; A9SR33; -.
DR OMA; TEPNICI; -.
DR OrthoDB; 688282at2759; -.
DR Proteomes; UP000006727; Chromosome 16.
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..342
FT /note="Mitogen-activated protein kinase kinase 1b"
FT /id="PRO_0000443445"
FT DOMAIN 66..328
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 190
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 72..80
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 342 AA; 38730 MW; F6B7783D1691615C CRC64;
MSRRHRTGGL RVAVPKQENS IHRFLTANGV FHDDDIQLDH MGLRVVSSES TAYANPPDAQ
LSLADLEAVR VLGKGAGGSV QLVRHKWTND IYALKGIQMN INETVRKQIV QELKINQLTL
HQCPYIVKCY HSFYHNGIIS IVLEYMDRGS LADIIKQTKQ IPEPYLAVIS NQVLKGLNYL
HQVRHIIHRD IKPSNLLINQ KGEVKISDFG VSAVLISSMA QRDTFVGTYT YMSPERLGGQ
SYAYDSDIWS LGLTILECAL GYFPYRPPGQ EEGWNNFFML MELVINQPPV AAPPDKFSPE
FCSFIAACIQ KRPGDRLSTA DLLKHPFLQK YSEEEYHLSN LR
