M3K1A_PHYPA
ID M3K1A_PHYPA Reviewed; 759 AA.
AC A9SY39;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2018, sequence version 2.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase 1a {ECO:0000305};
DE Short=PpMEKK1a {ECO:0000303|PubMed:27268428};
DE EC=2.7.11.25 {ECO:0000250|UniProtKB:Q39008};
DE AltName: Full=MAP kinase kinase kinase 1a {ECO:0000303|PubMed:27268428};
GN Name=MEKK1a {ECO:0000303|PubMed:27268428};
GN ORFNames=PHYPADRAFT_15847 {ECO:0000312|EMBL:EDQ63834.1};
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:EDQ63834.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (PARTIAL).
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 responses to chitin and acts
CC redundantly with MEKK1b. {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=2.7.11.25;
CC Evidence={ECO:0000250|UniProtKB:Q39008};
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=2.7.11.25; Evidence={ECO:0000250|UniProtKB:Q39008};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q39008}.
CC -!- INDUCTION: Up-regulated in response to chitosan.
CC {ECO:0000269|PubMed:27268428}.
CC -!- DISRUPTION PHENOTYPE: Reduced chitin-induced MPK phosphorylation.
CC Strongly reduced chitin-induced cell wall-associated depositions.
CC Reduced accumulation of PAL4 and CHS transcripts in response to chitin.
CC Double deletion mutant MEKK1a/MEKK1b does not phosphorylate MPK and is
CC unable to induce the depositions in response to chitin. The growth of
CC the double mutant is inhibited within 1 min after chitin exposure as in
CC wild-type. {ECO:0000269|PubMed:27268428}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDQ63834.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DS545025; EDQ63834.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001771274.1; XM_001771222.1.
DR AlphaFoldDB; A9SY39; -.
DR SMR; A9SY39; -.
DR STRING; 3218.PP1S136_5V6.3; -.
DR EnsemblPlants; Pp3c7_4010V3.1; PAC:32925011.CDS.1; Pp3c7_4010.
DR EnsemblPlants; Pp3c7_4010V3.2; PAC:32925012.CDS.1; Pp3c7_4010.
DR Gramene; Pp3c7_4010V3.1; PAC:32925011.CDS.1; Pp3c7_4010.
DR Gramene; Pp3c7_4010V3.2; PAC:32925012.CDS.1; Pp3c7_4010.
DR eggNOG; KOG0198; Eukaryota.
DR HOGENOM; CLU_000288_2_6_1; -.
DR InParanoid; A9SY39; -.
DR OrthoDB; 630495at2759; -.
DR Proteomes; UP000006727; Chromosome 7.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; ISS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00109; TYRKINASE.
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; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW Plant defense; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..759
FT /note="Mitogen-activated protein kinase kinase kinase 1a"
FT /id="PRO_0000443376"
FT DOMAIN 426..679
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 549
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 432..440
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 454
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 759 AA; 83316 MW; 2C9A606396F4EAD6 CRC64;
MIEERGSSRG SREDRGSSRG SSRGSFEDKG SSHDWKGMGG STPRPRLTRL VAKKDRNYDA
KVDSDFDDDS SVHSTSSPRL SPASSDNLSK ITIGQQSFRV GGDVDNLKAL YEALGATSPA
ALGIEASDWE SRRKSAVYSR PTSPPRVSHD TGQSSYSHDF QFPASRVDSS LESPPLSPRG
LAPMSPVRPI EVEWRKHRNN YAKPTISNRP GRENNPLKPS QPPPTMFPQS SGLRTPDPLP
PIDTSTSRLG RESLELQNRH TTLGAYSPPG LRKVHSELTG LVSARSDGAG WASDIESAKR
NEDLAVASPV FRDNLPSAAV AMPNGSLVRA SFTPRDSNRM NSVRSNSHGL RWNSCHAQEA
EAIAKTALEE TSNGLRIEDP ERIRDLEKPS PLIIEKVDEP LSEVSSSVST ESSPSVIPKR
PPWDTWAKGE FLGSGTFGSV YEGVARNGTF FAVKEVNLAD EGKLGRQAVK QLEREIALLS
DIQHPNIVQY LGTERTEDKL YIFLELLNKG SLANLYRKYG LFYEQIKAYT EQILTGLKYL
HDRKIIHRDI KCANILVDTN GVVKLADFGM AKQVEKFGFA KSFVGSAHWM APEVVDPKQQ
YNFAADIWSL GCTVLEMATE GPPFGELEFI AVFWKIGRGE APLIPDDLED ELKDFIAQCL
QVDASKRPTC DMLLAHPFIT GEEMTGPVTQ MGTPGLSTIS EERSVDMSVT SSIAVSSNSG
TSPRVIENLV NHLSIERRPK SMRTLRSELS MSSAESIAS
