M3K5G_ARATH
ID M3K5G_ARATH Reviewed; 716 AA.
AC Q9C5H5; O23721; Q0WLS6; Q93ZH4; Q9FKZ5;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase 5 {ECO:0000303|PubMed:27679653};
DE EC=2.7.11.25 {ECO:0000269|PubMed:27679653};
DE AltName: Full=MAP3K gamma protein kinase {ECO:0000303|PubMed:10095117};
DE Short=AtMAP3Kgamma {ECO:0000303|PubMed:10095117};
GN Name=MAPKKK5 {ECO:0000303|PubMed:27679653};
GN Synonyms=MAP3KG {ECO:0000303|PubMed:10095117};
GN OrderedLocusNames=At5g66850 {ECO:0000312|Araport:AT5G66850};
GN ORFNames=MUD21.11 {ECO:0000312|EMBL:BAB08627.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 345-716, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia; TISSUE=Pollen;
RX PubMed=10095117; DOI=10.1016/s0378-1119(99)00012-8;
RA Jouannic S., Hamal A., Leprince A.-S., Tregear J.W., Kreis M., Henry Y.;
RT "Characterisation of novel plant genes encoding MEKK/STE11 and RAF-related
RT protein kinases.";
RL Gene 229:171-181(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 521-716.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=10375615; DOI=10.1016/s0378-1119(99)00152-3;
RA Jouannic C., Hamal A., Leprince A.-S., Tregear J., Kreis M., Henry Y.;
RT "Plant MAP kinase kinase kinases structure, classification and evolution.";
RL Gene 233:1-11(1999).
RN [7]
RP GENE FAMILY.
RX PubMed=12119167; DOI=10.1016/s1360-1385(02)02302-6;
RG MAPK group;
RT "Mitogen-activated protein kinase cascades in plants: a new nomenclature.";
RL Trends Plant Sci. 7:301-308(2002).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF LYS-375; SER-617; SER-622;
RP SER-658; SER-660; THR-677 AND SER-685, INTERACTION WITH PBL27; MKK2; MKK4
RP AND MKK5, SUBCELLULAR LOCATION, INDUCTION BY CHITIN, PHOSPHORYLATION AT
RP SER-617; SER-622; SER-658; SER-660; THR-677 AND SER-685 BY PBL27, AND
RP CATALYTIC ACTIVITY.
RC STRAIN=cv. Columbia;
RX PubMed=27679653; DOI=10.15252/embj.201694248;
RA Yamada K., Yamaguchi K., Shirakawa T., Nakagami H., Mine A., Ishikawa K.,
RA Fujiwara M., Narusaka M., Narusaka Y., Ichimura K., Kobayashi Y.,
RA Matsui H., Nomura Y., Nomoto M., Tada Y., Fukao Y., Fukamizo T., Tsuda K.,
RA Shirasu K., Shibuya N., Kawasaki T.;
RT "The Arabidopsis CERK1-associated kinase PBL27 connects chitin perception
RT to MAPK activation.";
RL EMBO J. 35:2468-2483(2016).
CC -!- FUNCTION: Mitogen-activated protein kinase (MAPK) involved in the
CC transduction of signal between the host cell surface chitin receptor
CC complex CERK1-LYK5 and the intracellular MAPK cascade that leads to
CC chitin-induced immunity. Phosphorylates and activates MAPK targets
CC (e.g. MKK4, MKK5, and possibly MKK2) when phosphorylated by PBL27 after
CC elicitation by chitin. Required for resistance to the fungus
CC A.brassicicola. {ECO:0000269|PubMed:27679653}.
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:0000269|PubMed:27679653};
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:0000269|PubMed:27679653};
CC -!- SUBUNIT: Interacts with PBL27 at the plasma membrane; disassociation is
CC induced by chitin perception by the CERK1 complex. Interacts with MKK2,
CC MKK4, and MKK5 mainly in the cytosol. {ECO:0000269|PubMed:27679653}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27679653}.
CC Cytoplasm, cytosol {ECO:0000269|PubMed:27679653}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in flower buds. Also present in
CC pollen, roots, leaves and seedlings, and, at low levels, in stems and
CC immature siliques. {ECO:0000269|PubMed:10095117}.
CC -!- INDUCTION: Induced by chitin. Levels are regulated in a proteasome-
CC dependent manner (at proteome level). {ECO:0000269|PubMed:27679653}.
CC -!- PTM: Phosphorylated by PBL27 during chitin-mediated signaling in a
CC CERK1-dependent manner. {ECO:0000269|PubMed:27679653}.
CC -!- DISRUPTION PHENOTYPE: Normal morphology in standard conditions.
CC Impaired chitin-induced MAPK activation (e.g. MPK3, MPK4, and MPK6) and
CC altered subsequent disease resistance to A.brassicicola associated with
CC reduced levels of chitin-induced callose deposition.
CC {ECO:0000269|PubMed:27679653}.
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=BAB08627.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB010700; BAB08627.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED98271.1; -; Genomic_DNA.
DR EMBL; AF360242; AAK25952.1; -; mRNA.
DR EMBL; AY040040; AAK64098.1; -; mRNA.
DR EMBL; AY057533; AAL09773.1; -; mRNA.
DR EMBL; Y14316; CAA74696.1; -; mRNA.
DR EMBL; AK230114; BAF01931.1; -; mRNA.
DR PIR; T52621; T52621.
DR RefSeq; NP_569040.1; NM_126084.3.
DR AlphaFoldDB; Q9C5H5; -.
DR SMR; Q9C5H5; -.
DR IntAct; Q9C5H5; 1.
DR STRING; 3702.AT5G66850.1; -.
DR iPTMnet; Q9C5H5; -.
DR PaxDb; Q9C5H5; -.
DR PRIDE; Q9C5H5; -.
DR ProteomicsDB; 238811; -.
DR EnsemblPlants; AT5G66850.1; AT5G66850.1; AT5G66850.
DR GeneID; 836819; -.
DR Gramene; AT5G66850.1; AT5G66850.1; AT5G66850.
DR KEGG; ath:AT5G66850; -.
DR Araport; AT5G66850; -.
DR TAIR; locus:2174969; AT5G66850.
DR eggNOG; KOG0198; Eukaryota.
DR HOGENOM; CLU_000288_124_2_1; -.
DR InParanoid; Q9C5H5; -.
DR OrthoDB; 372687at2759; -.
DR PhylomeDB; Q9C5H5; -.
DR PRO; PR:Q9C5H5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9C5H5; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; HDA:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:GO_Central.
DR GO; GO:0000165; P:MAPK cascade; IMP:GO_Central.
DR GO; GO:0002221; P:pattern recognition receptor signaling pathway; IGI:TAIR.
DR GO; GO:0046777; P:protein autophosphorylation; HDA:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:2000071; P:regulation of defense response by callose deposition; IMP:UniProtKB.
DR GO; GO:1900424; P:regulation of defense response to bacterium; IGI:TAIR.
DR GO; GO:1900150; P:regulation of defense response to fungus; IGI:TAIR.
DR GO; GO:0045088; P:regulation of innate immune response; IMP:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
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.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Cytoplasm; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Plant defense; Reference proteome;
KW Transferase.
FT CHAIN 1..716
FT /note="Mitogen-activated protein kinase kinase kinase 5"
FT /id="PRO_0000438543"
FT DOMAIN 346..607
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..635
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..692
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..716
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 472
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 352..360
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 375
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 617
FT /note="Phosphoserine; by PBL27"
FT /evidence="ECO:0000269|PubMed:27679653"
FT MOD_RES 622
FT /note="Phosphoserine; by PBL27"
FT /evidence="ECO:0000269|PubMed:27679653"
FT MOD_RES 658
FT /note="Phosphoserine; by PBL27"
FT /evidence="ECO:0000269|PubMed:27679653"
FT MOD_RES 660
FT /note="Phosphoserine; by PBL27"
FT /evidence="ECO:0000269|PubMed:27679653"
FT MOD_RES 677
FT /note="Phosphothreonine; by PBL27"
FT /evidence="ECO:0000269|PubMed:27679653"
FT MOD_RES 685
FT /note="Phosphoserine; by PBL27"
FT /evidence="ECO:0000269|PubMed:27679653"
FT MUTAGEN 375
FT /note="K->M: Inactive. Interacts with PBL27."
FT /evidence="ECO:0000269|PubMed:27679653"
FT MUTAGEN 617
FT /note="S->A: Slight reduction of PBL27-mediated
FT phosphorylation. Impaired PBL27-mediated phosphorylation
FT but normal interaction with PBL27, and loss of chitin-
FT induced MAPK activation and callose deposition; when
FT associated with A-622; A-658; A-660; A-677 and A-685."
FT /evidence="ECO:0000269|PubMed:27679653"
FT MUTAGEN 622
FT /note="S->A: Strong reduction of PBL27-mediated
FT phosphorylation. Impaired PBL27-mediated phosphorylation
FT but normal interaction with PBL27, and loss of chitin-
FT induced MAPK activation and callose deposition; when
FT associated with A-617; A-658; A-660; A-677 and A-685."
FT /evidence="ECO:0000269|PubMed:27679653"
FT MUTAGEN 658
FT /note="S->A: Slight reduction of PBL27-mediated
FT phosphorylation. Impaired PBL27-mediated phosphorylation
FT but normal interaction with PBL27, and loss of chitin-
FT induced MAPK activation and callose deposition; when
FT associated with A-617; A-622; A-660; A-677 and A-685."
FT /evidence="ECO:0000269|PubMed:27679653"
FT MUTAGEN 660
FT /note="S->A: Slight reduction of PBL27-mediated
FT phosphorylation. Impaired PBL27-mediated phosphorylation
FT but normal interaction with PBL27, and loss of chitin-
FT induced MAPK activation and callose deposition; when
FT associated with A-617; A-622; A-658; A-677 and A-685."
FT /evidence="ECO:0000269|PubMed:27679653"
FT MUTAGEN 677
FT /note="T->A: Impaired PBL27-mediated phosphorylation but
FT normal interaction with PBL27, and loss of chitin-induced
FT MAPK activation and callose deposition; when associated
FT with A-617; A-622; A-658; A-660 and A-685."
FT /evidence="ECO:0000269|PubMed:27679653"
FT MUTAGEN 685
FT /note="S->A: Slight reduction of PBL27-mediated
FT phosphorylation. Impaired PBL27-mediated phosphorylation
FT but normal interaction with PBL27, and loss of chitin-
FT induced MAPK activation and callose deposition; when
FT associated with A-617; A-622; A-658; A-660 and A-677."
FT /evidence="ECO:0000269|PubMed:27679653"
FT CONFLICT 347
FT /note="K -> E (in Ref. 3; AAL09773)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 716 AA; 79319 MW; 9071054F2C6C68DD CRC64;
MRWLPQISFS SPSSSPSSSL KPVASYSESP DPDRNQDRDR FHRRLFRFNR GRLTRQRKLR
HLTDDDVLLG ERRASTSSST FDSGLTRSPS AFTAVPRSPS AVPLPLPLPL PEVAGIRNAA
NARGLDDRDR DPERLISDRT SSGPPLTSVN GGFARDSRKA TENSSYQDFS PRNRNGYWVN
IPTMSAPTSP YMSPVPSPQR KSTGHDLPFF YLPPKSNQAW SAPDMPLDTS GLPPPAFYDI
TAFSTDNSPI HSPQPRSPRK QIRSPQPSRP SSPLHSVDSS APPRDSVSSP LHPRLSTDVT
NGRRDCCNVH PLPLPPGATC SSSSAASVPS PQAPLKLDSF PMNSQWKKGK LIGRGTFGSV
YVASNSETGA LCAMKEVELF PDDPKSAECI KQLEQEIKLL SNLQHPNIVQ YFGSETVEDR
FFIYLEYVHP GSINKYIRDH CGTMTESVVR NFTRHILSGL AYLHNKKTVH RDIKGANLLV
DASGVVKLAD FGMAKHLTGQ RADLSLKGSP YWMAPELMQA VMQKDSNPDL AFAVDIWSLG
CTIIEMFTGK PPWSEFEGAA AMFKVMRDSP PIPESMSPEG KDFLRLCFQR NPAERPTASM
LLEHRFLKNS LQPTSPSNSD VSQLFNGMNI TEPSSRREKP NFKLDQVPRA RNMTSSESES
GQQQQQQQYR SPDLTGTVNR LSPRSTLEAI PSPCPSQRPK PSSSDRRRTG VTSDHL
