MPK18_ARATH
ID MPK18_ARATH Reviewed; 615 AA.
AC Q9C5C0; Q9LPG7;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 4.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Mitogen-activated protein kinase 18 {ECO:0000303|PubMed:12119167, ECO:0000303|PubMed:16537113, ECO:0000303|PubMed:19392697};
DE Short=AtMPK18 {ECO:0000303|PubMed:12119167, ECO:0000303|PubMed:16537113, ECO:0000303|PubMed:19392697};
DE Short=MAP kinase 18 {ECO:0000303|PubMed:12119167, ECO:0000303|PubMed:16537113, ECO:0000303|PubMed:19392697};
DE EC=2.7.11.24;
GN Name=MPK18 {ECO:0000303|PubMed:12119167, ECO:0000303|PubMed:16537113,
GN ECO:0000303|PubMed:19392697};
GN OrderedLocusNames=At1g53510 {ECO:0000312|Araport:AT1G53510};
GN ORFNames=F22G10.12 {ECO:0000312|EMBL:AAG51978.1},
GN T3F20.17 {ECO:0000312|EMBL:AAF78438.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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] OF 13-615.
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 GENE FAMILY, AND NOMENCLATURE.
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 [5]
RP GENE FAMILY.
RX PubMed=16537113; DOI=10.1016/j.tplants.2006.02.007;
RA Hamel L.P., Nicole M.C., Sritubtim S., Morency M.J., Ellis M., Ehlting J.,
RA Beaudoin N., Barbazuk B., Klessig D., Lee J., Martin G., Mundy J.,
RA Ohashi Y., Scheel D., Sheen J., Xing T., Zhang S., Seguin A., Ellis B.E.;
RT "Ancient signals: comparative genomics of plant MAPK and MAPKK gene
RT families.";
RL Trends Plant Sci. 11:192-198(2006).
RN [6]
RP FUNCTION, INTERACTION WITH PHS1, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19392697; DOI=10.1111/j.1365-313x.2009.03895.x;
RA Walia A., Lee J.S., Wasteneys G., Ellis B.;
RT "Arabidopsis mitogen-activated protein kinase MPK18 mediates cortical
RT microtubule functions in plant cells.";
RL Plant J. 59:565-575(2009).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, INTERACTION WITH
RP MAPKKK20, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=28848569; DOI=10.3389/fpls.2017.01352;
RA Benhamman R., Bai F., Drory S.B., Loubert-Hudon A., Ellis B., Matton D.P.;
RT "The Arabidopsis mitogen-activated protein kinase kinase kinase 20 (MKKK20)
RT acts upstream of MKK3 and MPK18 in two separate signaling pathways involved
RT in root microtubule functions.";
RL Front. Plant Sci. 8:1352-1352(2017).
RN [8]
RP REVIEW ON MITOGEN-ACTIVATED PROTEIN KINASE CASCADES.
RX PubMed=30349547; DOI=10.3389/fpls.2018.01387;
RA Jagodzik P., Tajdel-Zielinska M., Ciesla A., Marczak M., Ludwikow A.;
RT "Mitogen-activated protein kinase cascades in plant hormone signaling.";
RL Front. Plant Sci. 9:1387-1387(2018).
CC -!- FUNCTION: Mitogen-activated protein kinase (MAPK) that is specifically
CC regulated by PHS1 and MAPKKK20 and mediates signaling that regulates
CC cortical microtubule functions, maybe through regulation of microtubule
CC dynamic instability. {ECO:0000269|PubMed:19392697,
CC ECO:0000269|PubMed:28848569}.
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=2.7.11.24;
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=2.7.11.24;
CC -!- ACTIVITY REGULATION: Activated by threonine and tyrosine
CC phosphorylation (Probable). Inactivated by phosphatase PHS1.
CC {ECO:0000269|PubMed:19392697, ECO:0000305}.
CC -!- SUBUNIT: Interacts with PHS1 (PubMed:19392697). Binds to MAPKKK20
CC (PubMed:28848569). {ECO:0000269|PubMed:19392697,
CC ECO:0000269|PubMed:28848569}.
CC -!- INTERACTION:
CC Q9C5C0; Q17TI5: BRX; NbExp=3; IntAct=EBI-1238534, EBI-4426649;
CC Q9C5C0; Q9LQT8: GAI; NbExp=6; IntAct=EBI-1238534, EBI-963606;
CC Q9C5C0; Q75QN6: PHS1; NbExp=3; IntAct=EBI-1238534, EBI-2349366;
CC Q9C5C0; Q9SLH3: RGA; NbExp=4; IntAct=EBI-1238534, EBI-963624;
CC Q9C5C0; Q8GXW1: RGL2; NbExp=3; IntAct=EBI-1238534, EBI-963665;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28848569}. Cytoplasm
CC {ECO:0000269|PubMed:19392697, ECO:0000269|PubMed:28848569}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, seedlings, leaves, flower buds,
CC flowers and siliques. {ECO:0000269|PubMed:19392697,
CC ECO:0000269|PubMed:28848569}.
CC -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC whose phosphorylation activates the MAP kinases.
CC -!- PTM: Dually phosphorylated on Thr-187 and Tyr-189, which activates the
CC enzyme (By similarity). Phosphorylated by MAPKKK20 (PubMed:28848569).
CC {ECO:0000250|UniProtKB:A9T142, ECO:0000269|PubMed:28848569}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC condition, but mutant plants show reduced sensitivity to microtubule-
CC disrupting drugs (PubMed:19392697). Short roots with abnormal twisting
CC (e.g. leftward skewing) in media containing microtubule-disrupting
CC drugs (e.g. oryzalin) (PubMed:28848569). {ECO:0000269|PubMed:19392697,
CC ECO:0000269|PubMed:28848569}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. MAP kinase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF78438.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG51978.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC018748; AAF78438.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC024260; AAG51978.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32950.1; -; Genomic_DNA.
DR EMBL; AF360353; AAK28649.2; -; mRNA.
DR EMBL; BT000870; AAN41270.1; -; mRNA.
DR PIR; C96575; C96575.
DR RefSeq; NP_175756.2; NM_104229.4.
DR AlphaFoldDB; Q9C5C0; -.
DR SMR; Q9C5C0; -.
DR BioGRID; 27011; 16.
DR IntAct; Q9C5C0; 21.
DR STRING; 3702.AT1G53510.1; -.
DR iPTMnet; Q9C5C0; -.
DR PaxDb; Q9C5C0; -.
DR PRIDE; Q9C5C0; -.
DR ProteomicsDB; 250951; -.
DR EnsemblPlants; AT1G53510.1; AT1G53510.1; AT1G53510.
DR GeneID; 841786; -.
DR Gramene; AT1G53510.1; AT1G53510.1; AT1G53510.
DR KEGG; ath:AT1G53510; -.
DR Araport; AT1G53510; -.
DR TAIR; locus:2024887; AT1G53510.
DR eggNOG; KOG0660; Eukaryota.
DR HOGENOM; CLU_000288_181_13_1; -.
DR InParanoid; Q9C5C0; -.
DR OMA; NTHMAID; -.
DR OrthoDB; 741207at2759; -.
DR PRO; PR:Q9C5C0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C5C0; baseline and differential.
DR Genevisible; Q9C5C0; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004707; F:MAP kinase activity; ISS:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0043622; P:cortical microtubule organization; IMP:TAIR.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003527; MAP_kinase_CS.
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; PS01351; MAPK; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..615
FT /note="Mitogen-activated protein kinase 18"
FT /id="PRO_0000245818"
FT DOMAIN 25..316
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 414..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 187..189
FT /note="TXY"
FT COMPBIAS 414..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 151
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 31..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 187
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q39026"
FT MOD_RES 189
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q39026"
FT MOD_RES 192
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q39026"
SQ SEQUENCE 615 AA; 69352 MW; 1439ED0B3C82210E CRC64;
MQQNQVKKGT KEMEFFTEYG DANRYRILEV IGKGSYGVVC AAIDTHTGEK VAIKKINDVF
EHISDALRIL REVKLLRLLR HPDIVEIKSI MLPPSKREFK DIYVVFELME SDLHQVIKAN
DDLTREHHQF FLYQMLRALK FMHTANVYHR DLKPKNILAN ANCKLKVCDF GLARVAFNDT
PTTVFWTDYV ATRWYRAPEL CGSFFSKYTP AIDVWSIGCI FAEVLTGKPL FPGKSVVHQL
ELITDLLGTP KSETISGVRN DKARKYLTEM RKKNPVTFSQ KFSKADPLAL RLLQRLLAFD
PKDRPTPAEA LADPYFKGLS KIEREPSSQQ ISKMEFEFER RRLTKDDIRE LIYREILEYH
PQLLKDYMSG SEGSNFVYPS AIGHLRQQFT YLEENSSRNG PVIPLERKHA SLPRSTVHST
VVHSTSQPNL GATDSRRVSF EPSKNGASSA GHPSTSAYPT KSIGPPPRVP PSGRPGRVVE
SSVSYENGRN LKEAYFRSAV SSPHCYFRPN TMTNPENRNI EASSFPPKPQ NPVHQFSPTE
PPAATTNQAD VETMNHPNPY FQPQLPKTDQ LNNNTHMAID AKLLQAQSQF GPAGAAAVAV
AAHRNIGTIS YSAAS
