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   24-JAN-2024, entry version 137.
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}, T3F20.17
GN   {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.Q9C5C0; -.
DR   iPTMnet; Q9C5C0; -.
DR   PaxDb; 3702-AT1G53510-1; -.
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; AT1G53510; MPK18.
DR   eggNOG; KOG0660; Eukaryota.
DR   HOGENOM; CLU_000288_181_13_1; -.
DR   InParanoid; Q9C5C0; -.
DR   OMA; NTHMAID; -.
DR   OrthoDB; 1032011at2759; -.
DR   PRO; PR:Q9C5C0; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9C5C0; baseline and differential.
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:0043622; P:cortical microtubule organization; IMP:TAIR.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd07859; STKc_TDY_MAPK; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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   PANTHER; PTHR24055; MITOGEN-ACTIVATED PROTEIN KINASE; 1.
DR   PANTHER; PTHR24055:SF420; MITOGEN-ACTIVATED PROTEIN KINASE 18; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS01351; MAPK; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   Genevisible; Q9C5C0; AT.
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
//