MPK15_ARATH
ID MPK15_ARATH Reviewed; 576 AA.
AC Q9C9U4; Q94EY5;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 3.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Mitogen-activated protein kinase 15;
DE Short=AtMPK15;
DE Short=MAP kinase 15;
DE EC=2.7.11.24;
GN Name=MPK15; OrderedLocusNames=At1g73670; ORFNames=F25P22.9;
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] (ISOFORM 2).
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 INTERACTION WITH MKK7.
RX PubMed=19513235; DOI=10.4161/psb.3.12.6848;
RA Lee J.S., Huh K.W., Bhargava A., Ellis B.E.;
RT "Comprehensive analysis of protein-protein interactions between Arabidopsis
RT MAPKs and MAPK kinases helps define potential MAPK signalling modules.";
RL Plant Signal. Behav. 3:1037-1041(2008).
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. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MKK7. {ECO:0000269|PubMed:19513235}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9C9U4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C9U4-2; Sequence=VSP_020140, VSP_020141;
CC -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC whose phosphorylation activates the MAP kinases.
CC -!- PTM: Dually phosphorylated on Thr-252 and Tyr-254, which activates the
CC enzyme. {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 1]: Inferred from the gene model conservation
CC between members of the family.
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=AAG52072.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC012679; AAG52072.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35495.1; -; Genomic_DNA.
DR EMBL; AF387019; AAK62464.1; -; mRNA.
DR EMBL; BT001159; AAN65046.1; -; mRNA.
DR PIR; G96763; G96763.
DR RefSeq; NP_565070.2; NM_106026.3. [Q9C9U4-1]
DR AlphaFoldDB; Q9C9U4; -.
DR SMR; Q9C9U4; -.
DR IntAct; Q9C9U4; 1.
DR STRING; 3702.AT1G73670.1; -.
DR iPTMnet; Q9C9U4; -.
DR PaxDb; Q9C9U4; -.
DR PRIDE; Q9C9U4; -.
DR ProteomicsDB; 239071; -. [Q9C9U4-1]
DR EnsemblPlants; AT1G73670.1; AT1G73670.1; AT1G73670. [Q9C9U4-1]
DR GeneID; 843702; -.
DR Gramene; AT1G73670.1; AT1G73670.1; AT1G73670. [Q9C9U4-1]
DR KEGG; ath:AT1G73670; -.
DR Araport; AT1G73670; -.
DR TAIR; locus:2027814; AT1G73670.
DR eggNOG; KOG0660; Eukaryota.
DR HOGENOM; CLU_000288_181_5_1; -.
DR InParanoid; Q9C9U4; -.
DR OMA; GNQLSFM; -.
DR OrthoDB; 741207at2759; -.
DR PhylomeDB; Q9C9U4; -.
DR PRO; PR:Q9C9U4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C9U4; baseline and differential.
DR Genevisible; Q9C9U4; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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: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 Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..576
FT /note="Mitogen-activated protein kinase 15"
FT /id="PRO_0000245815"
FT DOMAIN 90..381
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 20..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 252..254
FT /note="TXY"
FT COMPBIAS 20..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..499
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 216
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 96..104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 252
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q39026"
FT MOD_RES 254
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q39026"
FT MOD_RES 257
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q39026"
FT VAR_SEQ 421..431
FT /note="ILEYHPQMLEE -> VMSLLYISSLV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_020140"
FT VAR_SEQ 432..576
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_020141"
SQ SEQUENCE 576 AA; 65251 MW; F4F429EAF3CF4EE7 CRC64;
MGGGGNLVDG VRRWLFFQRR PSSSSSSNNH DQIQNPPTVS NPNDDEDLKK LTDPSKLRQI
KVQQRNHLPM EKKGIPNAEF FTEYGEANRY QIQEVVGKGS YGVVGSAIDT HTGERVAIKK
INDVFDHISD ATRILREIKL LRLLLHPDVV EIKHIMLPPS RREFRDVYVV FELMESDLHQ
VIKANDDLTP EHHQFFLYQL LRGLKYVHAA NVFHRDLKPK NILANADCKL KICDFGLARV
SFNDAPTAIF WTDYVATRWY RAPELCGSFF SKYTPAIDIW SVGCIFAEML LGKPLFPGKN
VVHQLDIMTD FLGTPPPEAI SKIRNDKARR YLGNMRKKQP VPFSKKFPKA DPSALRLLER
LIAFDPKDRP SAEEALADPY FNGLSSKVRE PSTQPISKLE FEFERKKLTK DDIRELIYRE
ILEYHPQMLE EYLRGGNQLS FMYPSGVDRF RRQFAHLEEN QGPGGRSNAL QRQHASLPRE
RVPASKNETV EERSNDIERR TTAAVASTLD SPKASQQAEG TENGGGGGYS ARNLMKSSSI
SGSKCIGVQS KTNIEDSIVE EQDETVAVKV ASLHNS
