MPK17_ARATH
ID MPK17_ARATH Reviewed; 486 AA.
AC Q84M93; Q9ZVF9;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Mitogen-activated protein kinase 17;
DE Short=AtMPK17;
DE Short=MAP kinase 17;
DE EC=2.7.11.24;
GN Name=MPK17; OrderedLocusNames=At2g01450; ORFNames=F2I9.7;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 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).
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 -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC whose phosphorylation activates the MAP kinases.
CC -!- PTM: Dually phosphorylated on Thr-178 and Tyr-180, which activates the
CC enzyme. {ECO:0000250}.
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=AAC67338.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC005560; AAC67338.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC05452.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05453.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05454.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05455.1; -; Genomic_DNA.
DR EMBL; BT006469; AAP21277.1; -; mRNA.
DR PIR; H84424; H84424.
DR RefSeq; NP_001030939.1; NM_001035862.2.
DR RefSeq; NP_001030940.1; NM_001035863.1.
DR RefSeq; NP_001030941.1; NM_001035864.1.
DR RefSeq; NP_178254.2; NM_126206.4.
DR AlphaFoldDB; Q84M93; -.
DR SMR; Q84M93; -.
DR BioGRID; 76; 1.
DR IntAct; Q84M93; 2.
DR STRING; 3702.AT2G01450.3; -.
DR iPTMnet; Q84M93; -.
DR PaxDb; Q84M93; -.
DR PRIDE; Q84M93; -.
DR ProteomicsDB; 238276; -.
DR EnsemblPlants; AT2G01450.1; AT2G01450.1; AT2G01450.
DR EnsemblPlants; AT2G01450.2; AT2G01450.2; AT2G01450.
DR EnsemblPlants; AT2G01450.3; AT2G01450.3; AT2G01450.
DR EnsemblPlants; AT2G01450.4; AT2G01450.4; AT2G01450.
DR GeneID; 814673; -.
DR Gramene; AT2G01450.1; AT2G01450.1; AT2G01450.
DR Gramene; AT2G01450.2; AT2G01450.2; AT2G01450.
DR Gramene; AT2G01450.3; AT2G01450.3; AT2G01450.
DR Gramene; AT2G01450.4; AT2G01450.4; AT2G01450.
DR KEGG; ath:AT2G01450; -.
DR Araport; AT2G01450; -.
DR TAIR; locus:2049552; AT2G01450.
DR eggNOG; KOG0660; Eukaryota.
DR HOGENOM; CLU_000288_181_5_1; -.
DR InParanoid; Q84M93; -.
DR OMA; VWDDCED; -.
DR OrthoDB; 741207at2759; -.
DR PhylomeDB; Q84M93; -.
DR PRO; PR:Q84M93; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q84M93; baseline and differential.
DR Genevisible; Q84M93; 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; HDA:TAIR.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:1900064; P:positive regulation of peroxisome organization; IGI:TAIR.
DR GO; GO:0046777; P:protein autophosphorylation; HDA:TAIR.
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 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..486
FT /note="Mitogen-activated protein kinase 17"
FT /id="PRO_0000245817"
FT DOMAIN 16..307
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 386..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 178..180
FT /note="TXY"
FT COMPBIAS 386..418
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 142
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 22..30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 178
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q39026"
FT MOD_RES 180
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q39026"
FT MOD_RES 183
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q39026"
SQ SEQUENCE 486 AA; 55493 MW; 2741BC52DC3FFCE6 CRC64;
MLEKEFFTEY GEASQYQIQE VVGKGSYGVV ASAECPHTGG KVAIKKMTNV FEHVSDAIRI
LREIKLLRLL RHPDIVEIKH IMLPPCRKEF KDIYVVFELM ESDLHHVLKV NDDLTPQHHQ
FFLYQLLRGL KFMHSAHVFH RDLKPKNILA NADCKIKICD LGLARVSFTD SPSAVFWTDY
VATRWYRAPE LCGSFYSNYT PAIDMWSVGC IFAEMLTGKP LFPGKNVVHQ LELVTDLLGT
PSPITLSRIR NEKARKYLGN MRRKDPVPFT HKFPNIDPVA LKLLQRLIAF DPKDRPSAEE
ALADPYFQGL ANVDYEPSRQ PISKLEFEFE RRKLTRDDVR ELMYREILEY HPQMLQEYLQ
GEENINSHFL YPSGVDQFKQ EFARLEEHND DEEEHNSPPH QRKYTSLPRE RVCSSEDEGS
DSVHAQSSSA SVVFTPPQTP NTATGLSSQK ASQVDKAATP VKRSACLMRS DSICASRCVG
VSSAVS
