ID D1MFM1_MALDO Unreviewed; 394 AA. AC D1MFM1; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 08-MAY-2019, entry version 53. DE RecName: Full=Mitogen-activated protein kinase {ECO:0000256|RuleBase:RU361165, ECO:0000256|SAAS:SAAS00574127}; DE EC=2.7.11.24 {ECO:0000256|RuleBase:RU361165, ECO:0000256|SAAS:SAAS00574127}; GN Name=MPK1 {ECO:0000313|EMBL:ACY82513.1}; OS Malus domestica (Apple) (Pyrus malus). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Rosales; Rosaceae; Amygdaloideae; OC Maleae; Malus. OX NCBI_TaxID=3750 {ECO:0000313|EMBL:ACY82513.1}; RN [1] {ECO:0000313|EMBL:ACY82513.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Fruit {ECO:0000313|EMBL:ACY82513.1}; RA Wang X.-J., Zhu S.-Y., Lu Y.-F., Zhang D.-P.; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ACY82513.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Fruit {ECO:0000313|EMBL:ACY82513.1}; RX PubMed=20360020; DOI=10.1093/pcp/pcq037; RA Wang X.J., Zhu S.Y., Lu Y.F., Zhao R., Xin Q., Wang X.F., Zhang D.P.; RT "Two coupled components of the mitogen-activated protein kinase RT cascade MdMPK1 and MdMKK1 from apple function in ABA signal RT transduction."; RL Plant Cell Physiol. 51:754-766(2010). 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, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; CC EC=2.7.11.24; Evidence={ECO:0000256|SAAS:SAAS01125144}; 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; Evidence={ECO:0000256|RuleBase:RU361165, CC ECO:0000256|SAAS:SAAS01125154}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|RuleBase:RU361165}; CC -!- ACTIVITY REGULATION: Activated by threonine and tyrosine CC phosphorylation. {ECO:0000256|RuleBase:RU361165}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr CC protein kinase family. MAP kinase subfamily. CC {ECO:0000256|RuleBase:RU361165}. 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; GU139791; ACY82513.1; -; mRNA. DR RefSeq; NP_001280856.1; NM_001293927.1. DR GeneID; 103456346; -. DR KEGG; mdm:103456346; -. DR KO; K14512; -. DR OrthoDB; 741207at2759; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004707; F:MAP kinase activity; IEA:UniProtKB-EC. 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 InterPro; IPR008271; Ser/Thr_kinase_AS. 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. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 2: Evidence at transcript level; KW ATP-binding {ECO:0000256|RuleBase:RU000304, KW ECO:0000256|SAAS:SAAS00574094}; KW Kinase {ECO:0000256|RuleBase:RU361165, ECO:0000256|SAAS:SAAS00574086, KW ECO:0000313|EMBL:ACY82513.1}; KW Magnesium {ECO:0000256|RuleBase:RU361165}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU000304, KW ECO:0000256|SAAS:SAAS00574135}; KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000304, KW ECO:0000256|SAAS:SAAS00574114}; KW Transferase {ECO:0000256|RuleBase:RU361165, KW ECO:0000256|SAAS:SAAS00574095}. FT DOMAIN 61 346 Protein kinase. {ECO:0000259|PROSITE: FT PS50011}. SQ SEQUENCE 394 AA; 44892 MW; 3B2F316DA53414CC CRC64; MDGSAPQTDT VMSDAAAGQQ PAPPPLPMAG VESIPATLSH GGRFIQYNIF GNVFEVTAKY KPPIMPIGKG AYGIVCSALN SETNEHVAIK KIANAFDNKI DAKRTLREIK LLRHMDHENV VAIRDIIPPP QRNSFNDVYI AYGLMDTDLH QIIRSNQALS EEHCQYFLYQ ILRGLKYIHS ANVLHRDLKP SNLLLNANCD LKICDFGLAR VTSETDFMTE YVVTRWYRAP ELLLNSSDYT AAIDVWSVGC IFMELMDRKP LFPGRDHVHQ LRLLLELIGT PSEAELQFLN ENAKRYIRQL PLYRRQSFTE KFPHVHPSAI DLVEKMLTFD PTQRITVEDA LAHPYLTSLH DISDEPVCTT PFSFDFEQHA LSEEQMKELI YREALAFNPE YQLQ //