ID NTF3_TOBAC Reviewed; 372 AA. AC Q40517; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 109. DE RecName: Full=Mitogen-activated protein kinase homolog NTF3; DE EC=2.7.11.24; DE AltName: Full=P43; GN Name=NTF3; OS Nicotiana tabacum (Common tobacco). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae; OC Nicotiana. OX NCBI_TaxID=4097; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Petit Havana SR1; RX PubMed=8219089; DOI=10.1007/bf00019302; RA Wilson C., Eller N., Gartner A., Vicente O., Heberle-Bors E.; RT "Isolation and characterization of a tobacco cDNA clone encoding a putative RT MAP kinase."; RL Plant Mol. Biol. 23:543-551(1993). RN [2] RP MUTAGENESIS. RC STRAIN=cv. Petit Havana SR1; RX PubMed=7588752; DOI=10.1111/j.1432-1033.1995.249_1.x; RA Wilson C., Anglmayer R., Vicente O., Heberle-Bors E.; RT "Molecular cloning, functional expression in Escherichia coli, and RT characterization of multiple mitogen-activated-protein kinases from RT tobacco."; RL Eur. J. Biochem. 233:249-257(1995). 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 -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- ACTIVITY REGULATION: Activated by tyrosine and threonine CC phosphorylation. {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Ubiquitous. CC -!- DEVELOPMENTAL STAGE: Detected during gametophytic pollen development CC and constitutively expressed in embryogenic pollen. CC -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues CC whose phosphorylation activates the MAP kinases. CC -!- PTM: Dually phosphorylated on Thr-191 and Tyr-193, which activates the CC enzyme (By similarity). Very low autophosphorylation, although CC dramatically increased when Mn(2+) is added to the reaction instead of CC Mg(2+). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr CC protein kinase family. MAP kinase subfamily. {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; X69971; CAA49592.1; -; mRNA. DR PIR; S39559; S39559. DR AlphaFoldDB; Q40517; -. DR SMR; Q40517; -. DR STRING; 4097.Q40517; -. DR PaxDb; 4097-Q40517; -. DR BRENDA; 2.7.11.24; 3645. DR Proteomes; UP000084051; Unplaced. 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; IBA:GO_Central. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd07858; STKc_TEY_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 InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR24055; MITOGEN-ACTIVATED PROTEIN KINASE; 1. DR PANTHER; PTHR24055:SF588; MITOGEN-ACTIVATED PROTEIN KINASE 7; 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 PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 1: Evidence at protein level; KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Serine/threonine-protein kinase; Transferase. FT CHAIN 1..372 FT /note="Mitogen-activated protein kinase homolog NTF3" FT /id="PRO_0000186321" FT DOMAIN 32..319 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOTIF 191..193 FT /note="TXY" FT ACT_SITE 158 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 38..46 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 61 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000305" FT MOD_RES 191 FT /note="Phosphothreonine" FT /evidence="ECO:0000250" FT MOD_RES 193 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250" FT MUTAGEN 61 FT /note="K->R: Inactivation." FT /evidence="ECO:0000269|PubMed:7588752" SQ SEQUENCE 372 AA; 42776 MW; 3277355C89FF3EBA CRC64; MATPVEPPNG IRTPGKHYYS MWQSLFEIDT KYVPIKPIGR GAYGIVCSSV NRETNEKVAI KKINNAFENR IDALRTLREL KLLRHLRHEN VIALKDVMMP IHRRSFKDVY LVYELMDTDL HQIIKSSQTL SNDHCQYFLF QLLRGLKYLH SANILHRDLK PGNLLINANC DLKICDFGLA RTSSGKDQFM TEYVVTRWYR APELLLCCDN YGTSIDVWSV GCIFAELLGR KPVFPGTECL NQLKLIINIL GSQREEDIEF IDNPKARKYI KSLPYSPGTP FSRLYPHAHP LAIDLLQRML VFDPSKRISV IEALQHPYMS PLYDPNTDPP AQVPINLDID EDLGEETIRE MMWSEILEYH PEAATAAMEV VL //