NTF4_TOBAC
ID NTF4_TOBAC Reviewed; 393 AA.
AC Q40532;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Mitogen-activated protein kinase homolog NTF4;
DE EC=2.7.11.24;
DE AltName: Full=P45;
GN Name=NTF4;
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=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 -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC whose phosphorylation activates the MAP kinases.
CC -!- PTM: Dually phosphorylated on Thr-218 and Tyr-220, 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}.
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DR EMBL; X83880; CAA58761.1; -; mRNA.
DR PIR; S68190; S51321.
DR AlphaFoldDB; Q40532; -.
DR SMR; Q40532; -.
DR STRING; 4097.Q40532; -.
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: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 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; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..393
FT /note="Mitogen-activated protein kinase homolog NTF4"
FT /id="PRO_0000186322"
FT DOMAIN 60..345
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 218..220
FT /note="TXY"
FT ACT_SITE 186
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 66..74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 218
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 220
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 393 AA; 45120 MW; 76EC1F3B1F174AB9 CRC64;
MDGPAHQTDT VMSDAAGQQP APPSQPVAGI DNIPATLSHG GRFIQYNIFG NIFEVTAKYK
PPIMPIGKGA YGIVCSALNS ETNEHVAIKK IANAFDNKID AKRTLREIKL LRHMDHENIV
AIRDIIPPPQ REAFNDVYIA YELMDTDLHQ IIRSNQGLSE EHCQYFLYQI LRGLKYIHSA
NVLHRDLKPS NLLLNANCDL KICDFGLARV TSETDFMTEY VVTRWYRAPE LLLNSSDYTA
AIDVWSVGCI FMELMDRKPL FPGRDHVHQL RLLMELIGTP SEAEMEFLNE NAKRYIRQLP
LYRRQSFVEK FPHVNPAAID LVEKMLTFDP RRRITVEDAL AHPYLTSLHD ISDEPVCMTP
FNFDFEQHAL TEEQMKELIY REGLAFNPEY QHM
