NTF3_TOBAC
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 03-AUG-2022, entry version 104.
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}.
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DR EMBL; X69971; CAA49592.1; -; mRNA.
DR PIR; S39559; S39559.
DR AlphaFoldDB; Q40517; -.
DR SMR; Q40517; -.
DR STRING; 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: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 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
