ID MPK_PETHY Reviewed; 384 AA.
AC Q40884;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE RecName: Full=Mitogen-activated protein kinase homolog 1;
DE EC=2.7.11.24;
DE AltName: Full=PMEK1;
GN Name=MPK1; Synonyms=MEK1;
OS Petunia hybrida (Petunia).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX NCBI_TaxID=4102;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovule;
RX PubMed=7888623; DOI=10.1007/bf00020188;
RA Decroocq-Ferrant V., Decroocq S., van Went J., Schmidt E., Kreis M.;
RT "A homologue of the MAP/ERK family of protein kinase genes is expressed in
RT vegetative and in female reproductive organs of Petunia hybrida.";
RL Plant Mol. Biol. 27:339-350(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: Expressed in vegetative organs such as leaf, root,
CC or stem. In the reproductive organs, it is found in the ovary, but not
CC in the stamen.
CC -!- DEVELOPMENTAL STAGE: Present during flower development prior to
CC fertilization. At early stages of ovule development, the expression is
CC uniform throughout the ovule. At a later stage, is localized adjacent
CC to the embryo sac. When the flower opens and pollen is released, it is
CC found in the whole ovule and in the outer layer of the placenta.
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. {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; X83440; CAA58466.1; -; mRNA.
DR PIR; S52989; S52989.
DR AlphaFoldDB; Q40884; -.
DR SMR; Q40884; -.
DR BRENDA; 2.7.11.24; 4700.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004707; F:MAP kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
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 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..384
FT /note="Mitogen-activated protein kinase homolog 1"
FT /id="PRO_0000186320"
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:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 191
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 193
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 384 AA; 44445 MW; 7536CC960390EC58 CRC64;
MATPVEPPNG IRTPGKHYYS MWQSLFEIDT KYVPIKPIGR GAYGIVCSSV NRETNEKVAI
KKINNAFENR IDALRTLREL KLLRHLRHEN VIALKDVMMP IQRRSFKDVY LVYELMDTDL
HQIIKSSQTL SNDHCQYFLF QLLRGLKYLH SANILHRDLK PGNLLINANC DLKICDFGLA
RTSSGKDQFM TEYVVTRWYR APELLLCCDN YGTSIDVWSV GCIFADVLGR KPVFPGTECL
NQLKLIINIL GSQREEDIEF IDNPKARKYI KSLPYSPGTP FSRLYPNAHP LAIDLLQRML
VFDPSKRISV MEALQHPYMS PLYDPNTDPP AQVPINLDID EDLVEETIRE MMWEEILHYH
PEAAVALLWK LFYELLLVPS RHRP
//
