NPK1_TOBAC
ID NPK1_TOBAC Reviewed; 690 AA.
AC Q40541;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase NPK1;
DE EC=2.7.11.25;
DE AltName: Full=Nicotiana protein kinase 1;
GN Name=NPK1;
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], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Bright Yellow 2;
RX PubMed=8336712; DOI=10.1128/mcb.13.8.4745-4752.1993;
RA Banno H., Hirano K., Nakamura T., Irie K., Nomoto S., Matsumoto K.,
RA Machida Y.;
RT "NPK1, a tobacco gene that encodes a protein with a domain homologous to
RT yeast BCK1, STE11, and Byr2 protein kinases.";
RL Mol. Cell. Biol. 13:4745-4752(1993).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=9729893; DOI=10.1093/oxfordjournals.pcp.a029423;
RA Nakashima M., Hirano K., Nakashima S., Banno H., Nishihama R., Machida Y.;
RT "The expression pattern of the gene for NPK1 protein kinase related to
RT mitogen-activated protein kinase kinase kinase (MAPKKK) in a tobacco plant:
RT correlation with cell proliferation.";
RL Plant Cell Physiol. 39:690-700(1998).
RN [3]
RP FUNCTION.
RX PubMed=9790195; DOI=10.1038/27240;
RA Kovtun Y., Chiu W.L., Zeng W., Sheen J.;
RT "Suppression of auxin signal transduction by a MAPK cascade in higher
RT plants.";
RL Nature 395:716-720(1998).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=11159915; DOI=10.1101/gad.863701;
RA Nishihama R., Ishikawa M., Araki S., Soyano T., Asada T., Machida Y.;
RT "The NPK1 mitogen-activated protein kinase kinase kinase is a regulator of
RT cell-plate formation in plant cytokinesis.";
RL Genes Dev. 15:352-363(2001).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NACK1 AND NACK2.
RX PubMed=11955449; DOI=10.1016/s0092-8674(02)00691-8;
RA Nishihama R., Soyano T., Ishikawa M., Araki S., Tanaka H., Asada T.,
RA Irie K., Ito M., Terada M., Banno H., Yamazaki Y., Machida Y.;
RT "Expansion of the cell plate in plant cytokinesis requires a kinesin-like
RT protein/MAPKKK complex.";
RL Cell 109:87-99(2002).
RN [6]
RP FUNCTION.
RX PubMed=12194859; DOI=10.1016/s1534-5807(02)00205-8;
RA Jin H., Axtell M.J., Dahlbeck D., Ekwenna O., Zhang S., Staskawicz B.,
RA Baker B.;
RT "NPK1, an MEKK1-like mitogen-activated protein kinase kinase kinase,
RT regulates innate immunity and development in plants.";
RL Dev. Cell 3:291-297(2002).
RN [7]
RP SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, INTERACTION WITH NACK1,
RP AND MUTAGENESIS OF 645-ARG-ARG-646; LYS-648 AND 657-ARG--ARG-659.
RX PubMed=12472693; DOI=10.1046/j.1365-313x.2002.01469.x;
RA Ishikawa M., Soyano T., Nishihama R., Machida Y.;
RT "The NPK1 mitogen-activated protein kinase kinase kinase contains a
RT functional nuclear localization signal at the binding site for the NACK1
RT kinesin-like protein.";
RL Plant J. 32:789-798(2002).
RN [8]
RP FUNCTION, INTERACTION WITH NACK1, AND PHOSPHORYLATION AT SER-575; SER-669
RP AND SER-687.
RX PubMed=22006334; DOI=10.1073/pnas.1110174108;
RA Sasabe M., Boudolf V., De Veylder L., Inze D., Genschik P., Machida Y.;
RT "Phosphorylation of a mitotic kinesin-like protein and a MAPKKK by cyclin-
RT dependent kinases (CDKs) is involved in the transition to cytokinesis in
RT plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:17844-17849(2011).
CC -!- FUNCTION: Functions in the NACK-PQR (NPK1-NQK1/MEK1-NRK1) MAP kinase
CC signaling pathway, which is essential for somatic cell cytokinesis,
CC especially for the cell-plate formation and its expansion, and depends
CC on NACK1 and NACK2 kinesin-related proteins. Functions in the
CC regulation of resistance gene-mediated resistance responses such as the
CC N-mediated resistance to tobamovirus (TMV) and the Rx-mediated
CC hypersensitive response (HR) to potato virus X (PVX).
CC {ECO:0000269|PubMed:11159915, ECO:0000269|PubMed:11955449,
CC ECO:0000269|PubMed:12194859, ECO:0000269|PubMed:22006334,
CC ECO:0000269|PubMed:9790195}.
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=2.7.11.25;
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=2.7.11.25;
CC -!- SUBUNIT: Interacts (via C-terminus) with NACK1 (via C-terminus).
CC {ECO:0000269|PubMed:11955449, ECO:0000269|PubMed:12472693,
CC ECO:0000269|PubMed:22006334}.
CC -!- INTERACTION:
CC Q40541; Q8S950: NACK1; NbExp=6; IntAct=EBI-639963, EBI-639977;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton,
CC phragmoplast. Note=In interphase and prophase, detected in the nucleus.
CC From prometaphase to metaphase, found in the cytoplasm in patches. At
CC anaphase, distributed around the spindle midzone and on the
CC phragmoplast equator at telophase and then redistributed to the newly
CC forming daughter nuclei.
CC -!- TISSUE SPECIFICITY: Expressed in root apex, lateral root primordia,
CC cotyledons, shoot apical meristem, stems, young leaves, vasculature
CC floral meristem, floral organ primordia, stigma, style and ovules in
CC the immature gynoecium. {ECO:0000269|PubMed:8336712,
CC ECO:0000269|PubMed:9729893}.
CC -!- INDUCTION: During the M phase of the cell cycle (at protein level).
CC {ECO:0000269|PubMed:11159915}.
CC -!- PTM: Phosphorylated at Ser-575, Ser-669 and Ser-687 by CDKAs and CDKBs.
CC The phosphorylation occurs before metaphase and inhibits the
CC interaction with NACK1 preventing the transition to cytokinesis.
CC {ECO:0000269|PubMed:22006334}.
CC -!- MISCELLANEOUS: Plants overexpressing the NPK1 kinase domain produced
CC seeds defective in embryo and endosperm development (PubMed:9790195).
CC Expression of kinase-negative NPK1 causes inhibition of phragmoplast
CC expansion and multinucleate cells (PubMed:11159915). Plants silencing
CC NPK1 exhibit reduced cell size, defective cytokinesis and an overall
CC dwarf phenotype (PubMed:12194859). {ECO:0000305|PubMed:11159915,
CC ECO:0000305|PubMed:12194859, ECO:0000305|PubMed:9790195}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {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; D26601; BAA05648.1; -; mRNA.
DR PIR; A48084; A48084.
DR RefSeq; NP_001312547.1; NM_001325618.1.
DR AlphaFoldDB; Q40541; -.
DR SMR; Q40541; -.
DR IntAct; Q40541; 1.
DR STRING; 4097.Q40541; -.
DR iPTMnet; Q40541; -.
DR GeneID; 107796336; -.
DR KEGG; nta:107796336; -.
DR OMA; KSGVPCD; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0009524; C:phragmoplast; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0000919; P:cell plate assembly; IGI:UniProtKB.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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; 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; Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Kinase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Plant defense;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..690
FT /note="Mitogen-activated protein kinase kinase kinase NPK1"
FT /id="PRO_0000422320"
FT DOMAIN 80..342
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 551..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 645..659
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 551..572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 208
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 86..94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 575
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22006334"
FT MOD_RES 669
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22006334"
FT MOD_RES 687
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22006334"
FT MUTAGEN 645..646
FT /note="RR->SS: Loss of nuclear localization; when
FT associated with T-648 and 657-S--S-659."
FT /evidence="ECO:0000269|PubMed:12472693"
FT MUTAGEN 648
FT /note="K->T: Loss of nuclear localization; when associated
FT with 645-S-S-646 and 657-S--S-659."
FT /evidence="ECO:0000269|PubMed:12472693"
FT MUTAGEN 657..659
FT /note="RKR->STS: Loss of nuclear localization; when
FT associated with 645-S-S-646 and T-648."
FT /evidence="ECO:0000269|PubMed:12472693"
SQ SEQUENCE 690 AA; 76242 MW; 2F9C2A3AA31C6094 CRC64;
MQDFIGSVRR SLVFKQSGDF DTGAAGVGSG FGGFVEKLGS SIRKSSIGIF SKAHVPALPS
ISKAELPAKA RKDDTPPIRW RKGEMIGCGA FGRVYMGMNV DSGELLAIKE VSIAMNGASR
ERAQAHVREL EEEVNLLKNL SHPNIVRYLG TAREAGSLNI LLEFVPGGSI SSLLGKFGSF
PESVIRMYTK QLLLGLEYLH KNGIMHRDIK GANILVDNKG CIKLADFGAS KKVVELATMT
GAKSMKGTPY WMAPEVILQT GHSFSADIWS VGCTIIEMAT GKPPWSQQYQ EVAALFHIGT
TKSHPPIPEH LSAESKDFLL KCLQKEPHLR HSASNLLQHP FVTAEHQEAR PFLRSSFMGN
PENMAAQRMD VRTSIIPDMR ASCNGLKDVC GVSAVRCSTV YPENSLGKES LWKLGNSDDD
MCQMDNDDFM FGASVKCSSD LHSPANYKSF NPMCEPDNDW PCKFDESPEL TKSQANLHYD
QATIKPTNNP IMSYKEDLAF TFPSGQSAAE DDDELTESKI RAFLDEKAMD LKKLQTPLYE
GFYNSLNVSS TPSPVGTGNK ENVPSNINLP PKSRSPKRML SRRLSTAIEG ACAPSPVTHS
KRISNIGGLN GEAIQEAQLP RHNEWKDLLG SQREAVNSSF SERQRRWKEE LDEELQRKRE
IMRQAVNLSP PKDPILNRCR SKSRFASPGR
