M3K2_ARATH
ID M3K2_ARATH Reviewed; 651 AA.
AC Q9FZ36; F4HYM4; O22041; Q9C7M0;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase 2;
DE EC=2.7.11.25;
DE AltName: Full=Arabidopsis NPK1-related protein kinase 2;
GN Name=ANP2; OrderedLocusNames=At1g54960; ORFNames=F14C21.49, T24C10.7;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-651, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=9263451; DOI=10.1046/j.1365-313x.1997.12010039.x;
RA Nishihama R., Banno H., Kawahara E., Irie K., Machida Y.;
RT "Possible involvement of differential splicing in regulation of the
RT activity of Arabidopsis ANP1 that is related to mitogen-activated protein
RT kinase kinase kinases (MAPKKKs).";
RL Plant J. 12:39-48(1997).
RN [4]
RP FUNCTION.
RX PubMed=20215588; DOI=10.1105/tpc.109.071746;
RA Beck M., Komis G., Mueller J., Menzel D., Samaj J.;
RT "Arabidopsis homologs of nucleus- and phragmoplast-localized kinase 2 and 3
RT and mitogen-activated protein kinase 4 are essential for microtubule
RT organization.";
RL Plant Cell 22:755-771(2010).
CC -!- FUNCTION: Involved in cortical microtubules organization and
CC stabilization by regulating the phosphorylation state of microtubule-
CC associated proteins such as MAP65-1. {ECO:0000269|PubMed:20215588}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and flowers.
CC {ECO:0000269|PubMed:9263451}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51109.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC064840; AAG00876.1; -; Genomic_DNA.
DR EMBL; AC069144; AAG51109.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33167.2; -; Genomic_DNA.
DR EMBL; CP002684; ANM58828.1; -; Genomic_DNA.
DR EMBL; AB000798; BAA21856.1; -; mRNA.
DR PIR; A96591; A96591.
DR RefSeq; NP_001319236.1; NM_001333684.1.
DR RefSeq; NP_175894.5; NM_104370.5.
DR AlphaFoldDB; Q9FZ36; -.
DR SMR; Q9FZ36; -.
DR BioGRID; 27162; 1.
DR STRING; 3702.AT1G54960.1; -.
DR iPTMnet; Q9FZ36; -.
DR PaxDb; Q9FZ36; -.
DR PRIDE; Q9FZ36; -.
DR ProteomicsDB; 250818; -.
DR EnsemblPlants; AT1G54960.1; AT1G54960.1; AT1G54960.
DR EnsemblPlants; AT1G54960.2; AT1G54960.2; AT1G54960.
DR GeneID; 841937; -.
DR Gramene; AT1G54960.1; AT1G54960.1; AT1G54960.
DR Gramene; AT1G54960.2; AT1G54960.2; AT1G54960.
DR KEGG; ath:AT1G54960; -.
DR Araport; AT1G54960; -.
DR eggNOG; KOG0198; Eukaryota.
DR HOGENOM; CLU_020952_1_0_1; -.
DR InParanoid; Q9FZ36; -.
DR OMA; CMESNIN; -.
DR OrthoDB; 361120at2759; -.
DR PhylomeDB; Q9FZ36; -.
DR PRO; PR:Q9FZ36; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FZ36; baseline and differential.
DR Genevisible; Q9FZ36; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
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:0043622; P:cortical microtubule organization; IMP:UniProtKB.
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 2: Evidence at transcript level;
KW ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Isopeptide bond; Kinase;
KW Microtubule; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Ubl conjugation.
FT CHAIN 1..651
FT /note="Mitogen-activated protein kinase kinase kinase 2"
FT /id="PRO_0000086271"
FT DOMAIN 68..330
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 460..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 105..130
FT /evidence="ECO:0000255"
FT COILED 605..628
FT /evidence="ECO:0000255"
FT COMPBIAS 550..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..651
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 196
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 74..82
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CROSSLNK 108
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:O22042"
FT CROSSLNK 110
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:O22042"
FT CONFLICT 99
FT /note="V -> A (in Ref. 3; BAA21856)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 651 AA; 71849 MW; 0204655E1F9E918E CRC64;
MQDLFGSVRR SLVFRSTTDD ENQENHPPPF PSLLADKITS CIRKSMVFAK SQSPPNNSTV
QIKPPIRWRK GQLIGRGAFG TVYMGMNLDS GELLAVKQVL ITSNCASKEK TQAHIQELEE
EVKLLKNLSH PNIVRYLGTV REDETLNILL EFVPGGSISS LLEKFGAFPE SVVRTYTNQL
LLGLEYLHNH AIMHRDIKGA NILVDNQGCI KLADFGASKQ VAELATISGA KSMKGTPYWM
APEVILQTGH SFSADIWSVG CTVIEMVTGK APWSQQYKEI AAIFHIGTTK SHPPIPDNIS
SDANDFLLKC LQQEPNLRPT ASELLKHPFV TGKQKESASK DLTSFMDNSC SPLPSELTNI
TSYQTSTSDD VGDICNLGSL TCTLAFPEKS IQNNSLCLKS NNGYDDDDDN DMCLIDDENF
LTYNGETGPS LDNNTDAKKS CDTMSEISDI LKCKFDENSG NGETETKVSM EVDHPSYSED
ENELTESKIK AFLDDKAAEL KKLQTPLYEE FYNGMITCSP ICMESNINNN KREEAPRGFL
KLPPKSRSPS QGHIGRSPSR ATDAACCSKS PESGNSSGAP KNSNASAGAE QESNSQSVAL
SEIERKWKEE LDQELERKRR EITRQAGMGS SPRDRSLSRH REKSRFASPG K
