ANP1_ARATH
ID ANP1_ARATH Reviewed; 666 AA.
AC O22040; O04030; O22039; Q8GZ05;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase ANP1;
DE EC=2.7.11.25;
DE AltName: Full=Arabidopsis NPK1-related kinase 1;
GN Name=ANP1; OrderedLocusNames=At1g09000; ORFNames=F7G19.13;
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 [MRNA] (ISOFORMS 1S AND 1L), 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 [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1L).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1L).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP FUNCTION, ACTIVITY REGULATION, AND MUTAGENESIS OF LYS-98.
RX PubMed=10717008; DOI=10.1073/pnas.97.6.2940;
RA Kovtun Y., Chiu W.-L., Tena G., Sheen J.;
RT "Functional analysis of oxidative stress-activated mitogen-activated
RT protein kinase cascade in plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:2940-2945(2000).
RN [7]
RP FUNCTION.
RX PubMed=12034900; DOI=10.1105/tpc.001164;
RA Krysan P.J., Jester P.J., Gottwald J.R., Sussman M.R.;
RT "An Arabidopsis mitogen-activated protein kinase kinase kinase gene family
RT encodes essential positive regulators of cytokinesis.";
RL Plant Cell 14:1109-1120(2002).
RN [8]
RP NOMENCLATURE.
RX PubMed=12119167; DOI=10.1016/s1360-1385(02)02302-6;
RG MAPK group;
RT "Mitogen-activated protein kinase cascades in plants: a new nomenclature.";
RL Trends Plant Sci. 7:301-308(2002).
CC -!- FUNCTION: May be involved in an oxidative stress-mediated signaling
CC cascade that phosphorylates downstream MAP kinases MPK3 and MPK6. May
CC suppress auxin signaling that promotes cell cycle. Functionally
CC redundant to ANP2 and ANP3 in the positive regulation of cytokinesis.
CC {ECO:0000269|PubMed:10717008, ECO:0000269|PubMed:12034900}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1L;
CC IsoId=O22040-1; Sequence=Displayed;
CC Name=1S;
CC IsoId=O22040-2; Sequence=VSP_010124, VSP_010125;
CC -!- TISSUE SPECIFICITY: Expressed in roots, inflorescence stems, flower
CC buds and flowers. Low amount in rosette and cauline leaves.
CC {ECO:0000269|PubMed:9263451}.
CC -!- MISCELLANEOUS: The protein kinase activity of isoform 1S is higher than
CC that of isoform 1L.
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=AAB70419.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB000796; BAA21854.1; -; mRNA.
DR EMBL; AB000797; BAA21855.1; -; mRNA.
DR EMBL; AC000106; AAB70419.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28381.1; -; Genomic_DNA.
DR EMBL; AK117282; BAC41954.1; -; mRNA.
DR EMBL; BT005949; AAO64884.1; -; mRNA.
DR PIR; H86221; H86221.
DR RefSeq; NP_563832.2; NM_100771.4. [O22040-1]
DR AlphaFoldDB; O22040; -.
DR SMR; O22040; -.
DR BioGRID; 22662; 2.
DR STRING; 3702.AT1G09000.1; -.
DR PaxDb; O22040; -.
DR PRIDE; O22040; -.
DR ProteomicsDB; 244449; -. [O22040-1]
DR EnsemblPlants; AT1G09000.1; AT1G09000.1; AT1G09000. [O22040-1]
DR GeneID; 837421; -.
DR Gramene; AT1G09000.1; AT1G09000.1; AT1G09000. [O22040-1]
DR KEGG; ath:AT1G09000; -.
DR Araport; AT1G09000; -.
DR TAIR; locus:2035989; AT1G09000.
DR eggNOG; KOG0198; Eukaryota.
DR HOGENOM; CLU_020952_1_0_1; -.
DR InParanoid; O22040; -.
DR OrthoDB; 361120at2759; -.
DR PhylomeDB; O22040; -.
DR PRO; PR:O22040; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O22040; baseline and differential.
DR Genevisible; O22040; AT.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; ISS:TAIR.
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:0004674; F:protein serine/threonine kinase activity; HDA:TAIR.
DR GO; GO:0046777; P:protein autophosphorylation; HDA:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0006979; P:response to oxidative stress; IDA:TAIR.
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 Alternative splicing; ATP-binding; Coiled coil; Isopeptide bond; Kinase;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Ubl conjugation.
FT CHAIN 1..666
FT /note="Mitogen-activated protein kinase kinase kinase ANP1"
FT /id="PRO_0000086270"
FT DOMAIN 69..331
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 452..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 101..131
FT /evidence="ECO:0000255"
FT COILED 620..643
FT /evidence="ECO:0000255"
FT COMPBIAS 550..587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..666
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 197
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 75..83
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CROSSLNK 109
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:O22042"
FT CROSSLNK 111
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:O22042"
FT VAR_SEQ 372..376
FT /note="VGDMC -> MMRIS (in isoform 1S)"
FT /evidence="ECO:0000303|PubMed:9263451"
FT /id="VSP_010124"
FT VAR_SEQ 377..666
FT /note="Missing (in isoform 1S)"
FT /evidence="ECO:0000303|PubMed:9263451"
FT /id="VSP_010125"
FT MUTAGEN 98
FT /note="K->M: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:10717008"
SQ SEQUENCE 666 AA; 73470 MW; 588C6339CDC58C18 CRC64;
MQDFFGSVRR SLVFRPSSDD DNQENQPPFP GVLADKITSC IRKSKIFIKP SFSPPPPANT
VDMAPPISWR KGQLIGRGAF GTVYMGMNLD SGELLAVKQV LIAANFASKE KTQAHIQELE
EEVKLLKNLS HPNIVRYLGT VREDDTLNIL LEFVPGGSIS SLLEKFGPFP ESVVRTYTRQ
LLLGLEYLHN HAIMHRDIKG ANILVDNKGC IKLADFGASK QVAELATMTG AKSMKGTPYW
MAPEVILQTG HSFSADIWSV GCTVIEMVTG KAPWSQQYKE VAAIFFIGTT KSHPPIPDTL
SSDAKDFLLK CLQEVPNLRP TASELLKHPF VMGKHKESAS TDLGSVLNNL STPLPLQINN
TKSTPDSTCD DVGDMCNFGS LNYSLVDPVK SIQNKNLWQQ NDNGGDEDDM CLIDDENFLT
FDGEMSSTLE KDCHLKKSCD DISDMSIALK SKFDESPGNG EKESTMSMEC DQPSYSEDDD
ELTESKIKAF LDEKAADLKK LQTPLYEEFY NSLITFSPSC MESNLSNSKR EDTARGFLKL
PPKSRSPSRG PLGGSPSRAT DATSCSKSPG SGGSRELNIN NGGDEASQDG VSARVTDWRG
LVVDTKQELS QCVALSEIEK KWKEELDQEL ERKRQEIMRQ AGLGSSPRDR GMSRQREKSR
FASPGK
