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 08-NOV-2023, entry version 175. 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}; 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; 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; 3702-AT1G09000-1; -. 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; AT1G09000; NP1. DR eggNOG; KOG0198; Eukaryota. DR HOGENOM; CLU_020952_1_0_1; -. DR InParanoid; O22040; -. DR OrthoDB; 145974at2759; -. 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: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:0006979; P:response to oxidative stress; IDA:TAIR. DR CDD; cd06606; STKc_MAPKKK; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. 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 PANTHER; PTHR48016; MAP KINASE KINASE KINASE SSK2-RELATED-RELATED; 1. DR PANTHER; PTHR48016:SF56; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 19; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 //