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 19-MAR-2014, entry version 115. 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; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1S AND 1L), AND TISSUE RP 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 RT protein 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., RA White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., RA Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., RA Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., RA Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., RA Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., RA Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., RA Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., RA Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., RA Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., RA Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., RA Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., RA Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., RA 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., RA Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis RT thaliana."; RL Nature 408:816-820(2000). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Resource (TAIR); RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. 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., RA Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., RA Shibata K., 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., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [6] RP FUNCTION, ENZYME 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 RT family 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 RT nomenclature."; RL Trends Plant Sci. 7:301-308(2002). CC -!- FUNCTION: May be involved in an oxidative stress-mediated CC signaling cascade that phosphorylates downstream MAP kinases MPK3 CC and MPK6. May suppress auxin signaling that promotes cell cycle. CC Functionally redundant to ANP2 and ANP3 in the positive regulation CC of cytokinesis. CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. 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, CC flower buds and flowers. Low amount in rosette and cauline leaves. CC -!- MISCELLANEOUS: The protein kinase activity of isoform 1S is higher CC than 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 -!- SIMILARITY: Contains 1 protein kinase domain. CC -!- SEQUENCE CAUTION: CC Sequence=AAB70419.1; Type=Erroneous gene model prediction; 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_100771.3. DR UniGene; At.48170; -. DR UniGene; At.70237; -. DR ProteinModelPortal; O22040; -. DR SMR; O22040; 74-331. DR BioGrid; 22662; 2. DR PaxDb; O22040; -. DR PRIDE; O22040; -. DR EnsemblPlants; AT1G09000.1; AT1G09000.1; AT1G09000. DR GeneID; 837421; -. DR KEGG; ath:AT1G09000; -. DR GeneFarm; 898; 89. DR TAIR; AT1G09000; -. DR eggNOG; COG0515; -. DR HOGENOM; HOG000033953; -. DR InParanoid; O22040; -. DR OMA; HKESAST; -. DR PhylomeDB; O22040; -. DR ProtClustDB; CLSN2690809; -. DR BioCyc; ARA:AT1G09000-MONOMER; -. DR PRO; PR:O22040; -. DR Genevestigator; O22040; -. 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:0009908; P:flower development; IGI:TAIR. DR GO; GO:0046777; P:protein autophosphorylation; IDA:TAIR. DR GO; GO:0006979; P:response to oxidative stress; IDA:TAIR. DR InterPro; IPR011009; Kinase-like_dom. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR002290; Ser/Thr_dual-sp_kinase_dom. 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; Complete proteome; KW Kinase; Nucleotide-binding; Reference proteome; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1 666 Mitogen-activated protein kinase kinase FT kinase ANP1. FT /FTId=PRO_0000086270. FT DOMAIN 69 331 Protein kinase. FT NP_BIND 75 83 ATP (By similarity). FT COILED 101 131 Potential. FT COILED 620 643 Potential. FT ACT_SITE 197 197 Proton acceptor (By similarity). FT BINDING 98 98 ATP (By similarity). FT VAR_SEQ 372 376 VGDMC -> MMRIS (in isoform 1S). FT /FTId=VSP_010124. FT VAR_SEQ 377 666 Missing (in isoform 1S). FT /FTId=VSP_010125. FT MUTAGEN 98 98 K->M: Loss of kinase activity. 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 //