STY46_ARATH
ID STY46_ARATH Reviewed; 575 AA.
AC F4JTP5; Q56Z78; Q9SZM7;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Serine/threonine-protein kinase STY46 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000269|PubMed:17090544};
DE AltName: Full=Serine/threonine/tyrosine-protein kinase 46 {ECO:0000303|PubMed:16429265};
GN Name=STY46 {ECO:0000303|PubMed:16429265};
GN OrderedLocusNames=At4g38470 {ECO:0000312|Araport:AT4G38470};
GN ORFNames=F20M13.30 {ECO:0000312|EMBL:CAB37503.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 [LARGE SCALE MRNA] OF 422-575.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP AUTOPHOSPHORYLATION.
RX PubMed=17090544; DOI=10.1074/jbc.m606580200;
RA Martin T., Sharma R., Sippel C., Waegemann K., Soll J., Vothknecht U.C.;
RT "A protein kinase family in Arabidopsis phosphorylates chloroplast
RT precursor proteins.";
RL J. Biol. Chem. 281:40216-40223(2006).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16429265; DOI=10.1007/s11103-005-4109-7;
RA Rudrabhatla P., Reddy M.M., Rajasekharan R.;
RT "Genome-wide analysis and experimentation of plant
RT serine/threonine/tyrosine-specific protein kinases.";
RL Plant Mol. Biol. 60:293-319(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-443, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-443, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-443, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [9]
RP FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT
RP THR-443, MUTAGENESIS OF THR-443, AND DISRUPTION PHENOTYPE.
RX PubMed=21799034; DOI=10.1104/pp.111.182774;
RA Lamberti G., Gugel I.L., Meurer J., Soll J., Schwenkert S.;
RT "The cytosolic kinases STY8, STY17, and STY46 are involved in chloroplast
RT differentiation in Arabidopsis.";
RL Plant Physiol. 157:70-85(2011).
CC -!- FUNCTION: Serine/threonine protein kinase that specifically
CC phosphorylates chloroplast precursor proteins in the cytosol within the
CC cleavable presequences (transit peptides). May be part of a cytosolic
CC regulatory network involved in chloroplast protein import. Does not
CC phosphorylate mitochondrion precursor proteins. Specific for ATP and
CC does not utilize other NTPs (PubMed:17090544, PubMed:16429265). Plays a
CC role in chloroplast biogenesis and differentiation in cotyledons,
CC possibly through phosphorylation of chloroplast preproteins
CC (PubMed:21799034). {ECO:0000269|PubMed:17090544,
CC ECO:0000269|PubMed:21799034}.
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=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:17090544};
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=2.7.11.1; Evidence={ECO:0000269|PubMed:17090544};
CC -!- ACTIVITY REGULATION: Activated by autophosphorylation at Thr-443.
CC {ECO:0000269|PubMed:21799034}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=67 uM for ATP {ECO:0000269|PubMed:17090544};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:21799034}.
CC -!- PTM: Autophosphorylated on serine and threonine residues.
CC Autophosphorylated at Thr-443. {ECO:0000269|PubMed:17090544,
CC ECO:0000269|PubMed:21799034}.
CC -!- DISRUPTION PHENOTYPE: Retarded growth. {ECO:0000269|PubMed:21799034}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD94956.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB37503.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80511.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL035540; CAB37503.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161593; CAB80511.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86931.1; -; Genomic_DNA.
DR EMBL; AK221091; BAD94956.1; ALT_INIT; mRNA.
DR PIR; T05675; T05675.
DR RefSeq; NP_568041.1; NM_120008.2.
DR AlphaFoldDB; F4JTP5; -.
DR SMR; F4JTP5; -.
DR STRING; 3702.AT4G38470.1; -.
DR iPTMnet; F4JTP5; -.
DR PaxDb; F4JTP5; -.
DR PRIDE; F4JTP5; -.
DR ProteomicsDB; 228310; -.
DR DNASU; 830003; -.
DR EnsemblPlants; AT4G38470.1; AT4G38470.1; AT4G38470.
DR GeneID; 830003; -.
DR Gramene; AT4G38470.1; AT4G38470.1; AT4G38470.
DR KEGG; ath:AT4G38470; -.
DR Araport; AT4G38470; -.
DR TAIR; locus:2121154; AT4G38470.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_000288_7_28_1; -.
DR InParanoid; F4JTP5; -.
DR OrthoDB; 173077at2759; -.
DR SABIO-RK; F4JTP5; -.
DR PRO; PR:F4JTP5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JTP5; baseline and differential.
DR Genevisible; F4JTP5; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IDA:TAIR.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0009658; P:chloroplast organization; IGI:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IDA:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF01842; ACT; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF55021; SSF55021; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..575
FT /note="Serine/threonine-protein kinase STY46"
FT /id="PRO_0000434000"
FT DOMAIN 178..252
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT DOMAIN 290..543
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 116..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 411
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 296..304
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 317
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 443
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:21799034,
FT ECO:0007744|PubMed:18433157, ECO:0007744|PubMed:19245862,
FT ECO:0007744|PubMed:19376835"
FT MUTAGEN 443
FT /note="T->A: Loss of autophosphorylation and enzyme
FT activation."
FT /evidence="ECO:0000269|PubMed:21799034"
SQ SEQUENCE 575 AA; 64811 MW; 299A583DB2E1CEF9 CRC64;
MVMEDNESCA SRVIFDALPT SQATMDRRER IKMEVFDEVL RRLRQSDIED AHLPGFEDDL
WNHFNRLPAR YALDVNVERA EDVLMHKRLL HSAYDPQNRP AIEVHLVQVQ PAGISADLDS
TSNDAGHSSP TRKSIHPPPA FGSSPNLEAL ALAASLSQDE DADNSVHNNS LYSRPLHEIT
FSTEDKPKLL FQLTALLAEL GLNIQEAHAF STTDGYSLDV FVVDGWPYEE TERLRISLEK
EAAKIELQSQ SWPMQQSFSP EKENGQTGAR THVPIPNDGT DVWEINLKHL KFGHKIASGS
YGDLYKGTYC SQEVAIKVLK PERLDSDLEK EFAQEVFIMR KVRHKNVVQF IGACTKPPHL
CIVTEFMPGG SVYDYLHKQK GVFKLPTLFK VAIDICKGMS YLHQNNIIHR DLKAANLLMD
ENEVVKVADF GVARVKAQTG VMTAETGTYR WMAPEVIEHK PYDHKADVFS YGIVLWELLT
GKLPYEYMTP LQAAVGVVQK GLRPTIPKNT HPKLAELLER LWEHDSTQRP DFSEIIEQLQ
EIAKEVGEEG EEKKKSSTGL GGGIFAALRR STTHH
