ID STY17_ARATH Reviewed; 570 AA. AC Q8RWL6; O81808; DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 03-AUG-2022, entry version 144. DE RecName: Full=Serine/threonine-protein kinase STY17 {ECO:0000305}; DE EC=2.7.11.1 {ECO:0000269|PubMed:17090544}; DE AltName: Full=Serine/threonine/tyrosine-protein kinase 17 {ECO:0000303|PubMed:16429265}; GN Name=STY17 {ECO:0000303|PubMed:16429265}; GN OrderedLocusNames=At4g35780 {ECO:0000312|Araport:AT4G35780}; GN ORFNames=F8D20.290 {ECO:0000312|EMBL:CAA20048.1}; 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]. 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 [4] RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. 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 IDENTIFICATION BY 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 [7] RP FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT RP THR-445, AND MUTAGENESIS OF THR-445. 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-445. CC {ECO:0000269|PubMed:21799034}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=14 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-445. {ECO:0000269|PubMed:21799034}. CC -!- MISCELLANEOUS: Plants silencing STY17 does not show visible phenotype CC under normal growth conditions, but plants silencing STY17 in the CC double mutant sty8 and sty46 background show more severe retarded CC growth compared to the double mutant itself. CC {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=CAA20048.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=CAB81487.1; 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; AL031135; CAA20048.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL161588; CAB81487.1; ALT_SEQ; Genomic_DNA. DR EMBL; CP002687; AEE86563.1; -; Genomic_DNA. DR EMBL; AY093017; AAM13016.1; -; mRNA. DR EMBL; AY128938; AAM91338.1; -; mRNA. DR PIR; T04683; T04683. DR PIR; T04688; T04688. DR RefSeq; NP_195303.2; NM_119744.5. DR AlphaFoldDB; Q8RWL6; -. DR SMR; Q8RWL6; -. DR IntAct; Q8RWL6; 2. DR STRING; 3702.AT4G35780.1; -. DR iPTMnet; Q8RWL6; -. DR PaxDb; Q8RWL6; -. DR PRIDE; Q8RWL6; -. DR ProteomicsDB; 228309; -. DR EnsemblPlants; AT4G35780.1; AT4G35780.1; AT4G35780. DR GeneID; 829731; -. DR Gramene; AT4G35780.1; AT4G35780.1; AT4G35780. DR KEGG; ath:AT4G35780; -. DR Araport; AT4G35780; -. DR TAIR; locus:2128043; AT4G35780. DR eggNOG; KOG0192; Eukaryota. DR HOGENOM; CLU_000288_7_28_1; -. DR InParanoid; Q8RWL6; -. DR OMA; CSKQKSI; -. DR OrthoDB; 173077at2759; -. DR PhylomeDB; Q8RWL6; -. DR SABIO-RK; Q8RWL6; -. DR PRO; PR:Q8RWL6; -. DR Proteomes; UP000006548; Chromosome 4. DR ExpressionAtlas; Q8RWL6; baseline and differential. DR Genevisible; Q8RWL6; 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; ISS:TAIR. DR GO; GO:0009658; P:chloroplast organization; IGI:TAIR. DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro. 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; 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..570 FT /note="Serine/threonine-protein kinase STY17" FT /id="PRO_0000433999" FT DOMAIN 180..260 FT /note="ACT" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007" FT DOMAIN 292..545 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 112..145 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 413 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 298..306 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 319 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 441 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O22558" FT MOD_RES 445 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:21799034" FT MUTAGEN 445 FT /note="T->A: Loss of autophosphorylation and enzyme FT activation." FT /evidence="ECO:0000269|PubMed:21799034" SQ SEQUENCE 570 AA; 64696 MW; D0961D218BE49344 CRC64; MAIKEETEES CGSRAVVASI TKESPRQHRM KLEVYGEVLQ RIQESNYEEA NFPGFDDLLW LHFNRLPARY ALDVNVERAE DVLTHQRLLK LAEDPATRPV FEVRCVQVSP TLNGNSGDVD PSDPAVNEDA QSSYNSRSLA PPTFGSSPNF EALTQAYKDH AQDDDSAVNA QLPNSRPMHE ITFSTIDRPK LLSQLTSMLG ELGLNIQEAH AFSTADGFSL DVFVVDGWSQ EETEGLKDAL KKEIRKFKDQ PCSKQKSITF FEHDKSTNEL LPACVEIPTD GTDEWEIDMK QLKIEKKVAC GSYGELFRGT YCSQEVAIKI LKPERVNAEM LREFSQEVYI MRKVRHKNVV QFIGACTRSP NLCIVTEFMT RGSIYDFLHK HKGVFKIQSL LKVALDVSKG MNYLHQNNII HRDLKTANLL MDEHEVVKVA DFGVARVQTE SGVMTAETGT YRWMAPEVIE HKPYDHRADV FSYAIVLWEL LTGELPYSYL TPLQAAVGVV QKGLRPKIPK ETHPKLTELL EKCWQQDPAL RPNFAEIIEM LNQLIREVGD DERHKDKHGG YFSGLKKGHR //