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 27-MAR-2024, entry version 152.
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};
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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.Q8RWL6; -.
DR iPTMnet; Q8RWL6; -.
DR PaxDb; 3702-AT4G35780-1; -.
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; AT4G35780; STY17.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_000288_7_28_1; -.
DR InParanoid; Q8RWL6; -.
DR OMA; PRQHRMK; -.
DR OrthoDB; 3039133at2759; -.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd04928; ACT_TyrKc; 1.
DR CDD; cd13999; STKc_MAP3K-like; 1.
DR Gene3D; 3.30.70.260; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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 PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR23257:SF970; SERINE_THREONINE-PROTEIN KINASE STY46; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF55021; ACT-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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
//
