STY8_ARATH
ID STY8_ARATH Reviewed; 546 AA.
AC O22558; Q56XF0;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Serine/threonine-protein kinase STY8 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000269|PubMed:17090544};
DE AltName: Full=Serine/threonine/tyrosine-protein kinase 8 {ECO:0000303|PubMed:16429265};
GN Name=STY8 {ECO:0000303|PubMed:16429265};
GN OrderedLocusNames=At2g17700 {ECO:0000312|Araport:AT2G17700};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, 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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-439, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435 AND THR-439, AND
RP IDENTIFICATION BY 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-439, 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 [10]
RP FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT
RP THR-439, MUTAGENESIS OF LYS-409 AND THR-439, 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-439.
CC {ECO:0000269|PubMed:21799034}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=21.6 uM for ATP {ECO:0000269|PubMed:17090544};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17090544,
CC ECO:0000269|PubMed:21799034}.
CC -!- PTM: Autophosphorylated on serine and threonine residues.
CC Autophosphorylated at Thr-439. {ECO:0000269|PubMed:17090544,
CC ECO:0000269|PubMed:21799034}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but the double mutant plants sty8 and sty46 show retarded
CC growth. {ECO:0000269|PubMed:21799034}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; CP002685; AEC06670.1; -; Genomic_DNA.
DR EMBL; AY070086; AAL49781.1; -; mRNA.
DR EMBL; AY096470; AAM20110.1; -; mRNA.
DR EMBL; AK221724; BAD93724.1; -; mRNA.
DR PIR; D84555; D84555.
DR PIR; T08864; T08864.
DR RefSeq; NP_179361.1; NM_127324.5.
DR AlphaFoldDB; O22558; -.
DR SMR; O22558; -.
DR IntAct; O22558; 1.
DR STRING; 3702.AT2G17700.1; -.
DR iPTMnet; O22558; -.
DR PaxDb; O22558; -.
DR PRIDE; O22558; -.
DR ProMEX; O22558; -.
DR ProteomicsDB; 228277; -.
DR EnsemblPlants; AT2G17700.1; AT2G17700.1; AT2G17700.
DR GeneID; 816278; -.
DR Gramene; AT2G17700.1; AT2G17700.1; AT2G17700.
DR KEGG; ath:AT2G17700; -.
DR Araport; AT2G17700; -.
DR TAIR; locus:2827943; AT2G17700.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_000288_7_28_1; -.
DR InParanoid; O22558; -.
DR OMA; GEDRHKD; -.
DR OrthoDB; 173077at2759; -.
DR PhylomeDB; O22558; -.
DR SABIO-RK; O22558; -.
DR PRO; PR:O22558; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22558; baseline and differential.
DR Genevisible; O22558; 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..546
FT /note="Serine/threonine-protein kinase STY8"
FT /id="PRO_0000433998"
FT DOMAIN 174..249
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT DOMAIN 286..539
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 407
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 292..300
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 313
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT MOD_RES 439
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 409
FT /note="K->R: Loss of activity."
FT /evidence="ECO:0000269|PubMed:21799034"
FT MUTAGEN 439
FT /note="T->A: Loss of autophosphorylation and enzyme
FT activation."
FT /evidence="ECO:0000269|PubMed:21799034"
FT CONFLICT 45
FT /note="N -> S (in Ref. 4; BAD93724)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 546 AA; 61509 MW; E74F30F60D91F426 CRC64;
MTIKDESESC GSRAVVASPS QENPRHYRMK LDVYSEVLQR LQESNYEEAT LPDFEDQLWL
HFNRLPARYA LDVKVERAED VLTHQRLLKL AADPATRPVF EVRSVQVSPR ISADSDPAVE
EDAQSSHQPS GPGVLAPPTF GSSPNFEAIT QGSKIVEDVD SVVNATLSTR PMHEITFSTI
DKPKLLSQLT SLLGELGLNI QEAHAFSTVD GFSLDVFVVD GWSQEETDGL RDALSKEILK
LKDQPGSKQK SISFFEHDKS SNELIPACIE IPTDGTDEWE IDVTQLKIEK KVASGSYGDL
HRGTYCSQEV AIKFLKPDRV NNEMLREFSQ EVFIMRKVRH KNVVQFLGAC TRSPTLCIVT
EFMARGSIYD FLHKQKCAFK LQTLLKVALD VAKGMSYLHQ NNIIHRDLKT ANLLMDEHGL
VKVADFGVAR VQIESGVMTA ETGTYRWMAP EVIEHKPYNH KADVFSYAIV LWELLTGDIP
YAFLTPLQAA VGVVQKGLRP KIPKKTHPKV KGLLERCWHQ DPEQRPLFEE IIEMLQQIMK
EVNVVV
