PBL6_ARATH
ID PBL6_ARATH Reviewed; 424 AA.
AC Q9SIB6; Q38979;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Probable serine/threonine-protein kinase PBL6 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=PBS1-like protein 6 {ECO:0000303|PubMed:20413097};
GN Name=PBL6 {ECO:0000303|PubMed:20413097};
GN Synonyms=AK14 {ECO:0000303|PubMed:8534852};
GN OrderedLocusNames=At2g28590 {ECO:0000312|Araport:AT2G28590};
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;
RA Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 227-283.
RC STRAIN=cv. Eil-0; TISSUE=Leaf;
RX PubMed=8534852; DOI=10.1007/bf00020984;
RA Thuemmler F., Kirchner M., Teuber R., Dittrich P.;
RT "Differential accumulation of the transcripts of 22 novel protein kinase
RT genes in Arabidopsis thaliana.";
RL Plant Mol. Biol. 29:551-565(1995).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=20413097; DOI=10.1016/j.chom.2010.03.007;
RA Zhang J., Li W., Xiang T., Liu Z., Laluk K., Ding X., Zou Y., Gao M.,
RA Zhang X., Chen S., Mengiste T., Zhang Y., Zhou J.M.;
RT "Receptor-like cytoplasmic kinases integrate signaling from multiple plant
RT immune receptors and are targeted by a Pseudomonas syringae effector.";
RL Cell Host Microbe 7:290-301(2010).
CC -!- FUNCTION: May be involved in plant defense signaling.
CC {ECO:0000250|UniProtKB:O48814}.
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:0000305};
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:0000305};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O48814};
CC Lipid-anchor {ECO:0000250|UniProtKB:O48814}.
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; AC006587; AAM15298.1; -; Genomic_DNA.
DR EMBL; AC007171; AAD24376.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08146.1; -; Genomic_DNA.
DR EMBL; BT029736; ABM06006.1; -; mRNA.
DR EMBL; X86959; CAA60522.1; -; Genomic_DNA.
DR PIR; G84686; G84686.
DR PIR; S66327; S66327.
DR RefSeq; NP_180426.1; NM_128419.3.
DR AlphaFoldDB; Q9SIB6; -.
DR SMR; Q9SIB6; -.
DR STRING; 3702.AT2G28590.1; -.
DR PaxDb; Q9SIB6; -.
DR PRIDE; Q9SIB6; -.
DR ProteomicsDB; 236795; -.
DR EnsemblPlants; AT2G28590.1; AT2G28590.1; AT2G28590.
DR GeneID; 817407; -.
DR Gramene; AT2G28590.1; AT2G28590.1; AT2G28590.
DR KEGG; ath:AT2G28590; -.
DR Araport; AT2G28590; -.
DR TAIR; locus:2056613; AT2G28590.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_21_0_1; -.
DR InParanoid; Q9SIB6; -.
DR OMA; DHLASCN; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9SIB6; -.
DR PRO; PR:Q9SIB6; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SIB6; baseline and differential.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
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 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Kinase; Lipoprotein; Membrane; Myristate;
KW Nucleotide-binding; Palmitate; Phosphoprotein; Plant defense;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..424
FT /note="Probable serine/threonine-protein kinase PBL6"
FT /id="PRO_0000438606"
FT DOMAIN 98..377
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 225
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 104..112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 127
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 87
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 172
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 260
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 265
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 273
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:Q9FE20"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9FE20"
FT CONFLICT 280
FT /note="T -> A (in Ref. 4; CAA60522)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 424 AA; 47279 MW; 3A7E22F78F8B4B8D CRC64;
MGCFGRTPKS NKRSDTKTTK NNDFTPKKLT VNANRDKLTQ PSSDCLKVSI CGDVSKEIVT
KKDQLALDAK DTNVEDEVIV KKAQTFTFEE LSVSTGNFKS DCFLGEGGFG KVYKGFIEKI
NQVVAIKQLD RNGAQGIREF VVEVLTLSLA DHPNLVKLIG FCAEGVQRLL VYEYMPLGSL
DNHLHDLPSG KNPLAWNTRM KIAAGAARGL EYLHDTMKPP VIYRDLKCSN ILIDEGYHAK
LSDFGLAKVG PRGSETHVST RVMGTYGYCA PDYALTGQLT FKSDVYSFGV VLLELITGRK
AYDNTRTRNH QSLVEWANPL FKDRKNFKKM VDPLLEGDYP VRGLYQALAI AAMCVQEQPS
MRPVIADVVM ALDHLASSKY DRSHRQKQDN VTETKVDEEK TLTTESNVCV EEKQEIKICS
DQAT
