PBL10_ARATH
ID PBL10_ARATH Reviewed; 412 AA.
AC P46573; Q7GAG3; Q9SLH5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Probable serine/threonine-protein kinase PBL10 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=PBS1-like protein 10 {ECO:0000303|PubMed:20413097};
DE AltName: Full=Protein kinase 1B {ECO:0000305};
GN Name=PBL10 {ECO:0000303|PubMed:20413097};
GN Synonyms=APK1B {ECO:0000303|PubMed:1450380},
GN PIX16 {ECO:0000303|PubMed:23951354}; OrderedLocusNames=At2g28930;
GN ORFNames=T9I4.1;
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=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 [MRNA] OF 143-346.
RC STRAIN=cv. Columbia;
RX PubMed=1450380; DOI=10.1007/bf00046450;
RA Hirayama T., Oka A.;
RT "Novel protein kinase of Arabidopsis thaliana (APK1) that phosphorylates
RT tyrosine, serine and threonine.";
RL Plant Mol. Biol. 20:653-662(1992).
RN [4]
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).
RN [5]
RP INTERACTION WITH XANTHOMONAS CAMPESTRIS XOPAC/AVRAC.
RX PubMed=23951354; DOI=10.1371/journal.pone.0073469;
RA Guy E., Lautier M., Chabannes M., Roux B., Lauber E., Arlat M., Noel L.D.;
RT "xopAC-triggered immunity against Xanthomonas depends on Arabidopsis
RT receptor-like cytoplasmic kinase genes PBL2 and RIPK.";
RL PLoS ONE 8:E73469-E73469(2013).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=24828466; DOI=10.1371/journal.pone.0097161;
RA Elhaddad N.S., Hunt L., Sloan J., Gray J.E.;
RT "Light-induced stomatal opening is affected by the guard cell protein
RT kinase APK1b.";
RL PLoS ONE 9:E97161-E97161(2014).
CC -!- FUNCTION: Possible bi-functional kinase. In vitro, it exhibits
CC serine/threonine activity. In vivo, can phosphorylate tyrosine residues
CC of limited substrates (By similarity). May be involved in plant defense
CC signaling (By similarity). Required for full light-induced stomatal
CC opening (PubMed:24828466). {ECO:0000250|UniProtKB:O48814,
CC ECO:0000250|UniProtKB:Q06548, ECO:0000269|PubMed:24828466}.
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 -!- SUBUNIT: Interacts with the Xanthomonas campestris effector
CC XopAC/AvrAC. {ECO:0000269|PubMed:23951354}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O48814};
CC Lipid-anchor {ECO:0000250|UniProtKB:O48814}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=P46573-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in stomatal guard cells of leaves.
CC {ECO:0000269|PubMed:24828466}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. Leaves of well-watered mutant plants have increased
CC relative water content due to decreased stomata opening.
CC {ECO:0000269|PubMed:24828466}.
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; AC005315; AAC33221.1; -; Genomic_DNA.
DR EMBL; AC005727; AAM15075.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08190.1; -; Genomic_DNA.
DR EMBL; D10152; BAA20968.1; -; mRNA.
DR PIR; T02725; T02725.
DR RefSeq; NP_001031439.1; NM_001036362.3. [P46573-1]
DR AlphaFoldDB; P46573; -.
DR SMR; P46573; -.
DR BioGRID; 2792; 2.
DR IntAct; P46573; 1.
DR STRING; 3702.AT2G28930.1; -.
DR iPTMnet; P46573; -.
DR PaxDb; P46573; -.
DR PRIDE; P46573; -.
DR ProteomicsDB; 236796; -. [P46573-1]
DR EnsemblPlants; AT2G28930.2; AT2G28930.2; AT2G28930. [P46573-1]
DR GeneID; 817442; -.
DR Gramene; AT2G28930.2; AT2G28930.2; AT2G28930. [P46573-1]
DR KEGG; ath:AT2G28930; -.
DR Araport; AT2G28930; -.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_21_1_1; -.
DR InParanoid; P46573; -.
DR OMA; DAMGNCL; -.
DR PhylomeDB; P46573; -.
DR BRENDA; 2.7.10.2; 399.
DR PRO; PR:P46573; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P46573; baseline and differential.
DR Genevisible; P46573; AT.
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:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:1902458; P:positive regulation of stomatal opening; IMP:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
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 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 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Kinase; Lipoprotein;
KW Membrane; Myristate; Nucleotide-binding; Palmitate; Phosphoprotein;
KW Plant defense; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Transit peptide; Tyrosine-protein kinase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..412
FT /note="Probable serine/threonine-protein kinase PBL10"
FT /id="PRO_0000024303"
FT DOMAIN 69..356
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 15..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 204
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 75..83
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 58
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 152
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 239
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 244
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 252
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 4
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9FE20"
SQ SEQUENCE 412 AA; 45746 MW; EB1CA0B1A626A5DA CRC64;
MGICLSAQIK AVSPGASPKY MSSEANDSLG SKSSSVSIRT NPRTEGEILQ SPNLKSFTFA
ELKAATRNFR PDSVLGEGGF GSVFKGWIDE QTLTASKPGT GVVIAVKKLN QDGWQGHQEW
LAEVNYLGQF SHPNLVKLIG YCLEDEHRLL VYEFMPRGSL ENHLFRRGSY FQPLSWTLRL
KVALGAAKGL AFLHNAETSV IYRDFKTSNI LLDSEYNAKL SDFGLAKDGP TGDKSHVSTR
IMGTYGYAAP EYLATGHLTT KSDVYSYGVV LLEVLSGRRA VDKNRPPGEQ KLVEWARPLL
ANKRKLFRVI DNRLQDQYSM EEACKVATLA LRCLTFEIKL RPNMNEVVSH LEHIQTLNEA
GGRNIDMVQR RMRRRSDSVA INQKPNAGFA RQTAVGVIAT AYPRPSDSPL FV
