PBL25_ARATH
ID PBL25_ARATH Reviewed; 381 AA.
AC Q9LRY1; Q1PEM1;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Probable serine/threonine-protein kinase PBL25 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=PBS1-like protein 25 {ECO:0000303|PubMed:20413097};
GN Name=PBL25 {ECO:0000303|PubMed:20413097};
GN OrderedLocusNames=At3g24790 {ECO:0000312|Araport:AT3G24790};
GN ORFNames=K7P8.8 {ECO:0000312|EMBL:BAB02889.1};
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
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] OF 19-381.
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
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).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AEE76947.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB028609; BAB02889.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76947.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002686; ANM64380.1; -; Genomic_DNA.
DR EMBL; DQ446696; ABE65965.1; -; mRNA.
DR RefSeq; NP_001326412.1; NM_001338709.1.
DR RefSeq; NP_189123.2; NM_113391.3.
DR AlphaFoldDB; Q9LRY1; -.
DR SMR; Q9LRY1; -.
DR STRING; 3702.AT3G24790.1; -.
DR PRIDE; Q9LRY1; -.
DR ProteomicsDB; 234947; -.
DR EnsemblPlants; AT3G24790.2; AT3G24790.2; AT3G24790.
DR GeneID; 822077; -.
DR Gramene; AT3G24790.2; AT3G24790.2; AT3G24790.
DR KEGG; ath:AT3G24790; -.
DR Araport; AT3G24790; -.
DR TAIR; locus:2087263; AT3G24790.
DR eggNOG; KOG1187; Eukaryota.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9LRY1; -.
DR PRO; PR:Q9LRY1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LRY1; 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;
KW Nucleotide-binding; Palmitate; Phosphoprotein; Plant defense; Receptor;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..381
FT /note="Probable serine/threonine-protein kinase PBL25"
FT /id="PRO_0000438617"
FT DOMAIN 65..342
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 16..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 192
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 71..79
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 54
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 139
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 232
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 240
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9FE20"
SQ SEQUENCE 381 AA; 42427 MW; 8F6949BDFE115A5F CRC64;
MSCFSCFSSK VLDNEGSSMP APYKQPNSPK RTTGEVVAKN ANGPSNNMGA RIFTFRELAT
ATKNFRQECL IGEGGFGRVY KGKLENPAQV VAVKQLDRNG LQGQREFLVE VLMLSLLHHR
NLVNLIGYCA DGDQRLLVYE YMPLGSLEDH LLDLEPGQKP LDWNTRIKIA LGAAKGIEYL
HDEADPPVIY RDLKSSNILL DPEYVAKLSD FGLAKLGPVG DTLHVSSRVM GTYGYCAPEY
QRTGYLTNKS DVYSFGVVLL ELISGRRVID TMRPSHEQNL VTWALPIFRD PTRYWQLADP
LLRGDYPEKS LNQAIAVAAM CLHEEPTVRP LMSDVITALS FLGASSNSSN TGSNHLQQNR
SNKYQDAVQW DSSPRYANSQ M
