PBL12_ARATH
ID PBL12_ARATH Reviewed; 424 AA.
AC O64842; Q39229; Q6NMK5;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Probable serine/threonine-protein kinase PBL12 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=PBS1-like protein 12 {ECO:0000303|PubMed:20413097};
DE AltName: Full=Root-specific kinase 1 {ECO:0000305};
GN Name=PBL12 {ECO:0000303|PubMed:20413097};
GN Synonyms=ARSK1 {ECO:0000303|PubMed:7655506};
GN OrderedLocusNames=At2g26290 {ECO:0000312|Araport:AT2G26290};
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 [GENOMIC DNA], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=7655506; DOI=10.1046/j.1365-313x.1995.08010037.x;
RA Hwang I., Goodman H.M.;
RT "An Arabidopsis thaliana root-specific kinase homolog is induced by
RT dehydration, ABA, and NaCl.";
RL Plant J. 8:37-43(1995).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 131-424 AND 171-424.
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
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 play a role in the signal transduction pathway of osmotic
CC stress (Probable). May be involved in plant defense signaling (By
CC similarity). {ECO:0000250|UniProtKB:O48814,
CC ECO:0000305|PubMed:7655506}.
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:Q9ZUF4}.
CC -!- TISSUE SPECIFICITY: Expressed specifically in roots.
CC {ECO:0000269|PubMed:7655506}.
CC -!- INDUCTION: Induced in roots by exposure to air, abscisic acid (ABA) and
CC salt treatment. {ECO:0000269|PubMed:7655506}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA81538.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L22302; AAA81538.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AC004484; AAC14522.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07819.1; -; Genomic_DNA.
DR EMBL; BT010769; AAR23739.1; -; mRNA.
DR EMBL; BT011654; AAS47660.1; -; mRNA.
DR PIR; F84658; F84658.
DR RefSeq; NP_180197.1; NM_128186.3.
DR AlphaFoldDB; O64842; -.
DR SMR; O64842; -.
DR IntAct; O64842; 1.
DR STRING; 3702.AT2G26290.1; -.
DR iPTMnet; O64842; -.
DR PaxDb; O64842; -.
DR PRIDE; O64842; -.
DR ProteomicsDB; 236283; -.
DR EnsemblPlants; AT2G26290.1; AT2G26290.1; AT2G26290.
DR GeneID; 817169; -.
DR Gramene; AT2G26290.1; AT2G26290.1; AT2G26290.
DR KEGG; ath:AT2G26290; -.
DR Araport; AT2G26290; -.
DR TAIR; locus:2057770; AT2G26290.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_21_2_1; -.
DR InParanoid; O64842; -.
DR OMA; EWMAEII; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; O64842; -.
DR PRO; PR:O64842; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64842; 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:0016301; F:kinase activity; ISS:TAIR.
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; 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; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW Plant defense; Reference proteome; Serine/threonine-protein kinase;
KW Stress response; Transferase.
FT CHAIN 1..424
FT /note="Probable serine/threonine-protein kinase PBL12"
FT /id="PRO_0000438607"
FT DOMAIN 88..368
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 218
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 94..102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 190
FT /note="W -> YV (in Ref. 1; AAA81538)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="A -> R (in Ref. 1; AAA81538)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 424 AA; 48086 MW; C11DD637020B8307 CRC64;
MAVFKKKKTS LTSLFLGCYK AKNASKYEGG EKAVMKIRTC PAFKRLSLSD ISDPSSPMSV
MDDLSHSFTS QKLRLFTLSE LRVITHNFSR SNMLGEGGFG PVYKGFIDDK VKPGIEAQPV
AVKALDLHGH QGHREWLAEI LFLGQLSNKH LVKLIGFCCE EEQRVLVYEY MPRGSLENQL
FRRNSLAMAW GIRMKIALGA AKGLAFLHEA EKPVIYRDFK TSNILLDSDY NAKLSDFGLA
KDGPEGEHTH VTTRVMGTQG YAAPEYIMTG HLTTMNDVYS FGVVLLELIT GKRSMDNTRT
RREQSLVEWA RPMLRDQRKL ERIIDPRLAN QHKTEAAQVA ASLAYKCLSQ HPKYRPTMCE
VVKVLESIQE VDIRKHDGNN NKEGKKFVDI NKFRHHRKGK RRVNIAYSDS LVYKESKAKQ
NDGI
