PBL21_ARATH
ID PBL21_ARATH Reviewed; 381 AA.
AC Q9LDZ5; Q67YK2;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Probable serine/threonine-protein kinase PBL21 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=PBS1-like protein 21 {ECO:0000303|PubMed:20413097};
DE AltName: Full=Protein ALTERED SEED GERMINATION 5 {ECO:0000305};
GN Name=PBL21 {ECO:0000303|PubMed:20413097}; Synonyms=ASG5 {ECO:0000305};
GN OrderedLocusNames=At1g20650 {ECO:0000312|Araport:AT1G20650};
GN ORFNames=F2D10.13 {ECO:0000312|EMBL:AAF80637.1},
GN F5M15.3 {ECO:0000312|EMBL:AAF79602.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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].
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION BY 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 [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 -!- PTM: Palmitoylation at Cys-3 and Cys-7 are required for plasma membrane
CC location. {ECO:0000250|UniProtKB:Q9FE20}.
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; AC027665; AAF79602.1; -; Genomic_DNA.
DR EMBL; AC069251; AAF80637.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30001.1; -; Genomic_DNA.
DR EMBL; AK176466; BAD44229.1; -; mRNA.
DR EMBL; AK176526; BAD44289.1; -; mRNA.
DR RefSeq; NP_173489.2; NM_101916.4.
DR AlphaFoldDB; Q9LDZ5; -.
DR SMR; Q9LDZ5; -.
DR STRING; 3702.AT1G20650.1; -.
DR iPTMnet; Q9LDZ5; -.
DR PaxDb; Q9LDZ5; -.
DR PRIDE; Q9LDZ5; -.
DR ProteomicsDB; 236356; -.
DR EnsemblPlants; AT1G20650.1; AT1G20650.1; AT1G20650.
DR GeneID; 838654; -.
DR Gramene; AT1G20650.1; AT1G20650.1; AT1G20650.
DR KEGG; ath:AT1G20650; -.
DR Araport; AT1G20650; -.
DR TAIR; locus:2034344; AT1G20650.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_21_4_1; -.
DR InParanoid; Q9LDZ5; -.
DR OMA; NQEPLSW; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9LDZ5; -.
DR PRO; PR:Q9LDZ5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LDZ5; 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 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Kinase; Lipoprotein; Membrane;
KW Nucleotide-binding; Palmitate; Plant defense; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..381
FT /note="Probable serine/threonine-protein kinase PBL21"
FT /id="PRO_0000438613"
FT DOMAIN 78..354
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 362..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 204
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 84..92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9FE20"
FT CONFLICT 60
FT /note="G -> S (in Ref. 3; BAD44229)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 381 AA; 42257 MW; 384C4AE748274523 CRC64;
MTCCFSCLNP RTKDIRVDID NARCNSRYQT DSSVHGSDTT GTESISGILV NGKVNSPIPG
GGARSFTFKE LAAATRNFRE VNLLGEGGFG RVYKGRLDSG QVVAIKQLNP DGLQGNREFI
VEVLMLSLLH HPNLVTLIGY CTSGDQRLLV YEYMPMGSLE DHLFDLESNQ EPLSWNTRMK
IAVGAARGIE YLHCTANPPV IYRDLKSANI LLDKEFSPKL SDFGLAKLGP VGDRTHVSTR
VMGTYGYCAP EYAMSGKLTV KSDIYCFGVV LLELITGRKA IDLGQKQGEQ NLVTWSRPYL
KDQKKFGHLV DPSLRGKYPR RCLNYAIAII AMCLNEEAHY RPFIGDIVVA LEYLAAQSRS
HEARNVSSPS PEISRTPRRD L
