PBL7_ARATH
ID PBL7_ARATH Reviewed; 378 AA.
AC Q0WRY5; Q9LZ05;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Probable serine/threonine-protein kinase PBL7 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000269|PubMed:21855796};
DE AltName: Full=CDG1-like protein 1 {ECO:0000303|PubMed:21855796};
DE AltName: Full=PBS1-like protein 7 {ECO:0000303|PubMed:20413097};
GN Name=PBL7 {ECO:0000303|PubMed:20413097};
GN Synonyms=CDL1 {ECO:0000303|PubMed:21855796};
GN OrderedLocusNames=At5g02800 {ECO:0000312|Araport:AT5G02800};
GN ORFNames=F9G14.110 {ECO:0000312|EMBL:CAB86034.1};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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 FUNCTION, INTERACTION WITH BSU1 AND BSL1, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=21855796; DOI=10.1016/j.molcel.2011.05.037;
RA Kim T.W., Guan S., Burlingame A.L., Wang Z.Y.;
RT "The CDG1 kinase mediates brassinosteroid signal transduction from BRI1
RT receptor kinase to BSU1 phosphatase and GSK3-like kinase BIN2.";
RL Mol. Cell 43:561-571(2011).
CC -!- FUNCTION: Serine/threonine-protein kinase involved in the positive
CC regulation of brassinosteroid (BR) signaling and plant growth.
CC Phosphorylates both BSU1 and BSL1 in vitro.
CC {ECO:0000269|PubMed:21855796}.
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:0000269|PubMed:21855796};
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:0000269|PubMed:21855796};
CC -!- SUBUNIT: Interacts with BSU1 and BSL1. {ECO:0000269|PubMed:21855796}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21855796};
CC Lipid-anchor {ECO:0000250|UniProtKB:O48814}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:21855796}.
CC -!- PTM: Phosphorylated at Ser-43, Ser-46 and Ser-234.
CC {ECO:0000250|UniProtKB:Q9LSE1}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants have reduced sensitivity to BR and
CC enhanced sensitivity to BR biosynthetic inhibitor brassinazole (BRZ).
CC {ECO:0000269|PubMed:21855796}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB86034.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL162973; CAB86034.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED90519.1; -; Genomic_DNA.
DR EMBL; AK228158; BAF00114.1; -; mRNA.
DR PIR; T48301; T48301.
DR RefSeq; NP_195900.2; NM_120358.5.
DR AlphaFoldDB; Q0WRY5; -.
DR SMR; Q0WRY5; -.
DR BioGRID; 16562; 3.
DR IntAct; Q0WRY5; 1.
DR STRING; 3702.AT5G02800.1; -.
DR iPTMnet; Q0WRY5; -.
DR PaxDb; Q0WRY5; -.
DR PRIDE; Q0WRY5; -.
DR ProteomicsDB; 236708; -.
DR EnsemblPlants; AT5G02800.1; AT5G02800.1; AT5G02800.
DR GeneID; 831285; -.
DR Gramene; AT5G02800.1; AT5G02800.1; AT5G02800.
DR KEGG; ath:AT5G02800; -.
DR Araport; AT5G02800; -.
DR TAIR; locus:2151191; AT5G02800.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_21_4_1; -.
DR InParanoid; Q0WRY5; -.
DR OMA; HIVAQTF; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q0WRY5; -.
DR PRO; PR:Q0WRY5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q0WRY5; baseline and differential.
DR Genevisible; Q0WRY5; AT.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
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:0009742; P:brassinosteroid mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:1900459; P:positive regulation of brassinosteroid mediated signaling pathway; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
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; Brassinosteroid signaling pathway; Cell membrane; Kinase;
KW Lipoprotein; Membrane; Myristate; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..378
FT /note="Probable serine/threonine-protein kinase PBL7"
FT /id="PRO_0000431233"
FT DOMAIN 73..350
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 200
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 79..87
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 62
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 147
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 235
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 240
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 248
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:Q9FE20"
SQ SEQUENCE 378 AA; 41672 MW; D34A25EAFA097608 CRC64;
MGWIPCSGKS SGRNKTRRNG DHKLDRKSSD CSVSTSEKSR AKSSLSESKS KGSDHIVAQT
FTFSELATAT RNFRKECLIG EGGFGRVYKG YLASTSQTAA IKQLDHNGLQ GNREFLVEVL
MLSLLHHPNL VNLIGYCADG DQRLLVYEYM PLGSLEDHLH DISPGKQPLD WNTRMKIAAG
AAKGLEYLHD KTMPPVIYRD LKCSNILLDD DYFPKLSDFG LAKLGPVGDK SHVSTRVMGT
YGYCAPEYAM TGQLTLKSDV YSFGVVLLEI ITGRKAIDSS RSTGEQNLVA WARPLFKDRR
KFSQMADPML QGQYPPRGLY QALAVAAMCV QEQPNLRPLI ADVVTALSYL ASQKFDPLAQ
PVQGSLFAPG TPPRSKRV
