PBL9_ARATH
ID PBL9_ARATH Reviewed; 410 AA.
AC Q06548; Q9LNY0;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Probable serine/threonine-protein kinase PBL9 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=PBS1-like protein 9 {ECO:0000303|PubMed:20413097};
DE AltName: Full=Protein kinase 1A {ECO:0000305};
GN Name=PBL9 {ECO:0000303|PubMed:20413097};
GN Synonyms=APK1 {ECO:0000303|PubMed:1450380},
GN APK1A {ECO:0000303|PubMed:1450380}, PIX15 {ECO:0000303|PubMed:23951354};
GN OrderedLocusNames=At1g07570; ORFNames=F22G5.5;
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 [MRNA], AND FUNCTION.
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 [2]
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 [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].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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).
RN [6]
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 [7]
RP TISSUE SPECIFICITY.
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 (PubMed:1450380). May be involved in plant
CC defense signaling (By similarity). {ECO:0000250|UniProtKB:O48814,
CC ECO:0000269|PubMed:1450380}.
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=Q06548-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in stomatal guard cells of leaves.
CC {ECO:0000269|PubMed:24828466}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79545.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; D12522; BAA02092.1; -; mRNA.
DR EMBL; AC022464; AAF79545.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28143.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28144.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58151.1; -; Genomic_DNA.
DR EMBL; BT004055; AAO42086.1; -; mRNA.
DR EMBL; BT005112; AAO50645.1; -; mRNA.
DR PIR; S28615; S28615.
DR RefSeq; NP_001320608.1; NM_001331710.1. [Q06548-1]
DR RefSeq; NP_172237.1; NM_100631.4. [Q06548-1]
DR RefSeq; NP_973778.1; NM_202049.3. [Q06548-1]
DR AlphaFoldDB; Q06548; -.
DR SMR; Q06548; -.
DR BioGRID; 22512; 2.
DR STRING; 3702.AT1G07570.3; -.
DR iPTMnet; Q06548; -.
DR PaxDb; Q06548; -.
DR PRIDE; Q06548; -.
DR EnsemblPlants; AT1G07570.1; AT1G07570.1; AT1G07570. [Q06548-1]
DR EnsemblPlants; AT1G07570.2; AT1G07570.2; AT1G07570. [Q06548-1]
DR EnsemblPlants; AT1G07570.5; AT1G07570.5; AT1G07570. [Q06548-1]
DR GeneID; 837271; -.
DR Gramene; AT1G07570.1; AT1G07570.1; AT1G07570. [Q06548-1]
DR Gramene; AT1G07570.2; AT1G07570.2; AT1G07570. [Q06548-1]
DR Gramene; AT1G07570.5; AT1G07570.5; AT1G07570. [Q06548-1]
DR KEGG; ath:AT1G07570; -.
DR Araport; AT1G07570; -.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_21_13_1; -.
DR InParanoid; Q06548; -.
DR OMA; CITLAIC; -.
DR PhylomeDB; Q06548; -.
DR BRENDA; 2.7.10.2; 399.
DR PRO; PR:Q06548; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q06548; baseline and differential.
DR Genevisible; Q06548; 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 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; Tyrosine-protein kinase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..410
FT /note="Probable serine/threonine-protein kinase PBL9"
FT /id="PRO_0000024302"
FT DOMAIN 68..352
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 11..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 203
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 74..82
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 MOD_RES 151
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 238
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 243
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 251
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 410 AA; 45519 MW; 5BAB28D9E0065082 CRC64;
MGICLSAQVK AESSGASTKY DAKDIGSLGS KASSVSVRPS PRTEGEILQS PNLKSFSFAE
LKSATRNFRP DSVLGEGGFG CVFKGWIDEK SLTASRPGTG LVIAVKKLNQ DGWQGHQEWL
AEVNYLGQFS HRHLVKLIGY CLEDEHRLLV YEFMPRGSLE NHLFRRGLYF QPLSWKLRLK
VALGAAKGLA FLHSSETRVI YRDFKTSNIL LDSEYNAKLS DFGLAKDGPI GDKSHVSTRV
MGTHGYAAPE YLATGHLTTK SDVYSFGVVL LELLSGRRAV DKNRPSGERN LVEWAKPYLV
NKRKIFRVID NRLQDQYSME EACKVATLSL RCLTTEIKLR PNMSEVVSHL EHIQSLNAAI
GGNMDKTDRR MRRRSDSVVS KKVNAGFARQ TAVGSTVVAY PRPSASPLYV
