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Probable serine/threonine-protein kinase PBL9 (EC 2.7.11.1) (PBS1-like protein 9) (Protein kinase 1A)

 PBL9_ARATH              Reviewed;         410 AA.
Q06548; Q9LNY0;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
25-APR-2018, entry version 144.
RecName: Full=Probable serine/threonine-protein kinase PBL9 {ECO:0000305};
EC=2.7.11.1 {ECO:0000305};
AltName: Full=PBS1-like protein 9 {ECO:0000303|PubMed:20413097};
AltName: Full=Protein kinase 1A {ECO:0000305};
Name=PBL9 {ECO:0000303|PubMed:20413097};
Synonyms=APK1 {ECO:0000303|PubMed:1450380},
APK1A {ECO:0000303|PubMed:1450380},
PIX15 {ECO:0000303|PubMed:23951354}; OrderedLocusNames=At1g07570;
ORFNames=F22G5.5;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
STRAIN=cv. Columbia;
PubMed=1450380; DOI=10.1007/BF00046450;
Hirayama T., Oka A.;
"Novel protein kinase of Arabidopsis thaliana (APK1) that
phosphorylates tyrosine, serine and threonine.";
Plant Mol. Biol. 20:653-662(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
GENE FAMILY, AND NOMENCLATURE.
PubMed=20413097; DOI=10.1016/j.chom.2010.03.007;
Zhang J., Li W., Xiang T., Liu Z., Laluk K., Ding X., Zou Y., Gao M.,
Zhang X., Chen S., Mengiste T., Zhang Y., Zhou J.M.;
"Receptor-like cytoplasmic kinases integrate signaling from multiple
plant immune receptors and are targeted by a Pseudomonas syringae
effector.";
Cell Host Microbe 7:290-301(2010).
[6]
INTERACTION WITH XANTHOMONAS CAMPESTRIS XOPAC/AVRAC.
PubMed=23951354; DOI=10.1371/journal.pone.0073469;
Guy E., Lautier M., Chabannes M., Roux B., Lauber E., Arlat M.,
Noel L.D.;
"xopAC-triggered immunity against Xanthomonas depends on Arabidopsis
receptor-like cytoplasmic kinase genes PBL2 and RIPK.";
PLoS ONE 8:E73469-E73469(2013).
[7]
TISSUE SPECIFICITY.
PubMed=24828466; DOI=10.1371/journal.pone.0097161;
Elhaddad N.S., Hunt L., Sloan J., Gray J.E.;
"Light-induced stomatal opening is affected by the guard cell protein
kinase APK1b.";
PLoS ONE 9:E97161-E97161(2014).
-!- FUNCTION: Possible bi-functional kinase. In vitro, it exhibits
serine/threonine activity. In vivo, can phosphorylate tyrosine
residues of limited substrates (PubMed:1450380). May be involved
in plant defense signaling (By similarity).
{ECO:0000250|UniProtKB:O48814, ECO:0000269|PubMed:1450380}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000305}.
-!- SUBUNIT: Interacts with the Xanthomonas campestris effector
XopAC/AvrAC. {ECO:0000269|PubMed:23951354}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:O48814}; Lipid-anchor
{ECO:0000250|UniProtKB:O48814}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A number of isoforms are produced. According to EST
sequences.;
Name=1;
IsoId=Q06548-1; Sequence=Displayed;
-!- TISSUE SPECIFICITY: Expressed in stomatal guard cells of leaves.
{ECO:0000269|PubMed:24828466}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
-!- SEQUENCE CAUTION:
Sequence=AAF79545.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=PlantP kinase Classification PPC;
URL="http://plantsp.genomics.purdue.edu/family/class.html";
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; D12522; BAA02092.1; -; mRNA.
EMBL; AC022464; AAF79545.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002684; AEE28143.1; -; Genomic_DNA.
EMBL; CP002684; AEE28144.1; -; Genomic_DNA.
EMBL; CP002684; ANM58151.1; -; Genomic_DNA.
EMBL; BT004055; AAO42086.1; -; mRNA.
EMBL; BT005112; AAO50645.1; -; mRNA.
PIR; S28615; S28615.
RefSeq; NP_001320608.1; NM_001331710.1. [Q06548-1]
RefSeq; NP_172237.1; NM_100631.4. [Q06548-1]
RefSeq; NP_973778.1; NM_202049.3. [Q06548-1]
UniGene; At.348; -.
ProteinModelPortal; Q06548; -.
SMR; Q06548; -.
BioGrid; 22512; 1.
STRING; 3702.AT1G07570.3; -.
iPTMnet; Q06548; -.
PaxDb; Q06548; -.
EnsemblPlants; AT1G07570.1; AT1G07570.1; AT1G07570. [Q06548-1]
EnsemblPlants; AT1G07570.2; AT1G07570.2; AT1G07570. [Q06548-1]
EnsemblPlants; AT1G07570.5; AT1G07570.5; AT1G07570. [Q06548-1]
GeneID; 837271; -.
Gramene; AT1G07570.1; AT1G07570.1; AT1G07570. [Q06548-1]
Gramene; AT1G07570.2; AT1G07570.2; AT1G07570. [Q06548-1]
Gramene; AT1G07570.5; AT1G07570.5; AT1G07570. [Q06548-1]
KEGG; ath:AT1G07570; -.
Araport; AT1G07570; -.
eggNOG; KOG1187; Eukaryota.
eggNOG; COG0515; LUCA.
HOGENOM; HOG000116550; -.
InParanoid; Q06548; -.
PhylomeDB; Q06548; -.
BRENDA; 2.7.10.2; 399.
PRO; PR:Q06548; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q06548; baseline and differential.
Genevisible; Q06548; AT.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF07714; Pkinase_Tyr; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Cell membrane; Complete proteome;
Kinase; Lipoprotein; Membrane; Myristate; Nucleotide-binding;
Palmitate; Phosphoprotein; Plant defense; Reference proteome;
Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase.
INIT_MET 1 1 Removed. {ECO:0000305}.
CHAIN 2 410 Probable serine/threonine-protein kinase
PBL9.
/FTId=PRO_0000024302.
DOMAIN 68 352 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 74 82 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 203 203 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 106 106 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 151 151 Phosphotyrosine.
{ECO:0000250|UniProtKB:O48814}.
MOD_RES 207 207 Phosphoserine.
{ECO:0000250|UniProtKB:O48814}.
MOD_RES 237 237 Phosphoserine.
{ECO:0000250|UniProtKB:O48814}.
MOD_RES 238 238 Phosphothreonine.
{ECO:0000250|UniProtKB:O48814}.
MOD_RES 243 243 Phosphothreonine.
{ECO:0000250|UniProtKB:O48814}.
MOD_RES 251 251 Phosphotyrosine.
{ECO:0000250|UniProtKB:O48814}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000250|UniProtKB:Q9FE20}.
LIPID 4 4 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:Q9FE20}.
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


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