(data stored in ACNUC13479 zone)

SWISSPROT: PBL8_ARATH

ID   PBL8_ARATH              Reviewed;         410 AA.
AC   Q8GXZ3; Q9LFD4;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   30-AUG-2017, entry version 108.
DE   RecName: Full=Probable serine/threonine-protein kinase PBL8 {ECO:0000305};
DE            EC=2.7.11.1 {ECO:0000305};
DE   AltName: Full=PBS1-like protein 8 {ECO:0000303|PubMed:20413097};
GN   Name=PBL8 {ECO:0000303|PubMed:20413097};
GN   Synonyms=PIX17 {ECO:0000303|PubMed:23951354};
GN   OrderedLocusNames=At5g01020; ORFNames=F7J8.5;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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.,
RA   Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
RA   Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
RA   Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
RA   Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
RA   Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
RA   Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
RA   Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
RA   Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
RA   Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
RA   Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
RA   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.,
RA   Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
RA   Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
RA   van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
RA   Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
RA   Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
RA   Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:823-826(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Portal (Araport);
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M.,
RA   Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T.,
RA   Shibata K., Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
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
RT   plant immune receptors and are targeted by a Pseudomonas syringae
RT   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.,
RA   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).
CC   -!- FUNCTION: May be involved in plant defense signaling.
CC       {ECO:0000250|UniProtKB:O48814}.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC       {ECO:0000305}.
CC   -!- SUBUNIT: Interacts with the Xanthomonas campestris effector
CC       XopAC/AvrAC. {ECO:0000269|PubMed:23951354}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000250|UniProtKB:O48814}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:O48814}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC       protein kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB99493.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=PlantP kinase Classification PPC;
CC       URL="http://plantsp.genomics.purdue.edu/family/class.html";
DR   EMBL; AL137189; CAB99493.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED90288.1; -; Genomic_DNA.
DR   EMBL; AK117952; BAC42590.1; -; mRNA.
DR   RefSeq; NP_195722.2; NM_120179.3.
DR   UniGene; At.22644; -.
DR   ProteinModelPortal; Q8GXZ3; -.
DR   SMR; Q8GXZ3; -.
DR   STRING; 3702.AT5G01020.1; -.
DR   iPTMnet; Q8GXZ3; -.
DR   PaxDb; Q8GXZ3; -.
DR   PRIDE; Q8GXZ3; -.
DR   EnsemblPlants; AT5G01020.1; AT5G01020.1; AT5G01020.
DR   GeneID; 831918; -.
DR   Gramene; AT5G01020.1; AT5G01020.1; AT5G01020.
DR   KEGG; ath:AT5G01020; -.
DR   Araport; AT5G01020; -.
DR   TAIR; locus:2150019; AT5G01020.
DR   eggNOG; KOG1187; Eukaryota.
DR   eggNOG; COG0515; LUCA.
DR   HOGENOM; HOG000116550; -.
DR   InParanoid; Q8GXZ3; -.
DR   OMA; WCTRIRI; -.
DR   OrthoDB; EOG09360B87; -.
DR   PhylomeDB; Q8GXZ3; -.
DR   PRO; PR:Q8GXZ3; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   Genevisible; Q8GXZ3; AT.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR   InterPro; IPR011009; Kinase-like_dom.
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; Pkinase_Tyr; 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;
DR   PRODOM; Q8GXZ3.
DR   SWISS-2DPAGE; Q8GXZ3.
KW   ATP-binding; Cell membrane; Complete proteome; Kinase; Lipoprotein;
KW   Membrane; Myristate; Nucleotide-binding; Palmitate; Phosphoprotein;
KW   Plant defense; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase.
FT   INIT_MET      1      1       Removed. {ECO:0000305}.
FT   CHAIN         2    410       Probable serine/threonine-protein kinase
FT                                PBL8.
FT                                /FTId=PRO_0000403345.
FT   DOMAIN       69    350       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND      75     83       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   ACT_SITE    199    199       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   BINDING     104    104       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   MOD_RES     149    149       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:O48814}.
FT   MOD_RES     203    203       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O48814}.
FT   MOD_RES     233    233       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O48814}.
FT   MOD_RES     234    234       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:O48814}.
FT   MOD_RES     239    239       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:O48814}.
FT   MOD_RES     247    247       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:O48814}.
FT   LIPID         2      2       N-myristoyl glycine.
FT                                {ECO:0000250|UniProtKB:Q9FE20}.
FT   LIPID         4      4       S-palmitoyl cysteine.
FT                                {ECO:0000250|UniProtKB:Q9FE20}.
SQ   SEQUENCE   410 AA;  45618 MW;  74895DE9AD283742 CRC64;
     MGNCGTRDEA AVFTPQAQAQ QLQKKHSRSV SDLSDPSTPR FRDDSRTPIS YAQVIPFTLF
     ELETITKSFR PDYILGEGGF GTVYKGYIDD NLRVGLKSLP VAVKVLNKEG LQGHREWLTE
     VNFLGQLRHP NLVKLIGYCC EDDHRLLVYE FMLRGSLENH LFRKTTAPLS WSRRMMIALG
     AAKGLAFLHN AERPVIYRDF KTSNILLDSD YTAKLSDFGL AKAGPQGDET HVSTRVMGTY
     GYAAPEYVMT GHLTARSDVY SFGVVLLEML TGRKSVDKTR PSKEQNLVDW ARPKLNDKRK
     LLQIIDPRLE NQYSVRAAQK ACSLAYYCLS QNPKARPLMS DVVETLEPLQ CTGDALIPCA
     TTTAGAAFAM GGVPDYRMHR RFAKNVGPGA ICRSPNPNYS PGGPAACRVR
//

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