ID   BIK1_ARATH              Reviewed;         395 AA.
AC   O48814;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   07-JUL-2009, entry version 77.
DE   RecName: Full=Serine/threonine-protein kinase BIK1;
DE            EC=2.7.11.1;
DE   AltName: Full=Protein BOTRYTIS-INDUCED KINASE 1;
GN   Name=BIK1; OrderedLocusNames=At2g39660; ORFNames=F17A14.3, F12L6.32;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=20083487; PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
RA   Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
RA   Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
RA   Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
RA   Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
RA   Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=16339855; DOI=10.1105/tpc.105.035576;
RA   Veronese P., Nakagami H., Bluhm B., AbuQamar S., Chen X., Salmeron J.,
RA   Dietrich R.A., Hirt H., Mengiste T.;
RT   "The membrane-anchored BOTRYTIS-INDUCED KINASE1 plays distinct roles
RT   in Arabidopsis resistance to necrotrophic and biotrophic pathogens.";
RL   Plant Cell 18:257-273(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, AND MASS
RP   SPECTROMETRY.
RX   PubMed=17317660; DOI=10.1074/mcp.M600429-MCP200;
RA   Benschop J.J., Mohammed S., O'Flaherty M., Heck A.J.R., Slijper M.,
RA   Menke F.L.H.;
RT   "Quantitative phosphoproteomics of early elicitor signaling in
RT   Arabidopsis.";
RL   Mol. Cell. Proteomics 6:1198-1214(2007).
CC   -!- FUNCTION: Required to activate the resistance responses to
CC       necrotrophic pathogens.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- INTERACTION:
CC       P62157:CALM (xeno); NbExp=1; IntAct=EBI-1238176, EBI-397403;
CC       O23320:CML8; NbExp=1; IntAct=EBI-1238176, EBI-1237764;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor.
CC   -!- INDUCTION: By infection with necrotrophic pathogens and by
CC       paraquat. Not induced by salicylic acid, jasmonate or 1-
CC       aminocyclopropane-1-carboxylate (ACC).
CC   -!- PTM: Phosphorylation level varies significantly during early
CC       response to general elicitors.
CC   -!- DISRUPTION PHENOTYPE: Plants show some altered growth traits and a
CC       severely impaired resistance to Botrytis and A.brassicicola.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC       protein kinase family.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; AC003674; AAB97121.1; -; Genomic_DNA.
DR   EMBL; AC004218; AAM14921.1; -; Genomic_DNA.
DR   EMBL; AF325086; AAK17154.1; -; mRNA.
DR   EMBL; AY062493; AAL32571.1; -; mRNA.
DR   EMBL; AY065029; AAL57667.1; -; mRNA.
DR   EMBL; AY093278; AAM13277.1; -; mRNA.
DR   EMBL; AY093997; AAM16258.1; -; mRNA.
DR   IPI; IPI00518414; -.
DR   PIR; T00574; T00574.
DR   RefSeq; NP_181496.1; -.
DR   UniGene; At.21254; -.
DR   HSSP; P08631; 2HCK.
DR   IntAct; O48814; 2.
DR   PRIDE; O48814; -.
DR   GeneID; 818549; -.
DR   GenomeReviews; CT485783_GR; AT2G39660.
DR   KEGG; ath:AT2G39660; -.
DR   NMPDR; fig|3702.1.peg.11080; -.
DR   GeneFarm; 1713; 129.
DR   TAIR; At2g39660; -.
DR   BRENDA; 2.7.11.1; 302.
DR   ArrayExpress; O48814; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR   GO; GO:0005730; C:nucleolus; IDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR   GO; GO:0046777; P:protein amino acid autophosphorylation; IDA:TAIR.
DR   InterPro; IPR000719; Prot_kinase_core.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_pkinase-rel.
DR   InterPro; IPR008271; Ser_thr_pkin_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   ProDom; PD000001; Prot_kinase; 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; Complete proteome; Kinase; Lipoprotein;
KW   Membrane; Myristate; Nucleotide-binding; Palmitate; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   INIT_MET      1      1       Removed (Potential).
FT   CHAIN         2    395       Serine/threonine-protein kinase BIK1.
FT                                /FTId=PRO_0000311118.
FT   DOMAIN       67    356       Protein kinase.
FT   NP_BIND      73     81       ATP (By similarity).
FT   ACT_SITE    202    202       Proton acceptor (By similarity).
FT   BINDING     105    105       ATP (By similarity).
FT   MOD_RES      28     28       Phosphoserine.
FT   LIPID         2      2       N-myristoyl glycine (Potential).
FT   LIPID         4      4       S-palmitoyl cysteine (Potential).
SQ   SEQUENCE   395 AA;  44097 MW;  4C06B1FD01889440 CRC64;
     MGSCFSSRVK ADIFHNGKSS DLYGLSLSSR KSSSTVAAAQ KTEGEILSST PVKSFTFNEL
     KLATRNFRPD SVIGEGGFGC VFKGWLDEST LTPTKPGTGL VIAVKKLNQE GFQGHREWLT
     EINYLGQLSH PNLVKLIGYC LEDEHRLLVY EFMQKGSLEN HLFRRGAYFK PLPWFLRVNV
     ALDAAKGLAF LHSDPVKVIY RDIKASNILL DADYNAKLSD FGLARDGPMG DLSYVSTRVM
     GTYGYAAPEY MSSGHLNARS DVYSFGVLLL EILSGKRALD HNRPAKEENL VDWARPYLTS
     KRKVLLIVDN RLDTQYLPEE AVRMASVAVQ CLSFEPKSRP TMDQVVRALQ QLQDNLGKPS
     QTNPVKDTKK LGFKTGTTKS SEKRFTQKPF GRHLV
//