BAK1_ORYSJ
ID BAK1_ORYSJ Reviewed; 624 AA.
AC Q6Z4U4;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=LRR receptor kinase BAK1 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=BRI1-associated receptor kinase 1 homolog {ECO:0000305};
DE Short=OsBAK1 {ECO:0000303|PubMed:19754838};
DE AltName: Full=Benzothiadiazole-induced SERK1 {ECO:0000303|PubMed:17520342};
DE Short=BTH-induced SERK1 {ECO:0000305};
DE Short=OsBISERK1 {ECO:0000303|PubMed:17520342};
DE AltName: Full=Somatic embryogenesis receptor kinase 1 {ECO:0000305};
DE Short=OsSERK1 {ECO:0000303|PubMed:16081169};
DE Flags: Precursor;
GN Name=BAK1 {ECO:0000303|PubMed:19754838};
GN Synonyms=BISERK1 {ECO:0000303|PubMed:17520342};
GN OrderedLocusNames=Os08g0174700 {ECO:0000312|EMBL:BAF23022.1},
GN LOC_Os08g07760 {ECO:0000305};
GN ORFNames=OsJ_26221 {ECO:0000312|EMBL:EEE68130.1},
GN OSJNBa0054L03.30 {ECO:0000312|EMBL:BAD05545.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Nipponbare;
RX PubMed=16081169; DOI=10.1016/j.bbaexp.2005.06.007;
RA Ito Y., Takaya K., Kurata N.;
RT "Expression of SERK family receptor-like protein kinase genes in rice.";
RL Biochim. Biophys. Acta 1730:253-258(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP INDUCTION.
RX PubMed=17520342; DOI=10.1007/s11033-007-9080-8;
RA Song D., Li G., Song F., Zheng Z.;
RT "Molecular characterization and expression analysis of OsBISERK1, a gene
RT encoding a leucine-rich repeat receptor-like kinase, during disease
RT resistance responses in rice.";
RL Mol. Biol. Rep. 35:275-283(2008).
RN [8]
RP FUNCTION, INTERACTION WITH BRI1, SUBCELLULAR LOCATION, AND BIOTECHNOLOGY.
RC STRAIN=cv. Zhonghua 11;
RX PubMed=19754838; DOI=10.1111/j.1467-7652.2009.00444.x;
RA Li D., Wang L., Wang M., Xu Y.Y., Luo W., Liu Y.J., Xu Z.H., Li J.,
RA Chong K.;
RT "Engineering OsBAK1 gene as a molecular tool to improve rice architecture
RT for high yield.";
RL Plant Biotechnol. J. 7:791-806(2009).
RN [9]
RP FUNCTION.
RX PubMed=22058019; DOI=10.1007/s10059-011-0178-4;
RA Park H.S., Ryu H.Y., Kim B.H., Kim S.Y., Yoon I.S., Nam K.H.;
RT "A subset of OsSERK genes, including OsBAK1, affects normal growth and leaf
RT development of rice.";
RL Mol. Cells 32:561-569(2011).
RN [10]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH BRI1.
RX PubMed=25266270; DOI=10.1111/jipb.12290;
RA Zuo S., Zhou X., Chen M., Zhang S., Schwessinger B., Ruan D., Yuan C.,
RA Wang J., Chen X., Ronald P.C.;
RT "OsSERK1 regulates rice development but not immunity to Xanthomonas oryzae
RT pv. oryzae or Magnaporthe oryzae.";
RL J. Integr. Plant Biol. 56:1179-1192(2014).
RN [11]
RP FUNCTION, AND INTERACTION WITH BRI1 AND REM4.1.
RX PubMed=27424498; DOI=10.1016/j.devcel.2016.06.011;
RA Gui J., Zheng S., Liu C., Shen J., Li J., Li L.;
RT "OsREM4.1 interacts with OsSERK1 to coordinate the interlinking between
RT abscisic acid and brassinosteroid signaling in rice.";
RL Dev. Cell 38:201-213(2016).
CC -!- FUNCTION: LRR receptor kinase involved in defense response
CC (PubMed:22058019). Does not seem to be required specifically for XA21-
CC mediated immunity or basal resistance to Xanthomonas oryzae pv. oryzae
CC (Xoo), or immunity to Magnaporthe oryzae (PubMed:25266270). Involved in
CC brassinosteroid (BR) signaling pathway. Acts as coreceptor of BRI1.
CC Forms at the plasma membrane a receptor complex with BRI1 which is
CC activated in response to brassinolide. Phosphorylates BRI1
CC (PubMed:27424498). Required for normal plant growth and leaf
CC development (PubMed:22058019, PubMed:25266270). Possesses kinase
CC activity in vitro (PubMed:25266270). {ECO:0000269|PubMed:19754838,
CC ECO:0000269|PubMed:22058019, ECO:0000269|PubMed:25266270,
CC ECO:0000269|PubMed:27424498}.
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: Forms homodimers (PubMed:25266270). Interacts with BRI1
CC (PubMed:19754838, PubMed:25266270, PubMed:27424498). Interacts with
CC REM4.1 (PubMed:27424498). {ECO:0000269|PubMed:19754838,
CC ECO:0000269|PubMed:25266270, ECO:0000269|PubMed:27424498}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19754838};
CC Single-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in developing lateral roots, shoot apex,
CC leaf blades, lamina joints and flowers. Expressed at low levels in leaf
CC sheaths and panicles. {ECO:0000269|PubMed:16081169}.
CC -!- INDUCTION: Induced by benzothiadiazole (BTH) and infection with an
CC incompatible strain of the blast fungus Magnaporthe oryzae.
CC {ECO:0000269|PubMed:17520342}.
CC -!- BIOTECHNOLOGY: Over-expression of a truncated intracellular domain of
CC BAK1 induces partial suppression of endogenous BAK1 expression, leading
CC to an erect leaf phenotype. This could be a potential tool to improve
CC rice grain yield at high density planting.
CC {ECO:0000269|PubMed:19754838}.
CC -!- MISCELLANEOUS: Plants over-expressing BAK1 have brassinosteroid gain-
CC of-function phenotypes, including enlarged lamina joint angle, stunted
CC stature and hypersensitivity to 24-epibrassinolide (BL)
CC (PubMed:19754838). Plants silencing BAK1 show decreased sensitivity to
CC BL, are semi-dwarf, have abnormal growth patterns in leaf development,
CC increased expression level of pathogenesis-related genes and enhanced
CC susceptibility to the rice blast fungal pathogen Magnaporthe oryzae
CC (PubMed:22058019). {ECO:0000269|PubMed:19754838,
CC ECO:0000269|PubMed:22058019}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AB188247; BAD86793.1; -; mRNA.
DR EMBL; AP005164; BAD05545.1; -; Genomic_DNA.
DR EMBL; AP008214; BAF23022.1; -; Genomic_DNA.
DR EMBL; AP014964; BAT04050.1; -; Genomic_DNA.
DR EMBL; CM000145; EEE68130.1; -; Genomic_DNA.
DR EMBL; AK103038; BAG95849.1; -; mRNA.
DR RefSeq; XP_015649858.1; XM_015794372.1.
DR AlphaFoldDB; Q6Z4U4; -.
DR SMR; Q6Z4U4; -.
DR STRING; 4530.OS08T0174700-01; -.
DR iPTMnet; Q6Z4U4; -.
DR PaxDb; Q6Z4U4; -.
DR PRIDE; Q6Z4U4; -.
DR EnsemblPlants; Os08t0174700-01; Os08t0174700-01; Os08g0174700.
DR GeneID; 4344785; -.
DR Gramene; Os08t0174700-01; Os08t0174700-01; Os08g0174700.
DR KEGG; osa:4344785; -.
DR eggNOG; ENOG502QQ7B; Eukaryota.
DR HOGENOM; CLU_000288_92_7_1; -.
DR InParanoid; Q6Z4U4; -.
DR OMA; SNMEGDA; -.
DR OrthoDB; 684563at2759; -.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000007752; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
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; IMP:UniProtKB.
DR GO; GO:0009729; P:detection of brassinosteroid stimulus; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF08263; LRRNT_2; 1.
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;
KW Glycoprotein; Kinase; Leucine-rich repeat; Membrane; Nucleotide-binding;
KW Receptor; Reference proteome; Repeat; Serine/threonine-protein kinase;
KW Signal; Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..624
FT /note="LRR receptor kinase BAK1"
FT /evidence="ECO:0000255"
FT /id="PRO_5008971835"
FT TOPO_DOM 26..237
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..624
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 91..115
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 117..139
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 140..163
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 164..188
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT DOMAIN 301..588
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 205..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..227
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 428
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 307..315
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 329
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 624 AA; 68702 MW; 1FE222AE18A95077 CRC64;
MAAHRWAVWA VLLLRLLVPA ARVLANMEGD ALHSLRTNLV DPNNVLQSWD PTLVNPCTWF
HVTCNNDNSV IRVDLGNAAL SGTLVPQLGQ LKNLQYLELY SNNISGTIPS ELGNLTNLVS
LDLYLNNFTG PIPDSLGNLL KLRFLRLNNN SLSGSIPKSL TAITALQVLD LSNNNLSGEV
PSTGSFSLFT PISFANNPSL CGPGTTKPCP GAPPFSPPPP YNPPTPVQSP GSSSSTGAIA
GGVAAGAALL FAIPAIGFAW YRRRKPQEHF FDVPAEEDPE VHLGQLKRFS LRELQVATDT
FSNKNILGRG GFGKVYKGRL ADGSLVAVKR LKEERTPGGE LQFQTEVEMI SMAVHRNLLR
LRGFCMTPTE RLLVYPYMAN GSVASRLRER PPSEPPLDWR TRRRIALGSA RGLSYLHDHC
DPKIIHRDVK AANILLDEDF EAVVGDFGLA KLMDYKDTHV TTAVRGTIGH IAPEYLSTGK
SSEKTDVFGY GIMLLELITG QRAFDLARLA NDDDVMLLDW VKGLLKEKRL EMLVDPDLQS
NYIDVEVESL IQVALLCTQG SPTERPKMAE VVRMLEGDGL AERWEEWQKI EVVRQEVELG
PHRNSEWIVD STDNLHAVEL SGPR
