BAK1_ORYSI
ID BAK1_ORYSI Reviewed; 624 AA.
AC B8BB68; Q6S7F1;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 85.
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 AltName: Full=Benzothiadiazole-induced SERK1 {ECO:0000305};
DE AltName: Full=Somatic embryogenesis receptor kinase 1 {ECO:0000305};
DE Flags: Precursor;
GN Name=BAK1 {ECO:0000305};
GN Synonyms=BISERK1 {ECO:0000303|PubMed:17520342}, SERK1 {ECO:0000305};
GN ORFNames=OsI_28003 {ECO:0000312|EMBL:EEC82980.1};
OS Oryza sativa subsp. indica (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=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Yuanfengzao;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
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).
CC -!- FUNCTION: LRR receptor kinase involved in defense response. Does not
CC seem to be required specifically for XA21-mediated immunity or basal
CC resistance to Xanthomonas oryzae pv. oryzae (Xoo), or immunity to
CC Magnaporthe oryzae. Involved in brassinosteroid (BR) signaling pathway.
CC Acts as coreceptor of BRI1. Forms at the plasma membrane a receptor
CC complex with BRI1 which is activated in response to brassinolide.
CC Phosphorylates BRI1. Required for normal plant growth and leaf
CC development. Possesses kinase activity in vitro.
CC {ECO:0000250|UniProtKB:Q6Z4U4}.
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. Interacts with BRI1. Interacts with REM4.1.
CC {ECO:0000250|UniProtKB:Q6Z4U4}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6Z4U4};
CC Single-pass membrane protein {ECO:0000255}.
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; AY463361; AAR26543.1; -; mRNA.
DR EMBL; CM000133; EEC82980.1; -; Genomic_DNA.
DR AlphaFoldDB; B8BB68; -.
DR SMR; B8BB68; -.
DR STRING; 39946.B8BB68; -.
DR EnsemblPlants; BGIOSGA028076-TA; BGIOSGA028076-PA; BGIOSGA028076.
DR Gramene; BGIOSGA028076-TA; BGIOSGA028076-PA; BGIOSGA028076.
DR HOGENOM; CLU_000288_92_7_1; -.
DR OMA; SNMEGDA; -.
DR PlantReactome; R-OSA-5632095; Brassinosteroid signaling.
DR PlantReactome; R-OSA-9035605; Regulation of seed size.
DR Proteomes; UP000007015; Chromosome 8.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:EnsemblPlants.
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; IEA:EnsemblPlants.
DR GO; GO:0009729; P:detection of brassinosteroid stimulus; IEA:EnsemblPlants.
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 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Glycoprotein; Kinase; Leucine-rich repeat;
KW Membrane; Nucleotide-binding; Receptor; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW 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_5002868727"
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"
FT CONFLICT 4
FT /note="P -> H (in Ref. 1; AAR26543)"
FT /evidence="ECO:0000305"
FT CONFLICT 182..185
FT /note="STGS -> YKHG (in Ref. 1; AAR26543)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 624 AA; 68662 MW; 0254FE9E088D09CA CRC64;
MAAPRWAVWA 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
