BRL2_ORYSJ
ID BRL2_ORYSJ Reviewed; 1110 AA.
AC Q7G768; Q0IZA4; Q94LN2;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Brassinosteroid LRR receptor kinase BRL2 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=BRI1-like receptor kinase 2 {ECO:0000305};
DE Flags: Precursor;
GN Name=BRL2 {ECO:0000305};
GN OrderedLocusNames=Os10g0114400 {ECO:0000312|EMBL:BAT09653.1},
GN LOC_Os10g02500 {ECO:0000312|EMBL:AAP51860.1};
GN ORFNames=OJ1014H12.3 {ECO:0000312|EMBL:AAM44864.1},
GN OsJ_34509 {ECO:0000312|EMBL:EAZ18974.1},
GN OSJNBa0092N12.12 {ECO:0000312|EMBL:AAK52544.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12791992; DOI=10.1126/science.1083523;
RA Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S.,
RA Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D.,
RA Oates R., Palmer M., Pries G., Gibson J., Anderson H., Paradkar M.,
RA Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F.,
RA Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M.,
RA Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R.,
RA Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F.,
RA Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D.,
RA Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R.,
RA Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S.,
RA Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S.,
RA Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R.,
RA Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M.,
RA Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R.,
RA Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E.,
RA Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.;
RT "In-depth view of structure, activity, and evolution of rice chromosome
RT 10.";
RL Science 300:1566-1569(2003).
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;
RG The rice full-length cDNA consortium;
RT "Oryza sativa full length cDNA.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be involved in brassenosteroid (BR) perception.
CC {ECO:0000250|UniProtKB:Q942F3}.
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- DOMAIN: Contains two pairs of conservatively spaced Cys (Cys pair 1 and
CC 2) possibly involved in forming some heterodimers.
CC {ECO:0000250|UniProtKB:O22476}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF25961.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC078891; AAK52544.1; -; Genomic_DNA.
DR EMBL; AC098694; AAM44864.1; -; Genomic_DNA.
DR EMBL; DP000086; AAP51860.1; -; Genomic_DNA.
DR EMBL; AP008216; BAF25961.2; ALT_INIT; Genomic_DNA.
DR EMBL; AP014966; BAT09653.1; -; Genomic_DNA.
DR EMBL; CM000148; EAZ18974.1; -; Genomic_DNA.
DR EMBL; AK243167; BAH01473.1; -; mRNA.
DR RefSeq; XP_015615048.1; XM_015759562.1.
DR AlphaFoldDB; Q7G768; -.
DR SMR; Q7G768; -.
DR STRING; 4530.OS10T0114400-01; -.
DR PaxDb; Q7G768; -.
DR PRIDE; Q7G768; -.
DR EnsemblPlants; Os10t0114400-01; Os10t0114400-01; Os10g0114400.
DR GeneID; 4347982; -.
DR Gramene; Os10t0114400-01; Os10t0114400-01; Os10g0114400.
DR KEGG; osa:4347982; -.
DR eggNOG; ENOG502QS1K; Eukaryota.
DR HOGENOM; CLU_000288_22_4_1; -.
DR InParanoid; Q7G768; -.
DR OMA; CTGLEWV; -.
DR OrthoDB; 684563at2759; -.
DR Proteomes; UP000000763; Chromosome 10.
DR Proteomes; UP000007752; Chromosome 11.
DR Proteomes; UP000059680; Chromosome 10.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:UniProtKB-KW.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR045381; BRI1_island_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
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; PF20141; Island; 1.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 8.
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; 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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1110
FT /note="Brassinosteroid LRR receptor kinase BRL2"
FT /evidence="ECO:0000255"
FT /id="PRO_5008972304"
FT TRANSMEM 741..761
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 87..110
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 112..136
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 137..161
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 163..183
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 184..207
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 209..231
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 232..255
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 257..281
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 283..305
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 306..330
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 332..354
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 356..379
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 381..403
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 405..427
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 428..451
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 453..474
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 475..499
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 501..523
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 591..615
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 616..639
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT REPEAT 641..662
FT /note="LRR 21"
FT /evidence="ECO:0000255"
FT REPEAT 663..688
FT /note="LRR 22"
FT /evidence="ECO:0000255"
FT DOMAIN 824..1101
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOTIF 52..59
FT /note="Cys pair 1"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOTIF 701..708
FT /note="Cys pair 2"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT ACT_SITE 952
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 580
FT /ligand="brassinolide"
FT /ligand_id="ChEBI:CHEBI:28277"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT BINDING 830..838
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 852
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 898..900
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT BINDING 904..907
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT BINDING 952..957
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT BINDING 970
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 139
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 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 450
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 485
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 498
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 627
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 662
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 675
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1110 AA; 118110 MW; B6723380BC0A8E9A CRC64;
MDILIPLLLS SIYVSSSAAA AETDAAALLR FKAFVHKDPR GVLSSWVDPG PCRWRGVTCN
GDGRVTELDL AAGGLAGRAE LAALSGLDTL CRLNLSGNGE LHVDAGDLVK LPRALLQLDL
SDGGLAGRLP DGFLACYPNL TDVSLARNNL TGELPGMLLA SNIRSFDVSG NNMSGDISGV
SLPATLAVLD LSGNRFTGAI PPSLSGCAGL TTLNLSYNGL AGAIPEGIGA IAGLEVLDVS
WNHLTGAIPP GLGRNACASL RVLRVSSNNI SGSIPESLSS CHALRLLDVA NNNVSGGIPA
AVLGNLTAVE SLLLSNNFIS GSLPDTIAHC KNLRVADLSS NKISGALPAE LCSPGAALEE
LRLPDNLVAG TIPPGLSNCS RLRVIDFSIN YLRGPIPPEL GRLRALEKLV MWFNGLDGRI
PADLGQCRNL RTLILNNNFI GGDIPVELFN CTGLEWVSLT SNQITGTIRP EFGRLSRLAV
LQLANNSLAG EIPRELGNCS SLMWLDLNSN RLTGEIPRRL GRQLGSTPLS GILSGNTLAF
VRNVGNSCKG VGGLLEFAGI RPERLLQVPT LKSCDFTRLY SGAAVSGWTR YQTLEYLDLS
YNSLDGEIPE ELGDMVVLQV LDLARNNLTG EIPASLGRLR NLGVFDVSRN RLQGGIPDSF
SNLSFLVQID ISDNNLSGEI PQRGQLSTLP ASQYAGNPGL CGMPLEPCGD RLPTATMSGL
AAAASTDPPP RRAVATWANG VILAVLVSAG LACAAAIWAV AARARRREVR SAMMLSSLQD
GTRTATTWKL GKAEKEALSI NVATFQRQLR KLTFTQLIEA TNGFSTASLI GSGGFGEVFK
ATLKDGSCVA IKKLIHLSYQ GDREFMAEME TLGKIKHKNL VPLLGYCKIG EERLLVYEFM
SHGSLEDTLH GDGGRSASPA MSWEQRKKVA RGAARGLCFL HYNCIPHIIH RDMKSSNVLL
DGDMEARVAD FGMARLISAL DTHLSVSTLA GTPGYVPPEY YQSFRCTVKG DVYSFGVVLL
ELLTGRRPTD KDDFGDTNLV GWVKMKVGDG AGKEVLDPEL VVEGADADEM ARFMDMALQC
VDDFPSKRPN MLQVVAMLRE LDAPPPATAI
