BRI1_ORYSJ
ID BRI1_ORYSJ Reviewed; 1121 AA.
AC Q942F3;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Brassinosteroid LRR receptor kinase BRI1 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=Protein BRASSINOSTEROID INSENSITIVE 1 homolog {ECO:0000303|PubMed:11006334};
DE Short=OsBRI1 {ECO:0000303|PubMed:11006334};
DE AltName: Full=Protein DWARF 61 {ECO:0000303|PubMed:11006334};
DE Flags: Precursor;
GN Name=BRI1 {ECO:0000303|PubMed:11006334};
GN Synonyms=D61 {ECO:0000303|PubMed:11006334};
GN OrderedLocusNames=Os01g0718300 {ECO:0000312|EMBL:BAF05991.1},
GN LOC_Os01g52050 {ECO:0000305};
GN ORFNames=P0480C01.18-1 {ECO:0000312|EMBL:BAB68053.1};
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=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
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 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 [6]
RP FUNCTION, MUTAGENESIS OF VAL-491 AND THR-989, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Taichung 65;
RX PubMed=11006334; DOI=10.2307/3871176;
RA Yamamuro C., Ihara Y., Wu X., Noguchi T., Fujioka S., Takatsuto S.,
RA Ashikari M., Kitano H., Matsuoka M.;
RT "Loss of function of a rice brassinosteroid insensitive1 homolog prevents
RT internode elongation and bending of the lamina joint.";
RL Plant Cell 12:1591-1606(2000).
RN [7]
RP INTERACTION WITH BIP103 AND BIP131, AND INDUCTION.
RX DOI=10.5511/plantbiotechnology.21.35;
RA Hirabayashi S., Matsushita Y., Sato M., Ohi R., Kasahara M., Abe H.,
RA Nyunoya H.;
RT "Two proton pump interactors identified from a direct phosphorylation
RT screening of a rice cDNA library by using a recombinant BRI1 receptor
RT kinase.";
RL Plant Biotechnol. 21:35-45(2004).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF HIS-420; ASN-426; ALA-467;
RP GLY-522; GLY-539 AND THR-854.
RX PubMed=16407447; DOI=10.1104/pp.105.072330;
RA Nakamura A., Fujioka S., Sunohara H., Kamiya N., Hong Z., Inukai Y.,
RA Miura K., Takatsuto S., Yoshida S., Ueguchi-Tanaka M., Hasegawa Y.,
RA Kitano H., Matsuoka M.;
RT "The role of OsBRI1 and its homologous genes, OsBRL1 and OsBRL3, in rice.";
RL Plant Physiol. 140:580-590(2006).
RN [9]
RP BIOTECHNOLOGY.
RX PubMed=16714407; DOI=10.1104/pp.106.077081;
RA Morinaka Y., Sakamoto T., Inukai Y., Agetsuma M., Kitano H., Ashikari M.,
RA Matsuoka M.;
RT "Morphological alteration caused by brassinosteroid insensitivity increases
RT the biomass and grain production of rice.";
RL Plant Physiol. 141:924-931(2006).
RN [10]
RP INTERACTION WITH BAK1 AND SERK2.
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 [11]
RP INTERACTION WITH SERK2.
RX PubMed=24482436; DOI=10.1093/mp/ssu003;
RA Chen X., Zuo S., Schwessinger B., Chern M., Canlas P.E., Ruan D., Zhou X.,
RA Wang J., Daudi A., Petzold C.J., Heazlewood J.L., Ronald P.C.;
RT "An XA21-associated kinase (OsSERK2) regulates immunity mediated by the
RT XA21 and XA3 immune receptors.";
RL Mol. Plant 7:874-892(2014).
RN [12]
RP FUNCTION, AND INTERACTION WITH BAK1.
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).
RN [13]
RP FUNCTION, AND INTERACTION WITH BSK3.
RX PubMed=26697897; DOI=10.1104/pp.15.01668;
RA Zhang B., Wang X., Zhao Z., Wang R., Huang X., Zhu Y., Yuan L., Wang Y.,
RA Xu X., Burlingame A.L., Gao Y., Sun Y., Tang W.;
RT "OsBRI1 activates BR signaling by preventing binding between the TPR and
RT kinase domains of OsBSK3 via phosphorylation.";
RL Plant Physiol. 170:1149-1161(2016).
CC -!- FUNCTION: Receptor kinase involved brassinosteroid (BR) signal
CC transduction. Regulates, in response to BR binding, a signaling cascade
CC involved in plant development, promotion of cell elongation and
CC flowering (Probable). Activates BR signaling by targeting and
CC phosphorylating BSK3, a positive regulator of BR signaling
CC (PubMed:26697897). Forms at the plasma membrane a receptor complex with
CC BAK1 which is activated in response to brassinolide. Phosphorylates
CC BAK1. Phosphorylates REM4.1, which reduces REM4.1 binding affinity to
CC BAK1 and allows the formation and subsequent activation of the BRI1-
CC BAK1 receptor complex (PubMed:27424498). Functions in various growth
CC and developmental processes, such as internode elongation, bending of
CC the lamina joint and skotomorphogenesis. Functions in internode
CC elongation by inducing the formation of the intercalary meristem and
CC the longitudinal elongation of internode cells (PubMed:11006334).
CC Involved in organ development through the control of cell division and
CC elongation. Does not seem essential for organ pattern formation or
CC organ initiation (PubMed:16407447). {ECO:0000269|PubMed:11006334,
CC ECO:0000269|PubMed:16407447, ECO:0000269|PubMed:26697897,
CC ECO:0000269|PubMed:27424498, ECO:0000305|PubMed:11006334,
CC ECO:0000305|PubMed:16407447}.
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: Interacts with BIP103 and BIP131 (Ref.7). Interacts with BAK1
CC (PubMed:19754838, PubMed:27424498). Interacts with BSK3
CC (PubMed:26697897). Interacts with SERK2 (PubMed:19754838,
CC PubMed:24482436). {ECO:0000269|PubMed:19754838,
CC ECO:0000269|PubMed:24482436, ECO:0000269|PubMed:26697897,
CC ECO:0000269|PubMed:27424498, ECO:0000269|Ref.7}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in shoots. Expressed at low levels
CC in roots. {ECO:0000269|PubMed:16407447}.
CC -!- INDUCTION: Down-regulated by brassinolide. {ECO:0000269|Ref.7}.
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 -!- DISRUPTION PHENOTYPE: Dwarf plants due to the lack of internode
CC elongation. Insensitivity to brassinolide.
CC {ECO:0000269|PubMed:11006334}.
CC -!- BIOTECHNOLOGY: Over-expression of a truncated form of BRI1 induces
CC partial suppression of endogenous BRI1 expression, leading to an erect
CC leaf phenotype. The estimated grain yield of the transformants is about
CC 30 per cent higher than that of wild type at high density planting.
CC {ECO:0000269|PubMed:16714407}.
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; AP003453; BAB68053.1; -; Genomic_DNA.
DR EMBL; AP008207; BAF05991.1; -; Genomic_DNA.
DR EMBL; AP014957; BAS74050.1; -; Genomic_DNA.
DR EMBL; AK073838; BAG93669.1; -; mRNA.
DR RefSeq; XP_015621030.1; XM_015765544.1.
DR AlphaFoldDB; Q942F3; -.
DR SMR; Q942F3; -.
DR STRING; 4530.OS01T0718300-01; -.
DR PaxDb; Q942F3; -.
DR PRIDE; Q942F3; -.
DR EnsemblPlants; Os01t0718300-01; Os01t0718300-01; Os01g0718300.
DR EnsemblPlants; Os01t0718300-02; Os01t0718300-02; Os01g0718300.
DR GeneID; 4324691; -.
DR Gramene; Os01t0718300-01; Os01t0718300-01; Os01g0718300.
DR Gramene; Os01t0718300-02; Os01t0718300-02; Os01g0718300.
DR KEGG; osa:4324691; -.
DR eggNOG; ENOG502QRF2; Eukaryota.
DR HOGENOM; CLU_000288_22_4_1; -.
DR InParanoid; Q942F3; -.
DR OMA; GWVKLHA; -.
DR OrthoDB; 151283at2759; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR ExpressionAtlas; Q942F3; baseline and differential.
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; IBA:GO_Central.
DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IMP:Gramene.
DR GO; GO:0009729; P:detection of brassinosteroid stimulus; IMP:Gramene.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0001578; P:microtubule bundle formation; IMP:Gramene.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0009647; P:skotomorphogenesis; IMP:Gramene.
DR Gene3D; 3.80.10.10; -; 1.
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; 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; PF13855; LRR_8; 4.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 5.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 17.
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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1121
FT /note="Brassinosteroid LRR receptor kinase BRI1"
FT /evidence="ECO:0000255"
FT /id="PRO_5008973918"
FT TRANSMEM 719..739
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 90..114
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 116..142
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 144..167
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 170..193
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 197..221
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 223..243
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 244..268
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 269..292
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 294..317
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 318..341
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 343..367
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 369..391
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 392..415
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 416..439
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 441..463
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 464..487
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 489..511
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 541..564
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 580..603
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 604..628
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT REPEAT 629..651
FT /note="LRR 21"
FT /evidence="ECO:0000255"
FT REPEAT 652..676
FT /note="LRR 22"
FT /evidence="ECO:0000255"
FT DOMAIN 807..1083
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 693..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 54..61
FT /note="Cys pair 1"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOTIF 689..696
FT /note="Cys pair 2"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT ACT_SITE 933
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 525
FT /ligand="brassinolide"
FT /ligand_id="ChEBI:CHEBI:28277"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT BINDING 569
FT /ligand="brassinolide"
FT /ligand_id="ChEBI:CHEBI:28277"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT BINDING 813..821
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 835
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 881..883
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT BINDING 887..890
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT BINDING 933..938
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT BINDING 951
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 501
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 564
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 580
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 658
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 665
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 684
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 420
FT /note="H->P: In d61-3; severe dwarf phenotype. Sterile
FT plants."
FT /evidence="ECO:0000269|PubMed:16407447"
FT MUTAGEN 426
FT /note="N->Y: In d61-5; severe dwarf phenotype. Sterile
FT plants."
FT /evidence="ECO:0000269|PubMed:16407447"
FT MUTAGEN 467
FT /note="A->V: In d61-7; mild dwarf phenotype. Fertile
FT plants."
FT /evidence="ECO:0000269|PubMed:16407447"
FT MUTAGEN 491
FT /note="V->M: In d61-2; mild dwarf phenotype. Fertile
FT plants. Insensitivity to brassinolide."
FT /evidence="ECO:0000269|PubMed:11006334"
FT MUTAGEN 522
FT /note="G->E: In d61-8; mild dwarf phenotype. Fertile
FT plants."
FT /evidence="ECO:0000269|PubMed:16407447"
FT MUTAGEN 539
FT /note="G->D: In d61-9; mild dwarf phenotype. Fertile
FT plants."
FT /evidence="ECO:0000269|PubMed:16407447"
FT MUTAGEN 854
FT /note="T->I: In d61-10; mild dwarf phenotype. Fertile
FT plants."
FT /evidence="ECO:0000269|PubMed:16407447"
FT MUTAGEN 989
FT /note="T->I: In d61-1; intermediate dwarf phenotype.
FT Fertile plants. Insensitivity to brassinolide."
FT /evidence="ECO:0000269|PubMed:11006334"
SQ SEQUENCE 1121 AA; 120181 MW; F71A49B45E0E2D09 CRC64;
MDSLWAAIAA LFVAAAVVVR GAAAADDAQL LEEFRQAVPN QAALKGWSGG DGACRFPGAG
CRNGRLTSLS LAGVPLNAEF RAVAATLLQL GSVEVLSLRG ANVSGALSAA GGARCGSKLQ
ALDLSGNAAL RGSVADVAAL ASACGGLKTL NLSGDAVGAA KVGGGGGPGF AGLDSLDLSN
NKITDDSDLR WMVDAGVGAV RWLDLALNRI SGVPEFTNCS GLQYLDLSGN LIVGEVPGGA
LSDCRGLKVL NLSFNHLAGV FPPDIAGLTS LNALNLSNNN FSGELPGEAF AKLQQLTALS
LSFNHFNGSI PDTVASLPEL QQLDLSSNTF SGTIPSSLCQ DPNSKLHLLY LQNNYLTGGI
PDAVSNCTSL VSLDLSLNYI NGSIPASLGD LGNLQDLILW QNELEGEIPA SLSRIQGLEH
LILDYNGLTG SIPPELAKCT KLNWISLASN RLSGPIPSWL GKLSYLAILK LSNNSFSGPI
PPELGDCQSL VWLDLNSNQL NGSIPKELAK QSGKMNVGLI VGRPYVYLRN DELSSECRGK
GSLLEFTSIR PDDLSRMPSK KLCNFTRMYV GSTEYTFNKN GSMIFLDLSY NQLDSAIPGE
LGDMFYLMIM NLGHNLLSGT IPSRLAEAKK LAVLDLSYNQ LEGPIPNSFS ALSLSEINLS
NNQLNGTIPE LGSLATFPKS QYENNTGLCG FPLPPCDHSS PRSSNDHQSH RRQASMASSI
AMGLLFSLFC IIVIIIAIGS KRRRLKNEEA STSRDIYIDS RSHSATMNSD WRQNLSGTNL
LSINLAAFEK PLQNLTLADL VEATNGFHIA CQIGSGGFGD VYKAQLKDGK VVAIKKLIHV
SGQGDREFTA EMETIGKIKH RNLVPLLGYC KAGEERLLVY DYMKFGSLED VLHDRKKIGK
KLNWEARRKI AVGAARGLAF LHHNCIPHII HRDMKSSNVL IDEQLEARVS DFGMARLMSV
VDTHLSVSTL AGTPGYVPPE YYQSFRCTTK GDVYSYGVVL LELLTGKPPT DSADFGEDNN
LVGWVKQHTK LKITDVFDPE LLKEDPSVEL ELLEHLKIAC ACLDDRPSRR PTMLKVMAMF
KEIQAGSTVD SKTSSAAAGS IDEGGYGVLD MPLREAKEEK D
