BRI1_ARATH
ID BRI1_ARATH Reviewed; 1196 AA.
AC O22476; C0LGS4;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Protein BRASSINOSTEROID INSENSITIVE 1 {ECO:0000303|PubMed:9298904};
DE Short=AtBRI1 {ECO:0000303|PubMed:9298904};
DE EC=2.7.10.1 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=Brassinosteroid LRR receptor kinase {ECO:0000303|PubMed:9298904};
DE Flags: Precursor;
GN Name=BRI1 {ECO:0000303|PubMed:9298904}; OrderedLocusNames=At4g39400;
GN ORFNames=F23K16.30;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, MUTANTS BRI1-101;
RP BRI1-104; BRI1-113 AND BRI1-115, AND MUTAGENESIS OF GLY-611; ALA-1031;
RP GLY-1048 AND GLU-1078.
RC STRAIN=cv. Columbia;
RX PubMed=9298904; DOI=10.1016/s0092-8674(00)80357-8;
RA Li J., Chory J.;
RT "A putative leucine-rich repeat receptor kinase involved in brassinosteroid
RT signal transduction.";
RL Cell 90:929-938(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, MUTANTS BRI1-5/DWF2-W41;
RP BRI1-6/BRI1-119/DWF2-399; BRI1-7/DWF2-WM3-2; BRI1-8/DWF2-WM6-2 AND
RP BRI1-9/DWF2-WMB19, MUTAGENESIS OF CYS-69; GLY-613; GLY-644; SER-662 AND
RP ARG-983, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. En-2, and cv. Wassilewskija-2;
RX PubMed=10557222; DOI=10.1104/pp.121.3.743;
RA Noguchi T., Fujioka S., Choe S., Takatsuto S., Yoshida S., Yuan H.,
RA Feldmann K.A., Tax F.E.;
RT "Brassinosteroid-insensitive dwarf mutants of Arabidopsis accumulate
RT brassinosteroids.";
RL Plant Physiol. 121:743-752(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, MUTANTS BRI1-1; BRI1-108; BRI1-117 AND BRI1-102, AND
RP MUTAGENESIS OF THR-750; ALA-909; ARG-983 AND ASP-1139.
RC STRAIN=cv. Columbia;
RX PubMed=10938344; DOI=10.1104/pp.123.4.1247;
RA Friedrichsen D.M., Joazeiro C.A.P., Li J., Hunter T., Chory J.;
RT "BRASSINOSTEROID-INSENSITIVE-1 is a ubiquitously expressed leucine-rich
RT repeat receptor serine/threonine kinase.";
RL Plant Physiol. 123:1247-1256(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=20064227; DOI=10.1186/1471-2164-11-19;
RA Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.;
RT "Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-
RT like protein kinase genes in Arabidopsis thaliana.";
RL BMC Genomics 11:19-19(2010).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [7]
RP PHOSPHORYLATION AT SER-838; THR-842; THR-846; SER-858 AND THR-872, AND
RP MUTAGENESIS OF LYS-911.
RX PubMed=11027724; DOI=10.1104/pp.124.2.751;
RA Oh M.-H., Ray W.K., Huber S.C., Asara J.M., Gage D.A., Clouse S.D.;
RT "Recombinant BRASSINOSTEROID INSENSITIVE 1 receptor-like kinase
RT autophosphorylates on serine and threonine residues and phosphorylates a
RT conserved peptide motif in vitro.";
RL Plant Physiol. 124:751-766(2000).
RN [8]
RP STEROID-BINDING.
RX PubMed=10875920; DOI=10.1126/science.288.5475.2360;
RA He Z., Wang Z.-Y., Li J., Zhu Q., Lamb C., Ronald P., Chory J.;
RT "Perception of brassinosteroids by the extracellular domain of the receptor
RT kinase BRI1.";
RL Science 288:2360-2363(2000).
RN [9]
RP SUBCELLULAR LOCATION, STEROID-BINDING, AND AUTOPHOSPHORYLATION.
RX PubMed=11268216; DOI=10.1038/35066597;
RA Wang Z.-Y., Seto H., Fujioka S., Yoshida S., Chory J.;
RT "BRI1 is a critical component of a plasma-membrane receptor for plant
RT steroids.";
RL Nature 410:380-383(2001).
RN [10]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH BAK1.
RX PubMed=12150928; DOI=10.1016/s0092-8674(02)00814-0;
RA Nam K.H., Li J.;
RT "BRI1/BAK1, a receptor kinase pair mediating brassinosteroid signaling.";
RL Cell 110:203-212(2002).
RN [11]
RP PHOSPHORYLATION, AND INTERACTION WITH BAK1.
RX PubMed=12150929; DOI=10.1016/s0092-8674(02)00812-7;
RA Li J., Wen J., Lease K.A., Doke J.T., Tax F.E., Walker J.C.;
RT "BAK1, an Arabidopsis LRR receptor-like protein kinase, interacts with BRI1
RT and modulates brassinosteroid signaling.";
RL Cell 110:213-222(2002).
RN [12]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH BAK1.
RX PubMed=15548744; DOI=10.1105/tpc.104.025387;
RA Russinova E., Borst J.-W., Kwaaitaal M., Cano-Delgado A., Yin Y., Chory J.,
RA de Vries S.C.;
RT "Heterodimerization and endocytosis of Arabidopsis brassinosteroid
RT receptors BRI1 and AtSERK3 (BAK1).";
RL Plant Cell 16:3216-3229(2004).
RN [13]
RP INTERACTION WITH TTL.
RX PubMed=15319482; DOI=10.1105/tpc.104.023903;
RA Nam K.H., Li J.;
RT "The Arabidopsis transthyretin-like protein is a potential substrate of
RT BRASSINOSTEROID-INSENSITIVE 1.";
RL Plant Cell 16:2406-2417(2004).
RN [14]
RP PHOSPHORYLATION AT SER-838; SER-858; THR-872; THR-880; THR-982 AND
RP SER-1168, INTERACTION WITH BAK1, AND MUTAGENESIS OF SER-838; THR-842;
RP THR-846; SER-858; THR-872; THR-1039; SER-1044; THR-1045; THR-1049;
RP SER-1168; SER-1172; 1179-SER-THR-1180 AND SER-1187.
RX PubMed=15894717; DOI=10.1105/tpc.105.031393;
RA Wang X., Goshe M.B., Soderblom E.J., Phinney B.S., Kuchar J.A., Li J.,
RA Asami T., Yoshida S., Huber S.C., Clouse S.D.;
RT "Identification and functional analysis of in vivo phosphorylation sites of
RT the Arabidopsis BRASSINOSTEROID-INSENSITIVE1 receptor kinase.";
RL Plant Cell 17:1685-1703(2005).
RN [15]
RP INTERACTION WITH SERK1.
RX PubMed=16473966; DOI=10.1105/tpc.105.039412;
RA Karlova R., Boeren S., Russinova E., Aker J., Vervoort J., de Vries S.C.;
RT "The Arabidopsis SOMATIC EMBRYOGENESIS RECEPTOR-LIKE KINASE1 protein
RT complex includes BRASSINOSTEROID-INSENSITIVE1.";
RL Plant Cell 18:626-638(2006).
RN [16]
RP FUNCTION.
RX PubMed=17138891; DOI=10.1126/science.1134040;
RA Belkhadir Y., Chory J.;
RT "Brassinosteroid signaling: a paradigm for steroid hormone signaling from
RT the cell surface.";
RL Science 314:1410-1411(2006).
RN [17]
RP SUBCELLULAR LOCATION.
RX PubMed=17578906; DOI=10.1101/gad.1561307;
RA Geldner N., Hyman D.L., Wang X., Schumacher K., Chory J.;
RT "Endosomal signaling of plant steroid receptor kinase BRI1.";
RL Genes Dev. 21:1598-1602(2007).
RN [18]
RP GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=17588517; DOI=10.1016/j.molcel.2007.05.015;
RA Jin H., Yan Z., Nam K.H., Li J.;
RT "Allele-specific suppression of a defective brassinosteroid receptor
RT reveals a physiological role of UGGT in ER quality control.";
RL Mol. Cell 26:821-830(2007).
RN [19]
RP FUNCTION, AND DOMAIN.
RX PubMed=17520012; DOI=10.1371/journal.pone.0000449;
RA Kwezi L., Meier S., Mungur L., Ruzvidzo O., Irving H., Gehring C.;
RT "The Arabidopsis thaliana brassinosteroid receptor (AtBRI1) contains a
RT domain that functions as a guanylyl cyclase in vitro.";
RL PLoS ONE 2:E449-E449(2007).
RN [20]
RP SUBUNIT.
RX PubMed=17905839; DOI=10.1529/biophysj.107.112003;
RA Hink M.A., Shah K., Russinova E., de Vries S.C., Visser A.J.;
RT "Fluorescence fluctuation analysis of Arabidopsis thaliana somatic
RT embryogenesis receptor-like kinase and brassinosteroid insensitive 1
RT receptor oligomerization.";
RL Biophys. J. 94:1052-1062(2008).
RN [21]
RP MUTAGENESIS OF GLY-989.
RX PubMed=18332904; DOI=10.1038/cr.2008.36;
RA Xu W., Huang J., Li B., Li J., Wang Y.;
RT "Is kinase activity essential for biological functions of BRI1?";
RL Cell Res. 18:472-478(2008).
RN [22]
RP FUNCTION, PHOSPHORYLATION AT SER-838; THR-846; SER-858; SER-1166 AND
RP THR-1180, INTERACTION WITH BAK1, AND MUTAGENESIS OF SER-838; THR-842;
RP THR-846; SER-858; THR-1049; SER-1166; SER-1168; SER-1172; SER-1179 AND
RP THR-1180.
RX PubMed=18694562; DOI=10.1016/j.devcel.2008.06.011;
RA Wang X., Kota U., He K., Blackburn K., Li J., Goshe M.B., Huber S.C.,
RA Clouse S.D.;
RT "Sequential transphosphorylation of the BRI1/BAK1 receptor kinase complex
RT impacts early events in brassinosteroid signaling.";
RL Dev. Cell 15:220-235(2008).
RN [23]
RP FUNCTION, AND INTERACTION WITH BSK1 AND BSK3.
RX PubMed=18653891; DOI=10.1126/science.1156973;
RA Tang W., Kim T.W., Oses-Prieto J.A., Sun Y., Deng Z., Zhu S., Wang R.,
RA Burlingame A.L., Wang Z.Y.;
RT "BSKs mediate signal transduction from the receptor kinase BRI1 in
RT Arabidopsis.";
RL Science 321:557-560(2008).
RN [24]
RP PHOSPHORYLATION AT SER-887, AND PHOSPHORYLATION OF SERK1.
RX PubMed=19105183; DOI=10.1002/pmic.200701059;
RA Karlova R., Boeren S., van Dongen W., Kwaaitaal M., Aker J., Vervoort J.,
RA de Vries S.C.;
RT "Identification of in vitro phosphorylation sites in the Arabidopsis
RT thaliana somatic embryogenesis receptor-like kinases.";
RL Proteomics 9:368-379(2009).
RN [25]
RP FUNCTION, MUTAGENESIS OF TYR-831; TYR-898; TYR-945; TYR-956; TYR-961;
RP TYR-1052; TYR-1057; TYR-1058; TYR-1070 AND TYR-1072, AUTOPHOSPHORYLATION,
RP AND PHOSPHORYLATION AT TYR-831 AND TYR-956.
RX PubMed=19124768; DOI=10.1073/pnas.0810249106;
RA Oh M.-H., Wang X., Kota U., Goshe M.B., Clouse S.D., Huber S.C.;
RT "Tyrosine phosphorylation of the BRI1 receptor kinase emerges as a
RT component of brassinosteroid signaling in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:658-663(2009).
RN [26]
RP INTERACTION WITH CDG1.
RX PubMed=21855796; DOI=10.1016/j.molcel.2011.05.037;
RA Kim T.W., Guan S., Burlingame A.L., Wang Z.Y.;
RT "The CDG1 kinase mediates brassinosteroid signal transduction from BRI1
RT receptor kinase to BSU1 phosphatase and GSK3-like kinase BIN2.";
RL Mol. Cell 43:561-571(2011).
RN [27]
RP FUNCTION, AND INTERACTION WITH BSK5; BSK6 AND BSK11.
RX PubMed=23496207; DOI=10.1111/tpj.12175;
RA Sreeramulu S., Mostizky Y., Sunitha S., Shani E., Nahum H., Salomon D.,
RA Hayun L.B., Gruetter C., Rauh D., Ori N., Sessa G.;
RT "BSKs are partially redundant positive regulators of brassinosteroid
RT signaling in Arabidopsis.";
RL Plant J. 74:905-919(2013).
RN [28]
RP INTERACTION WITH BIK1.
RX PubMed=23818580; DOI=10.1073/pnas.1302154110;
RA Lin W., Lu D., Gao X., Jiang S., Ma X., Wang Z., Mengiste T., He P.,
RA Shan L.;
RT "Inverse modulation of plant immune and brassinosteroid signaling pathways
RT by the receptor-like cytoplasmic kinase BIK1.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:12114-12119(2013).
RN [29]
RP LACK OF INTERACTION WITH CNGC17 AND PSKR1, AND SUBCELLULAR LOCATION.
RX PubMed=26071421; DOI=10.1105/tpc.15.00306;
RA Ladwig F., Dahlke R.I., Stuehrwohldt N., Hartmann J., Harter K., Sauter M.;
RT "Phytosulfokine regulates growth in Arabidopsis through a response module
RT at the plasma membrane that includes CYCLIC NUCLEOTIDE-GATED CHANNEL17, H+-
RT ATPase, and BAK1.";
RL Plant Cell 27:1718-1729(2015).
RN [30]
RP INTERACTION WITH B'ALPHA; B'BETA; B'GAMMA AND B'ETA.
RX PubMed=26517938; DOI=10.1016/j.molp.2015.10.007;
RA Wang R., Liu M., Yuan M., Oses-Prieto J.A., Cai X., Sun Y.,
RA Burlingame A.L., Wang Z.Y., Tang W.;
RT "The brassinosteroid-activated BRI1 receptor kinase is switched off by
RT dephosphorylation mediated by cytoplasm-localized PP2A B' subunits.";
RL Mol. Plant 9:148-157(2016).
RN [31]
RP X-RAY CRYSTALLOGRAPHY (2.52 ANGSTROMS) OF 29-788 IN COMPLEX WITH
RP BRASSINOLIDE, AND GLYCOSYLATION AT ASN-112; ASN-154; ASN-233; ASN-275;
RP ASN-351 AND ASN-545.
RX PubMed=21666665; DOI=10.1038/nature10153;
RA Hothorn M., Belkhadir Y., Dreux M., Dabi T., Noel J.P., Wilson I.A.,
RA Chory J.;
RT "Structural basis of steroid hormone perception by the receptor kinase
RT BRI1.";
RL Nature 474:467-471(2011).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 23-784 IN COMPLEX WITH
RP BRASSINOLIDE, AND GLYCOSYLATION AT ASN-112; ASN-154; ASN-233; ASN-275;
RP ASN-351; ASN-510; ASN-545 AND ASN-573.
RX PubMed=21666666; DOI=10.1038/nature10178;
RA She J., Han Z., Kim T.W., Wang J., Cheng W., Chang J., Shi S., Wang J.,
RA Yang M., Wang Z.Y., Chai J.;
RT "Structural insight into brassinosteroid perception by BRI1.";
RL Nature 474:472-476(2011).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 29-788 IN COMPLEX WITH
RP BRASSINOLIDE AND SERK1, INTERACTION WITH SERK1, AND GLYCOSYLATION AT
RP ASN-112; ASN-154; ASN-233; ASN-275; ASN-351; ASN-545 AND ASN-573.
RX PubMed=23929946; DOI=10.1126/science.1242468;
RA Santiago J., Henzler C., Hothorn M.;
RT "Molecular mechanism for plant steroid receptor activation by somatic
RT embryogenesis co-receptor kinases.";
RL Science 341:889-892(2013).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 865-1160 IN COMPLEX WITH ATP, AND
RP GLYCOSYLATION AT ASN-154; ASN-275 AND ASN-545.
RX PubMed=24461462; DOI=10.1111/tpj.12445;
RA Bojar D., Martinez J., Santiago J., Rybin V., Bayliss R., Hothorn M.;
RT "Crystal structures of the phosphorylated BRI1 kinase domain and
RT implications for brassinosteroid signal initiation.";
RL Plant J. 78:31-43(2014).
CC -!- FUNCTION: Receptor with a dual specificity kinase activity acting on
CC both serine/threonine- and tyrosine-containing substrates. Regulates,
CC in response to brassinosteroid binding, a signaling cascade involved in
CC plant development, including expression of light- and stress-regulated
CC genes, promotion of cell elongation, normal leaf and chloroplast
CC senescence, and flowering. Binds brassinolide (BL), and less
CC effectively castasterone (CS), but not 2,3,22,23-O-
CC tetramethylbrassinolide or ecdysone. May be involved in a feedback
CC regulation of brassinosteroid biosynthesis. Phosphorylates BRI1-
CC associated receptor kinase 1 (BAK1), Transthyretin-Like protein (TTL)
CC and SERK1 on 'Ser-299' and 'Thr-462' in vitro. May have a guanylyl
CC cyclase activity (PubMed:10557222, PubMed:10938344, PubMed:17138891,
CC PubMed:17520012, PubMed:18694562, PubMed:19124768). Phosphorylates
CC BSK1, BSK2 and BSK3 in vitro (PubMed:18653891). Phosphorylates BSK1,
CC BSK3, BSK5, BSK6, BSK8 AND BSK11 in vitro (PubMed:23496207).
CC {ECO:0000269|PubMed:10557222, ECO:0000269|PubMed:10938344,
CC ECO:0000269|PubMed:17138891, ECO:0000269|PubMed:17520012,
CC ECO:0000269|PubMed:18653891, ECO:0000269|PubMed:18694562,
CC ECO:0000269|PubMed:19124768, ECO:0000269|PubMed:23496207}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10027};
CC -!- ACTIVITY REGULATION: Activated by Ser and Thr phosphorylation.
CC -!- SUBUNIT: Monomer or homodimer in the plasma membrane. Heterodimer with
CC BAK1 in the endosomes. Interacts with SERK1 and TTL in a kinase-
CC dependent manner. Bind to SERK1 in a brassinolide-dependent manner
CC (PubMed:23929946). Component of the SERK1 signaling complex, composed
CC of KAPP, CDC48A, GRF6 or GRF7, SERK1, SERK2, SERK3/BAK1 and BRI1.
CC Interacts with CDG1 (PubMed:21855796). No interactions with PSKR1 or
CC CNGC17 (PubMed:26071421). Interacts with BIK1 (PubMed:23818580).
CC Interacts with B'ALPHA, B'BETA, B'GAMMA and B'ETA (PubMed:26517938).
CC Interacts with BSK1 and BSK3 (PubMed:18653891). Interacts with BSK5,
CC BSK6 and BSK11 (PubMed:23496207). {ECO:0000269|PubMed:12150928,
CC ECO:0000269|PubMed:12150929, ECO:0000269|PubMed:15319482,
CC ECO:0000269|PubMed:15548744, ECO:0000269|PubMed:15894717,
CC ECO:0000269|PubMed:16473966, ECO:0000269|PubMed:17905839,
CC ECO:0000269|PubMed:18653891, ECO:0000269|PubMed:18694562,
CC ECO:0000269|PubMed:21855796, ECO:0000269|PubMed:23496207,
CC ECO:0000269|PubMed:23818580, ECO:0000269|PubMed:23929946,
CC ECO:0000269|PubMed:26071421, ECO:0000269|PubMed:26517938}.
CC -!- INTERACTION:
CC O22476; Q94F62: BAK1; NbExp=9; IntAct=EBI-1797828, EBI-617138;
CC O22476; O65440-2: BAM3; NbExp=3; IntAct=EBI-1797828, EBI-20653325;
CC O22476; O22476: BRI1; NbExp=4; IntAct=EBI-1797828, EBI-1797828;
CC O22476; Q944A7: BSK1; NbExp=4; IntAct=EBI-1797828, EBI-1797846;
CC O22476; Q8W4L3: BSK3; NbExp=2; IntAct=EBI-1797828, EBI-1797930;
CC O22476; Q6XAT2: ERL2; NbExp=2; IntAct=EBI-1797828, EBI-16895926;
CC O22476; Q9ZVD4: LRR-RLK; NbExp=2; IntAct=EBI-1797828, EBI-20651739;
CC O22476; Q9S7I6: RPK2; NbExp=2; IntAct=EBI-1797828, EBI-16940204;
CC O22476; Q94AG2: SERK1; NbExp=7; IntAct=EBI-1797828, EBI-1555537;
CC O22476; Q8RWZ1: SUB; NbExp=2; IntAct=EBI-1797828, EBI-17072125;
CC O22476; Q9LVM5: TTL; NbExp=3; IntAct=EBI-1797828, EBI-1803584;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26071421};
CC Single-pass type I membrane protein {ECO:0000305}. Endosome membrane;
CC Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously.
CC {ECO:0000269|PubMed:10938344, ECO:0000269|PubMed:9298904}.
CC -!- DEVELOPMENTAL STAGE: Expressed constitutively in either dark- or light-
CC grown seedlings.
CC -!- DOMAIN: Contains one leucine-zipper motif and two pairs of
CC conservatively spaced Cys (Cys pair 1 and 2) involved in forming
CC heterodimers. {ECO:0000269|PubMed:17520012}.
CC -!- DOMAIN: A 70 amino acid island between the 21th and the 22th LRR is
CC essential for the binding of brassinosteroids.
CC {ECO:0000269|PubMed:21666665}.
CC -!- DOMAIN: The JM domain (815-883) is a positive regulator of kinase
CC activity and is required for Tyr phosphorylation.
CC {ECO:0000269|PubMed:17520012}.
CC -!- DOMAIN: A guanylyl cyclase domain (1021-1134) having an in vitro
CC activity is included in the C-terminal kinase domain.
CC {ECO:0000269|PubMed:17520012}.
CC -!- PTM: Autophosphorylated on Tyr-831, Tyr-956 and maybe Tyr-1072.
CC Phosphorylated on at least 12 sites, with a preference for Ser
CC residues. Transphosphorylated on Ser-887 by SERK1 and on Ser-838, Thr-
CC 846, Ser-858 and Ser-1166 by BAK1. Phosphorylation on Ser-1166 enhances
CC the kinase activity. {ECO:0000269|PubMed:11027724,
CC ECO:0000269|PubMed:12150928, ECO:0000269|PubMed:12150929,
CC ECO:0000269|PubMed:15894717, ECO:0000269|PubMed:18694562,
CC ECO:0000269|PubMed:19105183, ECO:0000269|PubMed:19124768}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:17588517}.
CC -!- DISRUPTION PHENOTYPE: Dwarf phenotype and aberrant leaf shape.
CC {ECO:0000269|PubMed:10557222}.
CC -!- MISCELLANEOUS: Binding of brassinosteroid induces intramolecular
CC autophosphorylation of BRI1. Interaction with BAK1 activates both
CC receptor kinases and the full activation of either receptor kinase
CC requires transphosphorylation by their partners. Optimum in vitro
CC phosphorylation of the substrate requires Arg or Lys residues at P-3,
CC P-4, and P+5 (relative to the phosphorylated amino acid at P=0).
CC Homodimerizes in the absence of ligand and binds brassinosteroid in the
CC absence of its coreceptor BAK1.
CC -!- MISCELLANEOUS: The bri1-9 mutation produces a fully active protein with
CC a subtle conformational change that is recognized for reglucosylation
CC by UGGT, resulting in its endoplasmic reticulum retention via
CC Glc(1)Man(9)GlcNAc(2)-calreticulin/calnexin interaction.
CC {ECO:0000305|PubMed:17588517}.
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; AF017056; AAC49810.1; -; Genomic_DNA.
DR EMBL; FJ708766; ACN59359.1; -; mRNA.
DR EMBL; AL078620; CAB44675.1; -; Genomic_DNA.
DR EMBL; AL161595; CAB80603.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE87069.1; -; Genomic_DNA.
DR PIR; T09356; T09356.
DR RefSeq; NP_195650.1; NM_120100.3.
DR PDB; 3RGX; X-ray; 2.47 A; A=23-784.
DR PDB; 3RGZ; X-ray; 2.28 A; A=23-784.
DR PDB; 3RIZ; X-ray; 2.52 A; A=29-788.
DR PDB; 3RJ0; X-ray; 2.54 A; A=29-788.
DR PDB; 4LSA; X-ray; 2.50 A; A=29-788.
DR PDB; 4LSX; X-ray; 3.30 A; A/B=29-788.
DR PDB; 4M7E; X-ray; 3.60 A; A/B=24-784.
DR PDB; 4OH4; X-ray; 2.25 A; A/B=863-1172.
DR PDB; 4Q5J; X-ray; 2.77 A; A/B=863-1180.
DR PDB; 5LPB; X-ray; 1.98 A; A=865-1160.
DR PDB; 5LPV; X-ray; 2.70 A; A=865-1160.
DR PDB; 5LPW; X-ray; 2.43 A; A=865-1160.
DR PDB; 5LPY; X-ray; 2.30 A; A=865-1160.
DR PDB; 5LPZ; X-ray; 2.48 A; A=865-1196.
DR PDB; 6FIF; X-ray; 2.54 A; A=1-788.
DR PDBsum; 3RGX; -.
DR PDBsum; 3RGZ; -.
DR PDBsum; 3RIZ; -.
DR PDBsum; 3RJ0; -.
DR PDBsum; 4LSA; -.
DR PDBsum; 4LSX; -.
DR PDBsum; 4M7E; -.
DR PDBsum; 4OH4; -.
DR PDBsum; 4Q5J; -.
DR PDBsum; 5LPB; -.
DR PDBsum; 5LPV; -.
DR PDBsum; 5LPW; -.
DR PDBsum; 5LPY; -.
DR PDBsum; 5LPZ; -.
DR PDBsum; 6FIF; -.
DR AlphaFoldDB; O22476; -.
DR SMR; O22476; -.
DR BioGRID; 15375; 45.
DR DIP; DIP-45997N; -.
DR IntAct; O22476; 32.
DR STRING; 3702.AT4G39400.1; -.
DR TCDB; 1.A.87.2.6; the mechanosensitive calcium channel (mca) family.
DR iPTMnet; O22476; -.
DR PaxDb; O22476; -.
DR PRIDE; O22476; -.
DR ProteomicsDB; 240703; -.
DR EnsemblPlants; AT4G39400.1; AT4G39400.1; AT4G39400.
DR GeneID; 830095; -.
DR Gramene; AT4G39400.1; AT4G39400.1; AT4G39400.
DR KEGG; ath:AT4G39400; -.
DR Araport; AT4G39400; -.
DR TAIR; locus:2005498; AT4G39400.
DR eggNOG; ENOG502QRF2; Eukaryota.
DR HOGENOM; CLU_000288_22_4_1; -.
DR InParanoid; O22476; -.
DR OMA; GWVKLHA; -.
DR OrthoDB; 151283at2759; -.
DR PhylomeDB; O22476; -.
DR EvolutionaryTrace; O22476; -.
DR PRO; PR:O22476; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O22476; baseline and differential.
DR Genevisible; O22476; AT.
DR GO; GO:0005768; C:endosome; IDA:TAIR.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0032991; C:protein-containing complex; IPI:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:TAIR.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:TAIR.
DR GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:TAIR.
DR GO; GO:0005496; F:steroid binding; IDA:TAIR.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0048657; P:anther wall tapetum cell differentiation; IMP:TAIR.
DR GO; GO:0010268; P:brassinosteroid homeostasis; IEP:TAIR.
DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IMP:TAIR.
DR GO; GO:0009729; P:detection of brassinosteroid stimulus; IMP:TAIR.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0048366; P:leaf development; IMP:TAIR.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:UniProtKB.
DR GO; GO:0010584; P:pollen exine formation; IMP:TAIR.
DR GO; GO:0009911; P:positive regulation of flower development; IGI:TAIR.
DR GO; GO:1900140; P:regulation of seedling development; IMP:UniProtKB.
DR GO; GO:0010224; P:response to UV-B; IGI:TAIR.
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; 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; 2.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 7.
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 3D-structure; ATP-binding; Brassinosteroid signaling pathway;
KW Cell membrane; Endosome; Glycoprotein; Kinase; Leucine-rich repeat;
KW Lipid-binding; Membrane; Nucleotide-binding; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Signal;
KW Steroid-binding; Transferase; Transmembrane; Transmembrane helix;
KW Tyrosine-protein kinase.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1196
FT /note="Protein BRASSINOSTEROID INSENSITIVE 1"
FT /id="PRO_0000024305"
FT TRANSMEM 793..813
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 71..98
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 99..121
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 122..146
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 148..169
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 172..197
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 199..221
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 222..244
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 245..268
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 269..290
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 291..314
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 316..338
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 339..363
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 364..388
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 390..413
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 415..439
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 441..463
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 464..487
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 488..511
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 513..535
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 536..559
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT REPEAT 561..583
FT /note="LRR 21"
FT /evidence="ECO:0000255"
FT REPEAT 653..677
FT /note="LRR 22"
FT /evidence="ECO:0000255"
FT REPEAT 678..701
FT /note="LRR 23"
FT /evidence="ECO:0000255"
FT REPEAT 702..725
FT /note="LRR 24"
FT /evidence="ECO:0000255"
FT REPEAT 727..750
FT /note="LRR 25"
FT /evidence="ECO:0000255"
FT DOMAIN 883..1158
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 640..642
FT /note="SERK1 binding"
FT /evidence="ECO:0000269|PubMed:23929946,
FT ECO:0007744|PDB:4LSX"
FT REGION 726..729
FT /note="SERK1 binding"
FT /evidence="ECO:0000269|PubMed:23929946,
FT ECO:0007744|PDB:4LSX"
FT REGION 746..750
FT /note="SERK1 binding"
FT /evidence="ECO:0000269|PubMed:23929946,
FT ECO:0007744|PDB:4LSX"
FT MOTIF 62..69
FT /note="Cys pair 1"
FT MOTIF 763..770
FT /note="Cys pair 2"
FT ACT_SITE 1009
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 597
FT /ligand="brassinolide"
FT /ligand_id="ChEBI:CHEBI:28277"
FT /evidence="ECO:0000269|PubMed:21666666,
FT ECO:0000269|PubMed:23929946"
FT BINDING 642
FT /ligand="brassinolide"
FT /ligand_id="ChEBI:CHEBI:28277"
FT /evidence="ECO:0000269|PubMed:23929946"
FT BINDING 647
FT /ligand="brassinolide"
FT /ligand_id="ChEBI:CHEBI:28277"
FT /evidence="ECO:0000269|PubMed:21666665,
FT ECO:0000269|PubMed:21666666, ECO:0000269|PubMed:23929946"
FT BINDING 705
FT /ligand="brassinolide"
FT /ligand_id="ChEBI:CHEBI:28277"
FT /evidence="ECO:0000269|PubMed:21666666"
FT BINDING 889..897
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 911
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:24461462"
FT BINDING 957..959
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:24461462"
FT BINDING 963..966
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:24461462"
FT BINDING 1009..1014
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:24461462"
FT BINDING 1027
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:24461462"
FT SITE 705
FT /note="Interacts with SERK1"
FT /evidence="ECO:0000269|PubMed:23929946,
FT ECO:0007744|PDB:4LSX"
FT SITE 765
FT /note="Interacts with SERK1"
FT /evidence="ECO:0000269|PubMed:23929946,
FT ECO:0007744|PDB:4LSX"
FT MOD_RES 831
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:19124768"
FT MOD_RES 838
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11027724,
FT ECO:0000269|PubMed:15894717, ECO:0000269|PubMed:18694562"
FT MOD_RES 842
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:11027724"
FT MOD_RES 846
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:11027724,
FT ECO:0000269|PubMed:18694562"
FT MOD_RES 851
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT MOD_RES 858
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11027724,
FT ECO:0000269|PubMed:15894717, ECO:0000269|PubMed:18694562"
FT MOD_RES 872
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:11027724,
FT ECO:0000269|PubMed:15894717"
FT MOD_RES 880
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:15894717"
FT MOD_RES 887
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19105183"
FT MOD_RES 891
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 956
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:19124768"
FT MOD_RES 981
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 982
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:15894717"
FT MOD_RES 1035
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 1039
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT MOD_RES 1042
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 1044
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7, ECO:0000255"
FT MOD_RES 1045
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT MOD_RES 1049
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT MOD_RES 1052
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 1060
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 1072
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 1166
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18694562"
FT MOD_RES 1168
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15894717"
FT MOD_RES 1169
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT MOD_RES 1172
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 1179
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 1180
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18694562"
FT MOD_RES 1187
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21666665,
FT ECO:0000269|PubMed:21666666, ECO:0000269|PubMed:23929946"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21666665,
FT ECO:0000269|PubMed:21666666, ECO:0000269|PubMed:23929946,
FT ECO:0000269|PubMed:24461462"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21666665,
FT ECO:0000269|PubMed:21666666, ECO:0000269|PubMed:23929946"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21666665,
FT ECO:0000269|PubMed:21666666, ECO:0000269|PubMed:23929946,
FT ECO:0000269|PubMed:24461462"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21666665,
FT ECO:0000269|PubMed:21666666, ECO:0000269|PubMed:23929946"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 438
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 510
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21666666"
FT CARBOHYD 545
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21666665,
FT ECO:0000269|PubMed:21666666, ECO:0000269|PubMed:23929946,
FT ECO:0000269|PubMed:24461462"
FT CARBOHYD 573
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21666666,
FT ECO:0000269|PubMed:23929946"
FT CARBOHYD 636
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 653
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 737
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 69
FT /note="C->Y: In bri1-5; brassinosteroid-insensitive semi-
FT dwarf mutant."
FT /evidence="ECO:0000269|PubMed:10557222"
FT MUTAGEN 611
FT /note="G->E: In bri1-113; brassinosteroid-insensitive semi-
FT dwarf mutant."
FT /evidence="ECO:0000269|PubMed:9298904"
FT MUTAGEN 613
FT /note="G->S: In bri1-7; brassinosteroid-insensitive semi-
FT dwarf mutant."
FT /evidence="ECO:0000269|PubMed:10557222"
FT MUTAGEN 644
FT /note="G->D: In bri1-6; brassinosteroid-insensitive semi-
FT dwarf mutant."
FT /evidence="ECO:0000269|PubMed:10557222"
FT MUTAGEN 662
FT /note="S->F: In bri1-9; brassinosteroid-insensitive semi-
FT dwarf mutant."
FT /evidence="ECO:0000269|PubMed:10557222"
FT MUTAGEN 750
FT /note="T->I: In bri1-102; brassinosteroid-insensitive dwarf
FT mutant."
FT /evidence="ECO:0000269|PubMed:10938344"
FT MUTAGEN 831
FT /note="Y->D,E: No effect on kinase activity, flowering time
FT or leaf size, but altered leaf shape."
FT /evidence="ECO:0000269|PubMed:19124768"
FT MUTAGEN 831
FT /note="Y->F: No effect on kinase activity but altered
FT flowering time and leaf size and shape."
FT /evidence="ECO:0000269|PubMed:19124768"
FT MUTAGEN 838
FT /note="S->A: Decreases peptide phosphorylation, but no
FT effect on autophosphorylation."
FT /evidence="ECO:0000269|PubMed:15894717,
FT ECO:0000269|PubMed:18694562"
FT MUTAGEN 838
FT /note="S->D: Increased kinase activity; when associated
FT with D-842; D-846 and D-858."
FT /evidence="ECO:0000269|PubMed:15894717,
FT ECO:0000269|PubMed:18694562"
FT MUTAGEN 842
FT /note="T->A: Decreases peptide phosphorylation, but no
FT effect on autophosphorylation."
FT /evidence="ECO:0000269|PubMed:15894717,
FT ECO:0000269|PubMed:18694562"
FT MUTAGEN 842
FT /note="T->D: Increased kinase activity; when associated
FT with D-838; D-846 and D-858."
FT /evidence="ECO:0000269|PubMed:15894717,
FT ECO:0000269|PubMed:18694562"
FT MUTAGEN 846
FT /note="T->A: Decreases peptide phosphorylation, but no
FT effect on autophosphorylation."
FT /evidence="ECO:0000269|PubMed:15894717,
FT ECO:0000269|PubMed:18694562"
FT MUTAGEN 846
FT /note="T->D: Increased kinase activity; when associated
FT with D-838; D-842 and D-858."
FT /evidence="ECO:0000269|PubMed:15894717,
FT ECO:0000269|PubMed:18694562"
FT MUTAGEN 858
FT /note="S->A: Decreases peptide phosphorylation, but no
FT effect on autophosphorylation."
FT /evidence="ECO:0000269|PubMed:15894717,
FT ECO:0000269|PubMed:18694562"
FT MUTAGEN 858
FT /note="S->D: Increased kinase activity; when associated
FT with D-838; D-842 and D-846."
FT /evidence="ECO:0000269|PubMed:15894717,
FT ECO:0000269|PubMed:18694562"
FT MUTAGEN 872
FT /note="T->A: 10-fold increase in peptide phosphorylation."
FT /evidence="ECO:0000269|PubMed:15894717"
FT MUTAGEN 898
FT /note="Y->F: No effect on kinase activity."
FT /evidence="ECO:0000269|PubMed:19124768"
FT MUTAGEN 909
FT /note="A->T: In bri1-1; brassinosteroid-insensitive dwarf
FT mutant."
FT /evidence="ECO:0000269|PubMed:10938344"
FT MUTAGEN 911
FT /note="K->E: Loss of kinase activity; dwarf mutant."
FT /evidence="ECO:0000269|PubMed:11027724"
FT MUTAGEN 945
FT /note="Y->F: No effect on kinase activity."
FT /evidence="ECO:0000269|PubMed:19124768"
FT MUTAGEN 956
FT /note="Y->F: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:19124768"
FT MUTAGEN 961
FT /note="Y->F: No effect on kinase activity."
FT /evidence="ECO:0000269|PubMed:19124768"
FT MUTAGEN 983
FT /note="R->N: In bri1-8; brassinosteroid-insensitive dwarf
FT mutant."
FT /evidence="ECO:0000269|PubMed:10557222"
FT MUTAGEN 983
FT /note="R->Q: In bri1-108; brassinosteroid-insensitive dwarf
FT mutant."
FT /evidence="ECO:0000269|PubMed:10938344"
FT MUTAGEN 989
FT /note="G->I: In bri1-301; impaired kinase activity and loss
FT of autophosphorylation."
FT /evidence="ECO:0000269|PubMed:18332904"
FT MUTAGEN 1031
FT /note="A->W: In bri1-104; brassinosteroid-insensitive dwarf
FT mutant, but no effect on interaction with TTL."
FT /evidence="ECO:0000269|PubMed:9298904"
FT MUTAGEN 1039
FT /note="T->A: Abolishes peptide phosphorylation, and to a
FT lower level autophosphorylation."
FT /evidence="ECO:0000269|PubMed:15894717"
FT MUTAGEN 1042
FT /note="S->A: Abolishes peptide phosphorylation, and to a
FT lower level autophosphorylation."
FT MUTAGEN 1044
FT /note="S->A: Abolishes peptide phosphorylation, and
FT autophosphorylation."
FT /evidence="ECO:0000269|PubMed:15894717"
FT MUTAGEN 1045
FT /note="T->A: Abolishes peptide phosphorylation, and
FT autophosphorylation."
FT /evidence="ECO:0000269|PubMed:15894717"
FT MUTAGEN 1048
FT /note="G->D: In bri1-115; brassinosteroid-insensitive dwarf
FT mutant and no interaction with TTL."
FT /evidence="ECO:0000269|PubMed:9298904"
FT MUTAGEN 1049
FT /note="T->A: Abolishes peptide phosphorylation, and
FT autophosphorylation."
FT /evidence="ECO:0000269|PubMed:15894717,
FT ECO:0000269|PubMed:18694562"
FT MUTAGEN 1049
FT /note="T->D: Loss of kinase activity and brassinosteroid
FT signaling."
FT /evidence="ECO:0000269|PubMed:15894717,
FT ECO:0000269|PubMed:18694562"
FT MUTAGEN 1052
FT /note="Y->F: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:19124768"
FT MUTAGEN 1057
FT /note="Y->F: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:19124768"
FT MUTAGEN 1058
FT /note="Y->F: No effect on kinase activity."
FT /evidence="ECO:0000269|PubMed:19124768"
FT MUTAGEN 1070
FT /note="Y->F: No effect on kinase activity."
FT /evidence="ECO:0000269|PubMed:19124768"
FT MUTAGEN 1072
FT /note="Y->F: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:19124768"
FT MUTAGEN 1078
FT /note="E->K: In bri1-101; brassinosteroid-insensitive dwarf
FT mutant and no interaction with TTL."
FT /evidence="ECO:0000269|PubMed:9298904"
FT MUTAGEN 1139
FT /note="D->N: In bri1-117; brassinosteroid-insensitive dwarf
FT mutant."
FT /evidence="ECO:0000269|PubMed:10938344"
FT MUTAGEN 1166
FT /note="S->D: Increased kinase activity; when associated
FT with D-1168; D-1172; D-1179 and D-1180."
FT /evidence="ECO:0000269|PubMed:18694562"
FT MUTAGEN 1168
FT /note="S->A: Decreases peptide phosphorylation, but no
FT effect on autophosphorylation."
FT /evidence="ECO:0000269|PubMed:15894717,
FT ECO:0000269|PubMed:18694562"
FT MUTAGEN 1168
FT /note="S->D: Increased kinase activity; when associated
FT with D-1166; D-1172; D-1179 and D-1180."
FT /evidence="ECO:0000269|PubMed:15894717,
FT ECO:0000269|PubMed:18694562"
FT MUTAGEN 1172
FT /note="S->A: Decreases peptide phosphorylation, but no
FT effect on autophosphorylation."
FT /evidence="ECO:0000269|PubMed:15894717,
FT ECO:0000269|PubMed:18694562"
FT MUTAGEN 1172
FT /note="S->D: Increased kinase activity; when associated
FT with D-1166; D-1168; D-1179 and D-1180."
FT /evidence="ECO:0000269|PubMed:15894717,
FT ECO:0000269|PubMed:18694562"
FT MUTAGEN 1179..1180
FT /note="ST->A: Decreases peptide phosphorylation, but no
FT effect on autophosphorylation."
FT /evidence="ECO:0000269|PubMed:15894717"
FT MUTAGEN 1179
FT /note="S->D: Increased kinase activity; when associated
FT with D-1166; D-1168; D-1172 and D-1180."
FT /evidence="ECO:0000269|PubMed:18694562"
FT MUTAGEN 1180
FT /note="T->D: Increased kinase activity; when associated
FT with D-1166; D-1168; D-1172 and D-1179."
FT /evidence="ECO:0000269|PubMed:18694562"
FT MUTAGEN 1187
FT /note="S->A: Decreases peptide phosphorylation, but no
FT effect on autophosphorylation."
FT /evidence="ECO:0000269|PubMed:15894717"
FT HELIX 32..43
FT /evidence="ECO:0007829|PDB:3RGZ"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:3RIZ"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:3RGX"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:3RGZ"
FT HELIX 88..94
FT /evidence="ECO:0007829|PDB:3RGZ"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:3RGZ"
FT HELIX 138..146
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:3RGX"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:3RGZ"
FT HELIX 190..195
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:3RGZ"
FT HELIX 261..264
FT /evidence="ECO:0007829|PDB:3RGZ"
FT TURN 265..267
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 300..306
FT /evidence="ECO:0007829|PDB:3RGZ"
FT HELIX 309..314
FT /evidence="ECO:0007829|PDB:3RGX"
FT TURN 315..317
FT /evidence="ECO:0007829|PDB:3RGX"
FT STRAND 319..322
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 325..330
FT /evidence="ECO:0007829|PDB:3RGZ"
FT HELIX 334..338
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 349..355
FT /evidence="ECO:0007829|PDB:3RGZ"
FT HELIX 358..361
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 374..379
FT /evidence="ECO:0007829|PDB:3RGZ"
FT HELIX 385..388
FT /evidence="ECO:0007829|PDB:3RGZ"
FT TURN 389..391
FT /evidence="ECO:0007829|PDB:3RGX"
FT STRAND 393..396
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 399..405
FT /evidence="ECO:0007829|PDB:3RGZ"
FT TURN 408..411
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:4LSA"
FT STRAND 420..422
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 425..431
FT /evidence="ECO:0007829|PDB:3RGZ"
FT HELIX 434..438
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 444..446
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 449..454
FT /evidence="ECO:0007829|PDB:3RGZ"
FT HELIX 458..462
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 468..470
FT /evidence="ECO:0007829|PDB:3RGZ"
FT HELIX 482..486
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 492..494
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 497..500
FT /evidence="ECO:0007829|PDB:3RIZ"
FT HELIX 506..510
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 516..518
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 525..527
FT /evidence="ECO:0007829|PDB:3RIZ"
FT HELIX 530..534
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 540..542
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 549..551
FT /evidence="ECO:0007829|PDB:3RGZ"
FT HELIX 554..558
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 564..566
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 569..575
FT /evidence="ECO:0007829|PDB:3RGZ"
FT HELIX 578..581
FT /evidence="ECO:0007829|PDB:3RGZ"
FT TURN 582..585
FT /evidence="ECO:0007829|PDB:3RGZ"
FT TURN 591..594
FT /evidence="ECO:0007829|PDB:4LSA"
FT STRAND 596..601
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 611..617
FT /evidence="ECO:0007829|PDB:3RGZ"
FT HELIX 623..631
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 641..645
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 651..654
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 658..660
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 663..668
FT /evidence="ECO:0007829|PDB:3RGZ"
FT HELIX 672..676
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 682..684
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 687..693
FT /evidence="ECO:0007829|PDB:3RGX"
FT HELIX 696..700
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 706..708
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 715..717
FT /evidence="ECO:0007829|PDB:3RGX"
FT HELIX 720..724
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 729..732
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 735..741
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 744..747
FT /evidence="ECO:0007829|PDB:3RGZ"
FT HELIX 748..750
FT /evidence="ECO:0007829|PDB:3RGZ"
FT HELIX 753..756
FT /evidence="ECO:0007829|PDB:3RGZ"
FT STRAND 761..764
FT /evidence="ECO:0007829|PDB:3RGZ"
FT HELIX 873..879
FT /evidence="ECO:0007829|PDB:5LPB"
FT TURN 880..883
FT /evidence="ECO:0007829|PDB:5LPB"
FT HELIX 885..887
FT /evidence="ECO:0007829|PDB:5LPB"
FT STRAND 888..892
FT /evidence="ECO:0007829|PDB:5LPB"
FT STRAND 895..901
FT /evidence="ECO:0007829|PDB:5LPB"
FT STRAND 907..913
FT /evidence="ECO:0007829|PDB:5LPB"
FT TURN 916..918
FT /evidence="ECO:0007829|PDB:5LPB"
FT HELIX 919..929
FT /evidence="ECO:0007829|PDB:5LPB"
FT HELIX 931..933
FT /evidence="ECO:0007829|PDB:5LPB"
FT STRAND 942..948
FT /evidence="ECO:0007829|PDB:5LPB"
FT STRAND 951..957
FT /evidence="ECO:0007829|PDB:5LPB"
FT HELIX 964..969
FT /evidence="ECO:0007829|PDB:5LPB"
FT HELIX 971..973
FT /evidence="ECO:0007829|PDB:5LPY"
FT HELIX 980..999
FT /evidence="ECO:0007829|PDB:5LPB"
FT STRAND 1001..1006
FT /evidence="ECO:0007829|PDB:5LPB"
FT HELIX 1012..1014
FT /evidence="ECO:0007829|PDB:5LPB"
FT STRAND 1015..1017
FT /evidence="ECO:0007829|PDB:5LPB"
FT STRAND 1023..1025
FT /evidence="ECO:0007829|PDB:5LPB"
FT STRAND 1032..1034
FT /evidence="ECO:0007829|PDB:5LPB"
FT TURN 1050..1052
FT /evidence="ECO:0007829|PDB:5LPB"
FT HELIX 1055..1058
FT /evidence="ECO:0007829|PDB:5LPB"
FT STRAND 1060..1063
FT /evidence="ECO:0007829|PDB:5LPB"
FT HELIX 1065..1081
FT /evidence="ECO:0007829|PDB:5LPB"
FT TURN 1089..1093
FT /evidence="ECO:0007829|PDB:4OH4"
FT HELIX 1096..1103
FT /evidence="ECO:0007829|PDB:5LPB"
FT HELIX 1108..1110
FT /evidence="ECO:0007829|PDB:5LPB"
FT HELIX 1114..1117
FT /evidence="ECO:0007829|PDB:5LPB"
FT HELIX 1121..1123
FT /evidence="ECO:0007829|PDB:5LPB"
FT HELIX 1124..1137
FT /evidence="ECO:0007829|PDB:5LPB"
FT HELIX 1142..1144
FT /evidence="ECO:0007829|PDB:5LPB"
FT HELIX 1148..1159
FT /evidence="ECO:0007829|PDB:5LPB"
SQ SEQUENCE 1196 AA; 130543 MW; C7FBA1C21294E600 CRC64;
MKTFSSFFLS VTTLFFFSFF SLSFQASPSQ SLYREIHQLI SFKDVLPDKN LLPDWSSNKN
PCTFDGVTCR DDKVTSIDLS SKPLNVGFSA VSSSLLSLTG LESLFLSNSH INGSVSGFKC
SASLTSLDLS RNSLSGPVTT LTSLGSCSGL KFLNVSSNTL DFPGKVSGGL KLNSLEVLDL
SANSISGANV VGWVLSDGCG ELKHLAISGN KISGDVDVSR CVNLEFLDVS SNNFSTGIPF
LGDCSALQHL DISGNKLSGD FSRAISTCTE LKLLNISSNQ FVGPIPPLPL KSLQYLSLAE
NKFTGEIPDF LSGACDTLTG LDLSGNHFYG AVPPFFGSCS LLESLALSSN NFSGELPMDT
LLKMRGLKVL DLSFNEFSGE LPESLTNLSA SLLTLDLSSN NFSGPILPNL CQNPKNTLQE
LYLQNNGFTG KIPPTLSNCS ELVSLHLSFN YLSGTIPSSL GSLSKLRDLK LWLNMLEGEI
PQELMYVKTL ETLILDFNDL TGEIPSGLSN CTNLNWISLS NNRLTGEIPK WIGRLENLAI
LKLSNNSFSG NIPAELGDCR SLIWLDLNTN LFNGTIPAAM FKQSGKIAAN FIAGKRYVYI
KNDGMKKECH GAGNLLEFQG IRSEQLNRLS TRNPCNITSR VYGGHTSPTF DNNGSMMFLD
MSYNMLSGYI PKEIGSMPYL FILNLGHNDI SGSIPDEVGD LRGLNILDLS SNKLDGRIPQ
AMSALTMLTE IDLSNNNLSG PIPEMGQFET FPPAKFLNNP GLCGYPLPRC DPSNADGYAH
HQRSHGRRPA SLAGSVAMGL LFSFVCIFGL ILVGREMRKR RRKKEAELEM YAEGHGNSGD
RTANNTNWKL TGVKEALSIN LAAFEKPLRK LTFADLLQAT NGFHNDSLIG SGGFGDVYKA
ILKDGSAVAI KKLIHVSGQG DREFMAEMET IGKIKHRNLV PLLGYCKVGD ERLLVYEFMK
YGSLEDVLHD PKKAGVKLNW STRRKIAIGS ARGLAFLHHN CSPHIIHRDM KSSNVLLDEN
LEARVSDFGM ARLMSAMDTH LSVSTLAGTP GYVPPEYYQS FRCSTKGDVY SYGVVLLELL
TGKRPTDSPD FGDNNLVGWV KQHAKLRISD VFDPELMKED PALEIELLQH LKVAVACLDD
RAWRRPTMVQ VMAMFKEIQA GSGIDSQSTI RSIEDGGFST IEMVDMSIKE VPEGKL
