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Q9ZPS9 (BRL2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase BRI1-like 2

EC=2.7.11.1
Alternative name(s):
BRASSINOSTEROID INSENSITIVE 1-like protein 2
Protein VASCULAR HIGHWAY 1
Gene names
Name:BRL2
Synonyms:VH1
Ordered Locus Names:At2g01950
ORF Names:F14H20.2
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length1143 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor with a serine/threonine-protein kinase activity, which may transduce extracellular spatial and temporal signals into downstream cell differentiation responses in provascular and procambial cells. In contrast to BRI1, BRL1 and BRL3, it does not bind brassinolide. Ref.4 Ref.6

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subunit structure

Interacts with TTL3. Ref.6

Subcellular location

Cell membrane; Single-pass type I membrane protein Ref.5.

Tissue specificity

Expressed in provascular and procambial sites throughout plant development. Expressed throughout globe- to heart-staged embryos. Then, it is restricted to procambial cells by the late torpedo stage, and this pattern persists throughout the duration of embryo development. After germination, it is expressed not only in procambial cells throughout the plant but also in all lateral organ primordia before the onset of vascularization. Ref.4 Ref.6

Domain

Contains two pairs of conservatively spaced Cys (Cys pair 1 and 2) possibly involved in forming some heterodimers By similarity.

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.

Contains 23 LRR (leucine-rich) repeats.

Contains 1 protein kinase domain.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential
Chain32 – 11431112Serine/threonine-protein kinase BRI1-like 2
PRO_0000024309

Regions

Topological domain32 – 756725Extracellular Potential
Transmembrane757 – 77721Helical; Potential
Topological domain778 – 1143366Cytoplasmic Potential
Repeat79 – 10022LRR 1
Repeat104 – 12623LRR 2
Repeat128 – 15023LRR 3
Repeat153 – 17523LRR 4
Repeat178 – 20023LRR 5
Repeat205 – 22824LRR 6
Repeat229 – 25123LRR 7
Repeat253 – 27523LRR 8
Repeat278 – 29922LRR 9
Repeat302 – 32322LRR 10
Repeat327 – 34923LRR 11
Repeat351 – 37222LRR 12
Repeat376 – 39823LRR 13
Repeat400 – 42223LRR 14
Repeat424 – 44623LRR 15
Repeat448 – 47023LRR 16
Repeat472 – 49423LRR 17
Repeat496 – 51823LRR 18
Repeat520 – 54223LRR 19
Repeat612 – 63423LRR 20
Repeat636 – 65823LRR 21
Repeat660 – 68223LRR 22
Repeat684 – 70623LRR 23
Domain838 – 1129292Protein kinase
Nucleotide binding844 – 8529ATP By similarity
Motif68 – 758Cys pair 1
Motif720 – 7278Cys pair 2

Sites

Active site9661Proton acceptor By similarity
Binding site8661ATP By similarity

Amino acid modifications

Modified residue8351Phosphothreonine By similarity
Modified residue9111Phosphotyrosine By similarity
Glycosylation841N-linked (GlcNAc...) Potential
Glycosylation1181N-linked (GlcNAc...) Potential
Glycosylation1631N-linked (GlcNAc...) Potential
Glycosylation1881N-linked (GlcNAc...) Potential
Glycosylation2261N-linked (GlcNAc...) Potential
Glycosylation2341N-linked (GlcNAc...) Potential
Glycosylation2881N-linked (GlcNAc...) Potential
Glycosylation3121N-linked (GlcNAc...) Potential
Glycosylation4121N-linked (GlcNAc...) Potential
Glycosylation4691N-linked (GlcNAc...) Potential
Glycosylation5061N-linked (GlcNAc...) Potential
Glycosylation6811N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q9ZPS9 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 7D1C88493F27A94E

FASTA1,143125,676
        10         20         30         40         50         60 
MTTSPIRVRI RTRIQISFIF LLTHLSQSSS SDQSSLKTDS LSLLSFKTMI QDDPNNILSN 

        70         80         90        100        110        120 
WSPRKSPCQF SGVTCLGGRV TEINLSGSGL SGIVSFNAFT SLDSLSVLKL SENFFVLNST 

       130        140        150        160        170        180 
SLLLLPLTLT HLELSSSGLI GTLPENFFSK YSNLISITLS YNNFTGKLPN DLFLSSKKLQ 

       190        200        210        220        230        240 
TLDLSYNNIT GPISGLTIPL SSCVSMTYLD FSGNSISGYI SDSLINCTNL KSLNLSYNNF 

       250        260        270        280        290        300 
DGQIPKSFGE LKLLQSLDLS HNRLTGWIPP EIGDTCRSLQ NLRLSYNNFT GVIPESLSSC 

       310        320        330        340        350        360 
SWLQSLDLSN NNISGPFPNT ILRSFGSLQI LLLSNNLISG DFPTSISACK SLRIADFSSN 

       370        380        390        400        410        420 
RFSGVIPPDL CPGAASLEEL RLPDNLVTGE IPPAISQCSE LRTIDLSLNY LNGTIPPEIG 

       430        440        450        460        470        480 
NLQKLEQFIA WYNNIAGEIP PEIGKLQNLK DLILNNNQLT GEIPPEFFNC SNIEWVSFTS 

       490        500        510        520        530        540 
NRLTGEVPKD FGILSRLAVL QLGNNNFTGE IPPELGKCTT LVWLDLNTNH LTGEIPPRLG 

       550        560        570        580        590        600 
RQPGSKALSG LLSGNTMAFV RNVGNSCKGV GGLVEFSGIR PERLLQIPSL KSCDFTRMYS 

       610        620        630        640        650        660 
GPILSLFTRY QTIEYLDLSY NQLRGKIPDE IGEMIALQVL ELSHNQLSGE IPFTIGQLKN 

       670        680        690        700        710        720 
LGVFDASDNR LQGQIPESFS NLSFLVQIDL SNNELTGPIP QRGQLSTLPA TQYANNPGLC 

       730        740        750        760        770        780 
GVPLPECKNG NNQLPAGTEE GKRAKHGTRA ASWANSIVLG VLISAASVCI LIVWAIAVRA 

       790        800        810        820        830        840 
RRRDADDAKM LHSLQAVNSA TTWKIEKEKE PLSINVATFQ RQLRKLKFSQ LIEATNGFSA 

       850        860        870        880        890        900 
ASMIGHGGFG EVFKATLKDG SSVAIKKLIR LSCQGDREFM AEMETLGKIK HRNLVPLLGY 

       910        920        930        940        950        960 
CKIGEERLLV YEFMQYGSLE EVLHGPRTGE KRRILGWEER KKIAKGAAKG LCFLHHNCIP 

       970        980        990       1000       1010       1020 
HIIHRDMKSS NVLLDQDMEA RVSDFGMARL ISALDTHLSV STLAGTPGYV PPEYYQSFRC 

      1030       1040       1050       1060       1070       1080 
TAKGDVYSIG VVMLEILSGK RPTDKEEFGD TNLVGWSKMK AREGKHMEVI DEDLLKEGSS 

      1090       1100       1110       1120       1130       1140 
ESLNEKEGFE GGVIVKEMLR YLEIALRCVD DFPSKRPNML QVVASLRELR GSENNSHSHS 


NSL 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"VH1, a provascular cell-specific receptor kinase that influences leaf cell patterns in Arabidopsis."
Clay N.K., Nelson T.
Plant Cell 14:2707-2722(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[5]"BRL1 and BRL3 are novel brassinosteroid receptors that function in vascular differentiation in Arabidopsis."
Cano-Delgado A., Yin Y., Yu C., Vafeados D., Mora-Garcia S., Cheng J.-C., Nam K.H., Li J., Chory J.
Development 131:5341-5351(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, LACK OF STEROID-BINDING.
[6]"VH1/BRL2 receptor-like kinase interacts with vascular-specific adaptor proteins VIT and VIK to influence leaf venation."
Ceserani T., Trofka A., Gandotra N., Nelson T.
Plant J. 57:1000-1014(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TTL3, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC006532 Genomic DNA. Translation: AAD20088.1.
CP002685 Genomic DNA. Translation: AEC05526.1.
AY074313 mRNA. Translation: AAL67010.1.
PIRB84431.
RefSeqNP_178304.1. NM_126256.3.
UniGeneAt.13922.

3D structure databases

ProteinModelPortalQ9ZPS9.
SMRQ9ZPS9. Positions 35-727, 790-1131.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9ZPS9. 64 interactions.
MINTMINT-8064047.

Proteomic databases

PaxDbQ9ZPS9.
PRIDEQ9ZPS9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G01950.1; AT2G01950.1; AT2G01950.
GeneID814726.
KEGGath:AT2G01950.

Organism-specific databases

GeneFarm616. 54.
TAIRAT2G01950.

Phylogenomic databases

eggNOGCOG4886.
HOGENOMHOG000116551.
InParanoidQ9ZPS9.
OMAAASWANS.
PhylomeDBQ9ZPS9.

Enzyme and pathway databases

BioCycARA:AT2G01950-MONOMER.

Gene expression databases

ArrayExpressQ9ZPS9.
GenevestigatorQ9ZPS9.

Family and domain databases

Gene3D2.60.120.200. 1 hit.
InterProIPR013320. ConA-like_subgrp.
IPR011009. Kinase-like_dom.
IPR001611. Leu-rich_rpt.
IPR013210. LRR-contain_N2.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00560. LRR_1. 3 hits.
PF13855. LRR_8. 2 hits.
PF08263. LRRNT_2. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS51450. LRR. 17 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBRL2_ARATH
AccessionPrimary (citable) accession number: Q9ZPS9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: May 1, 1999
Last modified: June 11, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names