Leucine-rich repeat receptor-like serine/threonine/tyrosine-protein kinase SOBIR1 precursor

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Q9SKB2 (SBIR1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 86. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Leucine-rich repeat receptor-like serine/threonine/tyrosine-protein kinase SOBIR1
EC=2.7.10.1
EC=2.7.11.1

Alternative name(s):
Protein EVERSHED
Protein SUPPRESSOR OF BIR1-1

Gene names

Name:	SOBIR1
Synonyms:	EVR
Ordered Locus Names:	At2g31880
ORF Names:	F20M17.8

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	641 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Dual specificity kinase acting on both serine/threonine- and tyrosine-containing substrates. Promotes the activation of plant defense and cell death. Functions as an inhibitor/regulator of abscission, probably by regulating membrane trafficking during abscission. Ref.8 Ref.9
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. Ref.9 ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.9
Subcellular location	Cell membrane; Single-pass type I membrane protein Ref.5 Ref.6 Ref.7 Ref.9.
Tissue specificity	Mostly present in leaves and flowers, with increasing expression in older flowers. Ref.9
Developmental stage	Expressed in floral organ abscission zones (AZs) prior to cell separation and subsequent shedding. Also present within the style of developing fruits, at the bases of cauline leaves, and in the stems of the first rosette leaves. Ref.9
Post-translational modification	Autophosphorylated on Ser, Thr and Tyr residues. Ref.9
Disruption phenotype	Suppresses BIR1 (bir1-1) disruption phenotype. When associated with AGD5/NEV disruption, premature shedding of floral organs and enlarge abscission zones. Ref.8 Ref.9
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Contains 5 LRR (leucine-rich) repeats. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Plant defense
Cellular component	Cell membrane Membrane
Domain	Leucine-rich repeat Repeat Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Receptor Serine/threonine-protein kinase Transferase Tyrosine-protein kinase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	defense response Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of floral organ abscission Inferred from genetic interaction Ref.9. Source: TAIR positive regulation of cell death Inferred from mutant phenotype Ref.8. Source: TAIR positive regulation of defense response Inferred from mutant phenotype Ref.8. Source: TAIR
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from direct assay Ref.6 Ref.7. Source: TAIR
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from direct assay Ref.9. Source: UniProtKB protein tyrosine kinase activity Inferred from direct assay Ref.9. Source: UniProtKB transmembrane receptor protein tyrosine kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 31

Potential

Chain

32 – 641

610

Leucine-rich repeat receptor-like serine/threonine/tyrosine-protein kinase SOBIR1

PRO_0000403355

Regions

Topological domain

32 – 284

253

Extracellular Potential

Transmembrane

285 – 305

Helical; Potential

Topological domain

306 – 641

336

Cytoplasmic Potential

Repeat

112 – 133

LRR 1

Repeat

136 – 159

LRR 2

Repeat

160 – 182

LRR 3

Repeat

183 – 205

LRR 4

Repeat

207 – 228

LRR 5

Domain

347 – 641

295

Protein kinase

Nucleotide binding

353 – 361

ATP By similarity

Compositional bias

261 – 283

Lys-rich

Sites

Active site

489

Proton acceptor By similarity

Binding site

377

ATP By similarity

Amino acid modifications

Glycosylation

154

N-linked (GlcNAc...) Potential

Glycosylation

186

N-linked (GlcNAc...) Potential

Glycosylation

256

N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis

129

V → M in sobir1-8; suppresses BIR1 (bir1-1) disruption phenotype. Ref.8

Mutagenesis

329

S → N in sobir1-4; suppresses BIR1 (bir1-1) disruption phenotype. Ref.8

Mutagenesis

356

G → R in sobir1-7; suppresses BIR1 (bir1-1) disruption phenotype. Ref.8

Mutagenesis

377

K → E: Loss of kinase activity. Ref.9

Mutagenesis

407

E → K in evr-2; loss of kinase activity. Ref.9

Mutagenesis

417

R → W in sobir1-9; suppresses BIR1 (bir1-1) disruption phenotype. Ref.8

Mutagenesis

455

N → D in sobir1-10; suppresses BIR1 (bir1-1) disruption phenotype. Ref.8

Mutagenesis

557

G → R in sobir1-5; suppresses BIR1 (bir1-1) disruption phenotype. Ref.8

Mutagenesis

575

E → K in sobir1-2; suppresses BIR1 (bir1-1) disruption phenotype. Ref.8

Mutagenesis

626

R → K in sobir1-6; suppresses BIR1 (bir1-1) disruption phenotype. Ref.8

Sequence conflict

112

E → V in AAL25569. Ref.3

Sequence conflict

490

L → S in AAL25569. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

Q9SKB2 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: C061139D4B52681C
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FASTA

641

71,111

        10         20         30         40         50         60 
MAVPTGSANL FLRPLILAVL SFLLLSSFVS SVEWLDIDSS DLKALQVIET ELGVNSQRSS 

        70         80         90        100        110        120 
ASDVNPCGRR GVFCERRHSA TTGEYVLRVT RLVYRSRSLT GTISPVIGML SELKELTLSN 

       130        140        150        160        170        180 
NQLVNAVPVD ILSCKQLEVL DLRKNRFSGQ IPGNFSSLSR LRILDLSSNK LSGNLNFLKN 

       190        200        210        220        230        240 
LRNLENLSVA NNLFSGKIPE QIVSFHNLRF FDFSGNRYLE GPAPVMSSIK LQTSPHQTRH 

       250        260        270        280        290        300 
ILAETPTSSP TNKPNNSTTS KAPKGAPKPG KLKKKKKKSK KKKVAAWILG FVVGAIGGTI 

       310        320        330        340        350        360 
SGFVFSVLFK LIIQAIRGSE KPPGPSIFSP LIKKAEDLAF LENEEALASL EIIGRGGCGE 

       370        380        390        400        410        420 
VFKAELPGSN GKIIAVKKVI QPPKDADELT DEDSKFLNKK MRQIRSEINT VGHIRHRNLL 

       430        440        450        460        470        480 
PLLAHVSRPE CHYLVYEYME KGSLQDILTD VQAGNQELMW PARHKIALGI AAGLEYLHMD 

       490        500        510        520        530        540 
HNPRIIHRDL KPANVLLDDD MEARISDFGL AKAMPDAVTH ITTSHVAGTV GYIAPEFYQT 

       550        560        570        580        590        600 
HKFTDKCDIY SFGVILGILV IGKLPSDEFF QHTDEMSLIK WMRNIITSEN PSLAIDPKLM 

       610        620        630        640 
DQGFDEQMLL VLKIACYCTL DDPKQRPNSK DVRTMLSQIK H

« Hide

References

	« Hide 'large scale' referencesShow '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. 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. Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-like protein kinase genes in Arabidopsis thaliana." Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J. BMC Genomics 11:19-19(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Arabidopsis plasma membrane proteomics identifies components of transport, signal transduction and membrane trafficking." Alexandersson E., Saalbach G., Larsson C., Kjellbom P. Plant Cell Physiol. 45:1543-1556(2004) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. Strain: cv. Columbia. Tissue: Leaf and Petiole.
[6]	"Quantitative phosphoproteomics of early elicitor signaling in Arabidopsis." Benschop J.J., Mohammed S., O'Flaherty M., Heck A.J.R., Slijper M., Menke F.L.H. Mol. Cell. Proteomics 6:1198-1214(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. Strain: cv. Columbia.
[7]	"A high content in lipid-modified peripheral proteins and integral receptor kinases features in the arabidopsis plasma membrane proteome." Marmagne A., Ferro M., Meinnel T., Bruley C., Kuhn L., Garin J., Barbier-Brygoo H., Ephritikhine G. Mol. Cell. Proteomics 6:1980-1996(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]	"Regulation of cell death and innate immunity by two receptor-like kinases in Arabidopsis." Gao M., Wang X., Wang D., Xu F., Ding X., Zhang Z., Bi D., Cheng Y.T., Chen S., Li X., Zhang Y. Cell Host Microbe 6:34-44(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF VAL-129; SER-329; GLY-356; ARG-417; ASN-455; GLY-557; GLU-575 AND ARG-626.
[9]	"The EVERSHED receptor-like kinase modulates floral organ shedding in Arabidopsis." Leslie M.E., Lewis M.W., Youn J.-Y., Daniels M.J., Liljegren S.J. Development 137:467-476(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE, AUTOPHOSPHORYLATION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, MUTAGENESIS OF LYS-377 AND GLU-407.
+	Additional computationally mapped references.

Web resources

PlantP kinase Classification PPC

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC006533 Genomic DNA. Translation: AAD32284.1. CP002685 Genomic DNA. Translation: AEC08599.1. AF370596 mRNA. Translation: AAK43915.1. AY058153 mRNA. Translation: AAL25569.1. FJ708707 mRNA. Translation: ACN59302.1.
IPI	IPI00522533.
PIR	C84726.
RefSeq	NP_180747.1. NM_128746.3.
UniGene	At.13945. At.75587.
3D structure databases
ProteinModelPortal	Q9SKB2.
SMR	Q9SKB2. Positions 25-232, 305-636.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT2G31880.1-P.
Proteomic databases
PaxDb	Q9SKB2.
PRIDE	Q9SKB2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT2G31880.1; AT2G31880.1; AT2G31880.
GeneID	817746.
KEGG	ath:AT2G31880.
Organism-specific databases
GeneFarm	2536. 55.
TAIR	At2g31880.
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000071072.
InParanoid	Q9SKB2.
OMA	IIGRGGC.
PhylomeDB	Q9SKB2.
ProtClustDB	CLSN2683270.
Gene expression databases
Genevestigator	Q9SKB2.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR001611. Leu-rich_rpt. IPR000719. Prot_kinase_cat_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS51450. LRR. 4 hits. PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SBIR1_ARATH

Accession

Primary (citable) accession number: Q9SKB2
Secondary accession number(s): Q93Z40

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2011
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents