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Q9SKB2 (SBIR1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 97. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length641 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.7 Ref.8

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.8

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.8

Subcellular location

Cell membrane; Single-pass type I membrane protein Ref.5 Ref.6 Ref.8.

Tissue specificity

Mostly present in leaves and flowers, with increasing expression in older flowers. Ref.8

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.8

Post-translational modification

Autophosphorylated on Ser, Thr and Tyr residues. Ref.8

Disruption phenotype

Suppresses BIR1 (bir1-1) disruption phenotype. When associated with AGD5/NEV disruption, premature shedding of floral organs and enlarge abscission zones. Ref.7 Ref.8

Sequence similarities

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

Contains 5 LRR (leucine-rich) repeats.

Contains 1 protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential
Chain32 – 641610Leucine-rich repeat receptor-like serine/threonine/tyrosine-protein kinase SOBIR1
PRO_0000403355

Regions

Topological domain32 – 284253Extracellular Potential
Transmembrane285 – 30521Helical; Potential
Topological domain306 – 641336Cytoplasmic Potential
Repeat112 – 13322LRR 1
Repeat136 – 15924LRR 2
Repeat160 – 18223LRR 3
Repeat183 – 20523LRR 4
Repeat207 – 22822LRR 5
Domain347 – 641295Protein kinase
Nucleotide binding353 – 3619ATP By similarity
Compositional bias261 – 28323Lys-rich

Sites

Active site4891Proton acceptor By similarity
Binding site3771ATP By similarity

Amino acid modifications

Glycosylation1541N-linked (GlcNAc...) Potential
Glycosylation1861N-linked (GlcNAc...) Potential
Glycosylation2561N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis1291V → M in sobir1-8; suppresses BIR1 (bir1-1) disruption phenotype. Ref.7
Mutagenesis3291S → N in sobir1-4; suppresses BIR1 (bir1-1) disruption phenotype. Ref.7
Mutagenesis3561G → R in sobir1-7; suppresses BIR1 (bir1-1) disruption phenotype. Ref.7
Mutagenesis3771K → E: Loss of kinase activity. Ref.8
Mutagenesis4071E → K in evr-2; loss of kinase activity. Ref.8
Mutagenesis4171R → W in sobir1-9; suppresses BIR1 (bir1-1) disruption phenotype. Ref.7
Mutagenesis4551N → D in sobir1-10; suppresses BIR1 (bir1-1) disruption phenotype. Ref.7
Mutagenesis5571G → R in sobir1-5; suppresses BIR1 (bir1-1) disruption phenotype. Ref.7
Mutagenesis5751E → K in sobir1-2; suppresses BIR1 (bir1-1) disruption phenotype. Ref.7
Mutagenesis6261R → K in sobir1-6; suppresses BIR1 (bir1-1) disruption phenotype. Ref.7
Sequence conflict1121E → V in AAL25569. Ref.3
Sequence conflict4901L → S in AAL25569. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9SKB2 [UniParc].

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

FASTA64171,111
        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' 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]"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: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Strain: cv. Columbia.
Tissue: Leaf and Petiole.
[6]"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: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]"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.
[8]"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.

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.
PIRC84726.
RefSeqNP_180747.1. NM_128746.3.
UniGeneAt.13945.
At.75587.

3D structure databases

ProteinModelPortalQ9SKB2.
SMRQ9SKB2. Positions 25-248, 305-640.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid3093. 1 interaction.
STRING3702.AT2G31880.1-P.

Proteomic databases

PaxDbQ9SKB2.
PRIDEQ9SKB2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G31880.1; AT2G31880.1; AT2G31880.
GeneID817746.
KEGGath:AT2G31880.

Organism-specific databases

GeneFarm2536. 55.
TAIRAT2G31880.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000071072.
InParanoidQ9SKB2.
OMAPECHYLV.
PhylomeDBQ9SKB2.

Enzyme and pathway databases

BioCycARA:AT2G31880-MONOMER.

Gene expression databases

GenevestigatorQ9SKB2.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR001611. Leu-rich_rpt.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF13855. LRR_8. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS51450. LRR. 4 hits.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSBIR1_ARATH
AccessionPrimary (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: June 11, 2014
This is version 97 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