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Protein

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

Gene

SOBIR1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.1 PublicationPROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei377 – 3771ATPPROSITE-ProRule annotation
Active sitei489 – 4891Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi353 – 3619ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein serine/threonine kinase activity Source: UniProtKB
  3. protein tyrosine kinase activity Source: UniProtKB
  4. transmembrane receptor protein tyrosine kinase activity Source: UniProtKB-EC

GO - Biological processi

  1. defense response Source: UniProtKB-KW
  2. negative regulation of floral organ abscission Source: TAIR
  3. peptidyl-tyrosine phosphorylation Source: GOC
  4. positive regulation of cell death Source: TAIR
  5. positive regulation of defense response Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Serine/threonine-protein kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Plant defense

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT2G31880-MONOMER.

Names & Taxonomyi

Protein namesi
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 namesi
Name:SOBIR1
Synonyms:EVR
Ordered Locus Names:At2g31880
ORF Names:F20M17.8
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 2

Organism-specific databases

TAIRiAT2G31880.

Subcellular locationi

Cell membrane 3 Publications; Single-pass type I membrane protein 3 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini32 – 284253ExtracellularSequence AnalysisAdd
BLAST
Transmembranei285 – 30521HelicalSequence AnalysisAdd
BLAST
Topological domaini306 – 641336CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Suppresses BIR1 (bir1-1) disruption phenotype. When associated with AGD5/NEV disruption, premature shedding of floral organs and enlarge abscission zones.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi129 – 1291V → M in sobir1-8; suppresses BIR1 (bir1-1) disruption phenotype. 1 Publication
Mutagenesisi329 – 3291S → N in sobir1-4; suppresses BIR1 (bir1-1) disruption phenotype. 1 Publication
Mutagenesisi356 – 3561G → R in sobir1-7; suppresses BIR1 (bir1-1) disruption phenotype. 1 Publication
Mutagenesisi377 – 3771K → E: Loss of kinase activity. 1 Publication
Mutagenesisi407 – 4071E → K in evr-2; loss of kinase activity. 1 Publication
Mutagenesisi417 – 4171R → W in sobir1-9; suppresses BIR1 (bir1-1) disruption phenotype. 1 Publication
Mutagenesisi455 – 4551N → D in sobir1-10; suppresses BIR1 (bir1-1) disruption phenotype. 1 Publication
Mutagenesisi557 – 5571G → R in sobir1-5; suppresses BIR1 (bir1-1) disruption phenotype. 1 Publication
Mutagenesisi575 – 5751E → K in sobir1-2; suppresses BIR1 (bir1-1) disruption phenotype. 1 Publication
Mutagenesisi626 – 6261R → K in sobir1-6; suppresses BIR1 (bir1-1) disruption phenotype. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131Sequence AnalysisAdd
BLAST
Chaini32 – 641610Leucine-rich repeat receptor-like serine/threonine/tyrosine-protein kinase SOBIR1PRO_0000403355Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi154 – 1541N-linked (GlcNAc...)Sequence Analysis
Glycosylationi186 – 1861N-linked (GlcNAc...)Sequence Analysis
Glycosylationi256 – 2561N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Autophosphorylated on Ser, Thr and Tyr residues.

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ9SKB2.
PRIDEiQ9SKB2.

Expressioni

Tissue specificityi

Mostly present in leaves and flowers, with increasing expression in older flowers.1 Publication

Developmental stagei

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.1 Publication

Gene expression databases

GenevestigatoriQ9SKB2.

Interactioni

Protein-protein interaction databases

BioGridi3093. 1 interaction.
STRINGi3702.AT2G31880.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ9SKB2.
SMRiQ9SKB2. Positions 25-225, 305-640.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati112 – 13322LRR 1Add
BLAST
Repeati136 – 15924LRR 2Add
BLAST
Repeati160 – 18223LRR 3Add
BLAST
Repeati183 – 20523LRR 4Add
BLAST
Repeati207 – 22822LRR 5Add
BLAST
Domaini347 – 641295Protein kinasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi261 – 28323Lys-richAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
Contains 5 LRR (leucine-rich) repeats.Curated
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000071072.
InParanoidiQ9SKB2.
OMAiQHTSEMS.
PhylomeDBiQ9SKB2.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR001611. Leu-rich_rpt.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF13855. LRR_8. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51450. LRR. 4 hits.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9SKB2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAVPTGSANL FLRPLILAVL SFLLLSSFVS SVEWLDIDSS DLKALQVIET
60 70 80 90 100
ELGVNSQRSS ASDVNPCGRR GVFCERRHSA TTGEYVLRVT RLVYRSRSLT
110 120 130 140 150
GTISPVIGML SELKELTLSN NQLVNAVPVD ILSCKQLEVL DLRKNRFSGQ
160 170 180 190 200
IPGNFSSLSR LRILDLSSNK LSGNLNFLKN LRNLENLSVA NNLFSGKIPE
210 220 230 240 250
QIVSFHNLRF FDFSGNRYLE GPAPVMSSIK LQTSPHQTRH ILAETPTSSP
260 270 280 290 300
TNKPNNSTTS KAPKGAPKPG KLKKKKKKSK KKKVAAWILG FVVGAIGGTI
310 320 330 340 350
SGFVFSVLFK LIIQAIRGSE KPPGPSIFSP LIKKAEDLAF LENEEALASL
360 370 380 390 400
EIIGRGGCGE VFKAELPGSN GKIIAVKKVI QPPKDADELT DEDSKFLNKK
410 420 430 440 450
MRQIRSEINT VGHIRHRNLL PLLAHVSRPE CHYLVYEYME KGSLQDILTD
460 470 480 490 500
VQAGNQELMW PARHKIALGI AAGLEYLHMD HNPRIIHRDL KPANVLLDDD
510 520 530 540 550
MEARISDFGL AKAMPDAVTH ITTSHVAGTV GYIAPEFYQT HKFTDKCDIY
560 570 580 590 600
SFGVILGILV IGKLPSDEFF QHTDEMSLIK WMRNIITSEN PSLAIDPKLM
610 620 630 640
DQGFDEQMLL VLKIACYCTL DDPKQRPNSK DVRTMLSQIK H
Length:641
Mass (Da):71,111
Last modified:May 1, 2000 - v1
Checksum:iC061139D4B52681C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti112 – 1121E → V in AAL25569. (PubMed:14593172)Curated
Sequence conflicti490 – 4901L → S in AAL25569. (PubMed:14593172)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiC84726.
RefSeqiNP_180747.1. NM_128746.3.
UniGeneiAt.13945.
At.75587.

Genome annotation databases

EnsemblPlantsiAT2G31880.1; AT2G31880.1; AT2G31880.
GeneIDi817746.
KEGGiath:AT2G31880.

Cross-referencesi

Web resourcesi

PlantP kinase Classification PPC

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiC84726.
RefSeqiNP_180747.1. NM_128746.3.
UniGeneiAt.13945.
At.75587.

3D structure databases

ProteinModelPortaliQ9SKB2.
SMRiQ9SKB2. Positions 25-225, 305-640.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi3093. 1 interaction.
STRINGi3702.AT2G31880.1-P.

Proteomic databases

PaxDbiQ9SKB2.
PRIDEiQ9SKB2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G31880.1; AT2G31880.1; AT2G31880.
GeneIDi817746.
KEGGiath:AT2G31880.

Organism-specific databases

GeneFarmi2536. 55.
TAIRiAT2G31880.

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000071072.
InParanoidiQ9SKB2.
OMAiQHTSEMS.
PhylomeDBiQ9SKB2.

Enzyme and pathway databases

BioCyciARA:AT2G31880-MONOMER.

Gene expression databases

GenevestigatoriQ9SKB2.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR001611. Leu-rich_rpt.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF13855. LRR_8. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51450. LRR. 4 hits.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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.
    , 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.

Entry informationi

Entry nameiSBIR1_ARATH
AccessioniPrimary (citable) accession number: Q9SKB2
Secondary accession number(s): Q93Z40
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2011
Last sequence update: May 1, 2000
Last modified: February 4, 2015
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.