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Q9SKB2

- SBIR1_ARATH

UniProt

Q9SKB2 - SBIR1_ARATH

Protein

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

Gene

SOBIR1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    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

    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

    GO - Cellular componenti

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

    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 25-248, 305-640.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

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

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei285 – 30521HelicalSequence AnalysisAdd
    BLAST

    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.
    OMAiPECHYLV.
    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

    MAVPTGSANL FLRPLILAVL SFLLLSSFVS SVEWLDIDSS DLKALQVIET    50
    ELGVNSQRSS ASDVNPCGRR GVFCERRHSA TTGEYVLRVT RLVYRSRSLT 100
    GTISPVIGML SELKELTLSN NQLVNAVPVD ILSCKQLEVL DLRKNRFSGQ 150
    IPGNFSSLSR LRILDLSSNK LSGNLNFLKN LRNLENLSVA NNLFSGKIPE 200
    QIVSFHNLRF FDFSGNRYLE GPAPVMSSIK LQTSPHQTRH ILAETPTSSP 250
    TNKPNNSTTS KAPKGAPKPG KLKKKKKKSK KKKVAAWILG FVVGAIGGTI 300
    SGFVFSVLFK LIIQAIRGSE KPPGPSIFSP LIKKAEDLAF LENEEALASL 350
    EIIGRGGCGE VFKAELPGSN GKIIAVKKVI QPPKDADELT DEDSKFLNKK 400
    MRQIRSEINT VGHIRHRNLL PLLAHVSRPE CHYLVYEYME KGSLQDILTD 450
    VQAGNQELMW PARHKIALGI AAGLEYLHMD HNPRIIHRDL KPANVLLDDD 500
    MEARISDFGL AKAMPDAVTH ITTSHVAGTV GYIAPEFYQT HKFTDKCDIY 550
    SFGVILGILV IGKLPSDEFF QHTDEMSLIK WMRNIITSEN PSLAIDPKLM 600
    DQGFDEQMLL VLKIACYCTL DDPKQRPNSK DVRTMLSQIK H 641
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi C84726.
    RefSeqi NP_180747.1. NM_128746.3.
    UniGenei At.13945.
    At.75587.

    3D structure databases

    ProteinModelPortali Q9SKB2.
    SMRi Q9SKB2. Positions 25-248, 305-640.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 3093. 1 interaction.
    STRINGi 3702.AT2G31880.1-P.

    Proteomic databases

    PaxDbi Q9SKB2.
    PRIDEi Q9SKB2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT2G31880.1 ; AT2G31880.1 ; AT2G31880 .
    GeneIDi 817746.
    KEGGi ath:AT2G31880.

    Organism-specific databases

    GeneFarmi 2536. 55.
    TAIRi AT2G31880.

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000071072.
    InParanoidi Q9SKB2.
    OMAi PECHYLV.
    PhylomeDBi Q9SKB2.

    Enzyme and pathway databases

    BioCyci ARA:AT2G31880-MONOMER.

    Gene expression databases

    Genevestigatori Q9SKB2.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR001611. Leu-rich_rpt.
    IPR000719. Prot_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF13855. LRR_8. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS51450. LRR. 4 hits.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 98 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