SD113_ARATH
ID SD113_ARATH Reviewed; 830 AA.
AC Q9LPZ9; Q9ZT06;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=G-type lectin S-receptor-like serine/threonine-protein kinase SD1-13;
DE EC=2.7.11.1;
DE AltName: Full=Calmodulin-binding receptor-like protein kinase 1;
DE AltName: Full=Receptor-like protein kinase 2;
DE AltName: Full=S-domain-1 (SD1) receptor kinase 13;
DE Short=SD1-13;
DE Flags: Precursor;
GN Name=SD113; Synonyms=CBRLK1, RKS2; OrderedLocusNames=At1g11350;
GN ORFNames=T23J18.2;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Ohtake Y., Takahashi T., Komeda Y.;
RT "Expression analysis of Arabidopsis thaliana genes encoding receptor-like
RT protein kinases.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [5]
RP GENE FAMILY, NOMENCLATURE, AND INTERACTION WITH PUB9; PUB13 AND PUB14.
RX PubMed=18552232; DOI=10.1104/pp.108.123380;
RA Samuel M.A., Mudgil Y., Salt J.N., Delmas F., Ramachandran S., Chilelli A.,
RA Goring D.R.;
RT "Interactions between the S-domain receptor kinases and AtPUB-ARM E3
RT ubiquitin ligases suggest a conserved signaling pathway in Arabidopsis.";
RL Plant Physiol. 147:2084-2095(2008).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INDUCTION BY BIOTIC
RP AND ABIOTIC STRESSES.
RX PubMed=19222996; DOI=10.1016/j.bbrc.2009.02.050;
RA Kim H.S., Jung M.S., Lee S.M., Kim K.E., Byun H., Choi M.S., Park H.C.,
RA Cho M.J., Chung W.S.;
RT "An S-locus receptor-like kinase plays a role as a negative regulator in
RT plant defense responses.";
RL Biochem. Biophys. Res. Commun. 381:424-428(2009).
RN [7]
RP SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, CATALYTIC ACTIVITY, INTERACTION
RP WITH CALMODULIN, IDENTIFICATION BY MASS SPECTROMETRY, AND PHOSPHORYLATION
RP AT THR-545; SER-546; SER-561; SER-641; SER-654; SER-670; THR-671; SER-714;
RP SER-715; SER-726; SER-805; SER-809; SER-810; SER-813; SER-818; SER-823;
RP THR-825 AND THR-828.
RX PubMed=19071125; DOI=10.1016/j.febslet.2008.11.046;
RA Kim H.S., Jung M.S., Lee K., Kim K.E., Yoo J.H., Kim M.C., Kim D.H.,
RA Cho M.J., Chung W.S.;
RT "An S-locus receptor-like kinase in plasma membrane interacts with
RT calmodulin in Arabidopsis.";
RL FEBS Lett. 583:36-42(2009).
CC -!- FUNCTION: Receptor-like serine/threonine-protein kinase that represses
CC the disease resistance signaling pathway triggered in response to
CC bacterial pathogen such as Pseudomonas syringae pv. tomato.
CC {ECO:0000269|PubMed:19222996}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:19071125};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:19071125};
CC -!- SUBUNIT: Interacts with PUB9, PUB13 and PUB14. Binds to calmodulin
CC (CaM) in a Ca(2+)-dependent manner. {ECO:0000269|PubMed:18552232,
CC ECO:0000269|PubMed:19071125}.
CC -!- INTERACTION:
CC Q9LPZ9; P25069: CAM5; NbExp=4; IntAct=EBI-8523200, EBI-1397259;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19071125};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:19071125}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in rosette leaves, and, to a lower
CC extent, in cauline leaves and stems. {ECO:0000269|PubMed:19222996}.
CC -!- INDUCTION: By P.syringae and salicylic acid (SA).
CC {ECO:0000269|PubMed:19222996}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:19071125}.
CC -!- DISRUPTION PHENOTYPE: Enhanced resistances to the virulent bacterial
CC pathogen P.syringae pv. tomato accompanied by an increase in PR1
CC expression. {ECO:0000269|PubMed:19222996}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF16650.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BX815523; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF084036; AAC95353.1; -; Genomic_DNA.
DR EMBL; AC011661; AAF16650.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28721.1; -; Genomic_DNA.
DR EMBL; BX815523; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_172602.1; NM_101008.3.
DR AlphaFoldDB; Q9LPZ9; -.
DR SMR; Q9LPZ9; -.
DR BioGRID; 22917; 3.
DR IntAct; Q9LPZ9; 4.
DR MINT; Q9LPZ9; -.
DR STRING; 3702.AT1G11350.1; -.
DR iPTMnet; Q9LPZ9; -.
DR PaxDb; Q9LPZ9; -.
DR PRIDE; Q9LPZ9; -.
DR ProteomicsDB; 232946; -.
DR EnsemblPlants; AT1G11350.1; AT1G11350.1; AT1G11350.
DR GeneID; 837677; -.
DR Gramene; AT1G11350.1; AT1G11350.1; AT1G11350.
DR KEGG; ath:AT1G11350; -.
DR Araport; AT1G11350; -.
DR TAIR; locus:2200151; AT1G11350.
DR eggNOG; ENOG502QSUU; Eukaryota.
DR HOGENOM; CLU_000288_116_1_1; -.
DR InParanoid; Q9LPZ9; -.
DR OMA; GANEQDC; -.
DR OrthoDB; 407794at2759; -.
DR PhylomeDB; Q9LPZ9; -.
DR PRO; PR:Q9LPZ9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LPZ9; baseline and differential.
DR Genevisible; Q9LPZ9; AT.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IDA:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0071446; P:cellular response to salicylic acid stimulus; IEP:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0048544; P:recognition of pollen; IEA:InterPro.
DR CDD; cd00028; B_lectin; 1.
DR Gene3D; 2.90.10.10; -; 1.
DR InterPro; IPR001480; Bulb-type_lectin_dom.
DR InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003609; Pan_app.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR021820; S-locus_recpt_kinase_C.
DR InterPro; IPR000858; S_locus_glycoprot_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR024171; SRK-like_kinase.
DR Pfam; PF01453; B_lectin; 1.
DR Pfam; PF11883; DUF3403; 1.
DR Pfam; PF08276; PAN_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00954; S_locus_glycop; 1.
DR PIRSF; PIRSF000641; SRK; 1.
DR SMART; SM00108; B_lectin; 1.
DR SMART; SM00473; PAN_AP; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF51110; SSF51110; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50927; BULB_LECTIN; 1.
DR PROSITE; PS50948; PAN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Calmodulin-binding; Cell membrane; Disulfide bond;
KW EGF-like domain; Glycoprotein; Kinase; Lectin; Membrane;
KW Nucleotide-binding; Phosphoprotein; Plant defense; Receptor;
KW Reference proteome; Serine/threonine-protein kinase; Signal; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..830
FT /note="G-type lectin S-receptor-like serine/threonine-
FT protein kinase SD1-13"
FT /id="PRO_0000401301"
FT TOPO_DOM 22..434
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 435..455
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 456..830
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 22..145
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DOMAIN 283..321
FT /note="EGF-like; atypical"
FT DOMAIN 340..423
FT /note="PAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 512..798
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 601..618
FT /note="CaM-binding"
FT REGION 789..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..830
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 637
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 518..526
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 540
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 545
FT /note="Phosphothreonine"
FT /evidence="ECO:0000305|PubMed:19071125"
FT MOD_RES 546
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:19071125"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:19071125"
FT MOD_RES 641
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19071125"
FT MOD_RES 654
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19071125"
FT MOD_RES 670
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19071125"
FT MOD_RES 671
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19071125"
FT MOD_RES 714
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:19071125"
FT MOD_RES 715
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:19071125"
FT MOD_RES 726
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:19071125"
FT MOD_RES 805
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:19071125"
FT MOD_RES 809
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:19071125"
FT MOD_RES 810
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:19071125"
FT MOD_RES 813
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:19071125"
FT MOD_RES 818
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:19071125"
FT MOD_RES 823
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:19071125"
FT MOD_RES 825
FT /note="Phosphothreonine"
FT /evidence="ECO:0000305|PubMed:19071125"
FT MOD_RES 828
FT /note="Phosphothreonine"
FT /evidence="ECO:0000305|PubMed:19071125"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 287..299
FT /evidence="ECO:0000250"
FT DISULFID 293..309
FT /evidence="ECO:0000250"
FT DISULFID 377..398
FT /evidence="ECO:0000250"
FT DISULFID 381..387
FT /evidence="ECO:0000250"
FT CONFLICT 313..314
FT /note="RG -> KR (in Ref. 1; AAC95353)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="Y -> N (in Ref. 1; AAC95353)"
FT /evidence="ECO:0000305"
FT CONFLICT 558
FT /note="V -> F (in Ref. 1; AAC95353)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 830 AA; 93234 MW; F1343BB026315BE8 CRC64;
MGCLLILLLT LICFSLRLCL ATDVITFSSE FRDSETVVSN HSTFRFGFFS PVNSTGRYAG
IWFNNIPVQT VVWVANSNSP INDSSGMVSI SKEGNLVVMD GRGQVHWSTN VLVPVAANTF
YARLLNTGNL VLLGTTNTGD EILWESFEHP QNIYLPTMSL ATDTKTGRSL KLRSWKSPFD
PSPGRYSAGL IPLPFPELVV WKDDLLMWRS GPWNGQYFIG LPNMDYRINL FELTLSSDNR
GSVSMSYAGN TLLYHFLLDS EGSVFQRDWN VAIQEWKTWL KVPSTKCDTY ATCGQFASCR
FNPGSTPPCM CIRGFKPQSY AEWNNGNWTQ GCVRKAPLQC ESRDNNDGSR KSDGFVRVQK
MKVPHNPQRS GANEQDCPES CLKNCSCTAY SFDRGIGCLL WSGNLMDMQE FSGTGVVFYI
RLADSEFKKR TNRSIVITVT LLVGAFLFAG TVVLALWKIA KHREKNRNTR LLNERMEALS
SNDVGAILVN QYKLKELPLF EFQVLAVATN NFSITNKLGQ GGFGAVYKGR LQEGLDIAVK
RLSRTSGQGV EEFVNEVVVI SKLQHRNLVR LLGFCIEGEE RMLVYEFMPE NCLDAYLFDP
VKQRLLDWKT RFNIIDGICR GLMYLHRDSR LKIIHRDLKA SNILLDENLN PKISDFGLAR
IFQGNEDEVS TVRVVGTYGY MAPEYAMGGL FSEKSDVFSL GVILLEIVSG RRNSSFYNDG
QNPNLSAYAW KLWNTGEDIA LVDPVIFEEC FENEIRRCVH VGLLCVQDHA NDRPSVATVI
WMLSSENSNL PEPKQPAFIP RRGTSEVESS GQSDPRASIN NVSLTKITGR
