SD11_ARATH
ID SD11_ARATH Reviewed; 815 AA.
AC O81833;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=G-type lectin S-receptor-like serine/threonine-protein kinase SD1-1;
DE EC=2.7.11.1;
DE AltName: Full=S-domain-1 (SD1) receptor kinase 1;
DE Short=SD1-1;
DE Flags: Precursor;
GN Name=SD11; OrderedLocusNames=At4g27300; ORFNames=M4I22.110;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
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 [3]
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).
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 -!- 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;
CC -!- SUBUNIT: Interacts with PUB9, PUB13 and PUB14.
CC {ECO:0000269|PubMed:18552232}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AL030978; CAA19724.1; -; Genomic_DNA.
DR EMBL; AL161566; CAB79585.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85322.1; -; Genomic_DNA.
DR PIR; T05754; T05754.
DR RefSeq; NP_194460.1; NM_118864.2.
DR AlphaFoldDB; O81833; -.
DR SMR; O81833; -.
DR STRING; 3702.AT4G27300.1; -.
DR iPTMnet; O81833; -.
DR PaxDb; O81833; -.
DR PRIDE; O81833; -.
DR ProteomicsDB; 232777; -.
DR EnsemblPlants; AT4G27300.1; AT4G27300.1; AT4G27300.
DR GeneID; 828838; -.
DR Gramene; AT4G27300.1; AT4G27300.1; AT4G27300.
DR KEGG; ath:AT4G27300; -.
DR Araport; AT4G27300; -.
DR TAIR; locus:2131694; AT4G27300.
DR eggNOG; ENOG502R6BG; Eukaryota.
DR HOGENOM; CLU_000288_116_5_1; -.
DR InParanoid; O81833; -.
DR OMA; WNISRGA; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; O81833; -.
DR PRO; PR:O81833; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O81833; baseline and differential.
DR Genevisible; O81833; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI: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; 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; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Disulfide bond; EGF-like domain; Glycoprotein;
KW Kinase; Lectin; Membrane; Nucleotide-binding; Phosphoprotein; Receptor;
KW Reference proteome; Serine/threonine-protein kinase; Signal; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..815
FT /note="G-type lectin S-receptor-like serine/threonine-
FT protein kinase SD1-1"
FT /id="PRO_0000401300"
FT TOPO_DOM 23..438
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 460..815
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..152
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DOMAIN 288..326
FT /note="EGF-like"
FT DOMAIN 345..428
FT /note="PAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 500..783
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 589..606
FT /note="CaM-binding"
FT /evidence="ECO:0000250"
FT ACT_SITE 625
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 506..514
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 528
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 534
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 642
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 659
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 797
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 803
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 810
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 292..304
FT /evidence="ECO:0000250"
FT DISULFID 298..314
FT /evidence="ECO:0000250"
FT DISULFID 378..403
FT /evidence="ECO:0000250"
FT DISULFID 382..388
FT /evidence="ECO:0000250"
SQ SEQUENCE 815 AA; 91875 MW; 04694DBD5DD8017E CRC64;
MREIHSLFSL SLFLISSSLS VALDYNVITP KEFLKDGDTL SSPDQVFQLG FFSLDQEEQP
QHRFLGLWYM EPFAVVWVAN RNNPLYGTSG FLNLSSLGDL QLFDGEHKAL WSSSSSSTKA
SKTANNPLLK ISCSGNLISS DGEEAVLWQS FDYPMNTILA GMKLGKNFKT QMEWSLSSWK
TLKDPSPGDF TLSLDTRGLP QLILRKNGDS SYSYRLGSWN GLSFTGAPAM GRENSLFDYK
FTSSAQEVNY SWTPRHRIVS RLVLNNTGKL HRFIQSKQNQ WILANTAPED ECDYYSICGA
YAVCGINSKN TPSCSCLQGF KPKSGRKWNI SRGAYGCVHE IPTNCEKKDA FVKFPGLKLP
DTSWSWYDAK NEMTLEDCKI KCSSNCSCTA YANTDIREGG KGCLLWFGDL VDMREYSSFG
QDVYIRMGFA KIEFKGREVV GMVVGSVVAI AVVLVVVFAC FRKKIMKRYR GENFRKGIEE
EDLDLPIFDR KTISIATDDF SYVNFLGRGG FGPVYKGKLE DGQEIAVKRL SANSGQGVEE
FKNEVKLIAK LQHRNLVRLL GCCIQGEECM LIYEYMPNKS LDFFIFDERR STELDWKKRM
NIINGVARGI LYLHQDSRLR IIHRDLKAGN VLLDNDMNPK ISDFGLAKSF GGDQSESSTN
RVVGTYGYMP PEYAIDGHFS VKSDVFSFGV LVLEIITGKT NRGFRHADHD LNLLGHVWKM
WVEDREIEVP EEEWLEETSV IPEVLRCIHV ALLCVQQKPE DRPTMASVVL MFGSDSSLPH
PTQPGFFTNR NVPDISSSLS LRSQNEVSIT MLQGR
