GenomeNet

Database: UniProt
Entry: O81833
LinkDB: O81833
Original site: O81833 
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   13-FEB-2019, entry version 147.
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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.,
RA   Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
RA   Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
RA   Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
RA   Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
RA   Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
RA   Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
RA   Langham S.-A., McCullagh B., Bilham L., Robben J.,
RA   van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
RA   Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA   Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
RA   Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
RA   De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
RA   van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
RA   Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
RA   Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
RA   Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
RA   Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA   Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
RA   Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
RA   Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
RA   Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
RA   Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
RA   Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
RA   Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
RA   Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
RA   Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
RA   Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
RA   Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
RA   Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
RA   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.,
RA   Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
RA   Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
RA   Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
RA   Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
RA   Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
RA   Chen E., Marra M.A., Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis
RT   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
RT   reference 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.,
RA   Chilelli A., Goring D.R.;
RT   "Interactions between the S-domain receptor kinases and AtPUB-ARM E3
RT   ubiquitin ligases suggest a conserved signaling pathway in
RT   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,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC         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
CC       type I membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC       protein kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- WEB RESOURCE: Name=PlantP kinase Classification PPC;
CC       URL="http://plantsp.genomics.purdue.edu/family/class.html";
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   UniGene; At.32109; -.
DR   ProteinModelPortal; O81833; -.
DR   SMR; O81833; -.
DR   STRING; 3702.AT4G27300.1; -.
DR   iPTMnet; O81833; -.
DR   PaxDb; O81833; -.
DR   PRIDE; O81833; -.
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; ENOG410JXQH; Eukaryota.
DR   eggNOG; COG0515; LUCA.
DR   HOGENOM; HOG000116559; -.
DR   InParanoid; O81833; -.
DR   OMA; GRKWNIS; -.
DR   OrthoDB; 684563at2759; -.
DR   PhylomeDB; O81833; -.
DR   PRO; PR:O81833; -.
DR   Proteomes; UP000006548; Chromosome 4.
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; IDA: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: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; Pkinase_Tyr; 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; Complete proteome; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Kinase; Lectin; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
KW   Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     22       {ECO:0000255}.
FT   CHAIN        23    815       G-type lectin S-receptor-like
FT                                serine/threonine-protein kinase SD1-1.
FT                                /FTId=PRO_0000401300.
FT   TOPO_DOM     23    438       Extracellular. {ECO:0000255}.
FT   TRANSMEM    439    459       Helical. {ECO:0000255}.
FT   TOPO_DOM    460    815       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       25    152       Bulb-type lectin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00038}.
FT   DOMAIN      288    326       EGF-like.
FT   DOMAIN      345    428       PAN. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00315}.
FT   DOMAIN      500    783       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND     506    514       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   REGION      589    606       CaM-binding. {ECO:0000250}.
FT   ACT_SITE    625    625       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159, ECO:0000255|PROSITE-
FT                                ProRule:PRU10027}.
FT   BINDING     528    528       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   MOD_RES     534    534       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9LPZ9}.
FT   MOD_RES     642    642       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9LPZ9}.
FT   MOD_RES     659    659       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9LPZ9}.
FT   MOD_RES     797    797       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9LPZ9}.
FT   MOD_RES     803    803       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9LPZ9}.
FT   MOD_RES     810    810       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9LPZ9}.
FT   CARBOHYD     93     93       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    249    249       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    265    265       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    329    329       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    385    385       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    292    304       {ECO:0000250}.
FT   DISULFID    298    314       {ECO:0000250}.
FT   DISULFID    378    403       {ECO:0000250}.
FT   DISULFID    382    388       {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
//
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