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Database: UniProt
Entry: P93756
LinkDB: P93756
Original site: P93756 
ID   SD31_ARATH              Reviewed;         764 AA.
AC   P93756;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   13-FEB-2019, entry version 145.
DE   RecName: Full=G-type lectin S-receptor-like serine/threonine-protein kinase SD3-1;
DE            EC=2.7.11.1;
DE   AltName: Full=S-domain-3 (SD3) receptor kinase 1;
DE            Short=SD3-1;
DE   Flags: Precursor;
GN   Name=SD31; OrderedLocusNames=At2g41890; ORFNames=T11A7.1;
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
RA   Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
RA   Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
RA   Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
RA   Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
RA   Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:761-768(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, AND NOMENCLATURE.
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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
CC       type I membrane protein {ECO:0000250}.
CC   -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC       inactive.
CC   -!- WEB RESOURCE: Name=PlantP kinase Classification PPC;
CC       URL="http://plantsp.genomics.purdue.edu/family/class.html";
DR   EMBL; AC002339; AAM14823.1; -; Genomic_DNA.
DR   EMBL; U90439; AAB63553.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC10045.1; -; Genomic_DNA.
DR   PIR; D84847; D84847.
DR   RefSeq; NP_001318404.1; NM_001336946.1.
DR   UniGene; At.49579; -.
DR   ProteinModelPortal; P93756; -.
DR   SMR; P93756; -.
DR   STRING; 3702.AT2G41890.1; -.
DR   PaxDb; P93756; -.
DR   EnsemblPlants; AT2G41890.1; AT2G41890.1; AT2G41890.
DR   GeneID; 818789; -.
DR   Gramene; AT2G41890.1; AT2G41890.1; AT2G41890.
DR   KEGG; ath:AT2G41890; -.
DR   Araport; AT2G41890; -.
DR   TAIR; locus:2054326; AT2G41890.
DR   eggNOG; ENOG410IGRM; Eukaryota.
DR   eggNOG; ENOG4111B0F; LUCA.
DR   HOGENOM; HOG000090663; -.
DR   InParanoid; P93756; -.
DR   OMA; NQCDVFA; -.
DR   OrthoDB; 495597at2759; -.
DR   PhylomeDB; P93756; -.
DR   PRO; PR:P93756; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   Genevisible; P93756; 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: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; IBA:GO_Central.
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; -; 2.
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; IPR000858; S_locus_glycoprot_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR024171; SRK-like_kinase.
DR   Pfam; PF01453; B_lectin; 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   SUPFAM; SSF51110; SSF51110; 2.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50927; BULB_LECTIN; 2.
DR   PROSITE; PS50948; PAN; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Complete proteome; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Kinase; Lectin; Membrane;
KW   Nucleotide-binding; Receptor; Reference proteome; Repeat;
KW   Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     24       {ECO:0000255}.
FT   CHAIN        25    764       G-type lectin S-receptor-like
FT                                serine/threonine-protein kinase SD3-1.
FT                                /FTId=PRO_0000401304.
FT   TOPO_DOM     25    442       Extracellular. {ECO:0000255}.
FT   TRANSMEM    443    463       Helical. {ECO:0000255}.
FT   TOPO_DOM    464    764       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       25    151       Bulb-type lectin 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00038}.
FT   DOMAIN      154    279       Bulb-type lectin 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00038}.
FT   DOMAIN      283    320       EGF-like; atypical.
FT   DOMAIN      332    413       Apple. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00315}.
FT   DOMAIN      466    764       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND     508    516       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   REGION      586    603       CaM-binding. {ECO:0000250}.
FT   BINDING     526    526       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   CARBOHYD     92     92       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    198    198       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    248    248       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    301    301       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    353    353       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    423    423       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    287    298       {ECO:0000250}.
FT   DISULFID    293    308       {ECO:0000250}.
FT   DISULFID    332    413       {ECO:0000250}.
FT   DISULFID    365    388       {ECO:0000250}.
FT   DISULFID    369    375       {ECO:0000250}.
SQ   SEQUENCE   764 AA;  85857 MW;  A63B02B07CF18285 CRC64;
     MKMLRALLLC LSLVFFLAFQ IVVSEIQLGS KLVVGENTLW VSNNGDFALG FFNPPGLLNR
     FSIGIWFNSN SIPYDQRKVV WVAGAGVVVS DNSSYFELTR NGELVLFDSL LGVPVWNSKT
     NRFSVSSALL RDDGNLVLLK DREEIVWQSF GTPTDTLLPN QKFPAFEMLR AASENSRSSY
     YSLHLEDSGR LELRWESNIT FWSSGNEVVK KKKKKKNIGA VLTSEGALFL EDQDLMRPVW
     SVFGEDHNDT VKFRFLRLDR DGNLRMYSWN EDSRIWKPVW QAVENQCRVF ATCGSQVCSF
     NSSGYTECNC PFNAFVSVSD PKCLVPYQKP GCKSGFNMVK FKNLELYGIY PANDSVISQI
     SSQRCKKLCL ENSACTAVTY TNDGEPQCRM KLTRYISGYS DPSLSSISYV KTCLDPIAVD
     PNNVSKESPV TVTKSHSICI PCLVGATSTT LVLFLGFQLG IVVYIYRRKK KLAKKKAERF
     SKATNPKGVM IFSVDEIKAM TDNFDNNIGP QIFKGVMPEN ELVAVKEVEA TLTEERKFRS
     SASKIGTMHH KNLANLEGYC CELGRRFLVY EYAKNGSILD HIVDPLRSKK LTWRIRTDTC
     LSVAKALCYL HMECREFVSH GNLNCGNILL GEDLEAKLTE YGFGLCAADK DVEDFGKTVL
     ALITGRYEPE GVVSEWVYRE WIGGRKETVV DKGLEGCFDV EELERVLRIS FWCVQTDERL
     RPSMGEVVKV LEGTLSVDPP PPPFACARSS PTNSSESSQS LYEP
//
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