SD31_ARATH
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 03-AUG-2022, entry version 161.
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; 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=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., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis 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 reference
RT 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., 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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
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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 AlphaFoldDB; P93756; -.
DR SMR; P93756; -.
DR STRING; 3702.AT2G41890.1; -.
DR PaxDb; P93756; -.
DR PRIDE; P93756; -.
DR ProteomicsDB; 232754; -.
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; ENOG502QW3Z; Eukaryota.
DR HOGENOM; CLU_000288_116_2_1; -.
DR InParanoid; P93756; -.
DR OMA; QKICVAC; -.
DR OrthoDB; 495597at2759; -.
DR PhylomeDB; P93756; -.
DR PRO; PR:P93756; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P93756; baseline and differential.
DR Genevisible; P93756; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; IEA:UniProt.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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; 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 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; Disulfide bond; EGF-like domain; Glycoprotein;
KW Kinase; Lectin; Membrane; Nucleotide-binding; Receptor; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; Signal; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..764
FT /note="G-type lectin S-receptor-like serine/threonine-
FT protein kinase SD3-1"
FT /id="PRO_0000401304"
FT TOPO_DOM 25..442
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 443..463
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 464..764
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..151
FT /note="Bulb-type lectin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DOMAIN 154..279
FT /note="Bulb-type lectin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DOMAIN 283..320
FT /note="EGF-like; atypical"
FT DOMAIN 332..413
FT /note="Apple"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 466..764
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 586..603
FT /note="CaM-binding"
FT /evidence="ECO:0000250"
FT REGION 738..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..764
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 508..516
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 526
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 287..298
FT /evidence="ECO:0000250"
FT DISULFID 293..308
FT /evidence="ECO:0000250"
FT DISULFID 332..413
FT /evidence="ECO:0000250"
FT DISULFID 365..388
FT /evidence="ECO:0000250"
FT DISULFID 369..375
FT /evidence="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
