Y2913_ARATH
ID Y2913_ARATH Reviewed; 828 AA.
AC O64477; Q0WWZ4;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=G-type lectin S-receptor-like serine/threonine-protein kinase At2g19130;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At2g19130; ORFNames=T20K24.15;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-189.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AC002392; AAD12030.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06850.1; -; Genomic_DNA.
DR EMBL; AK226189; BAE98354.1; -; mRNA.
DR PIR; T00534; T00534.
DR RefSeq; NP_179503.1; NM_127470.4.
DR AlphaFoldDB; O64477; -.
DR SMR; O64477; -.
DR BioGRID; 1787; 1.
DR IntAct; O64477; 1.
DR STRING; 3702.AT2G19130.1; -.
DR iPTMnet; O64477; -.
DR PaxDb; O64477; -.
DR PRIDE; O64477; -.
DR ProteomicsDB; 232353; -.
DR EnsemblPlants; AT2G19130.1; AT2G19130.1; AT2G19130.
DR GeneID; 816430; -.
DR Gramene; AT2G19130.1; AT2G19130.1; AT2G19130.
DR KEGG; ath:AT2G19130; -.
DR Araport; AT2G19130; -.
DR TAIR; locus:2059103; AT2G19130.
DR eggNOG; ENOG502QUMK; Eukaryota.
DR HOGENOM; CLU_000288_116_2_1; -.
DR InParanoid; O64477; -.
DR OMA; CTENAFT; -.
DR OrthoDB; 316208at2759; -.
DR PhylomeDB; O64477; -.
DR PRO; PR:O64477; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64477; baseline and differential.
DR Genevisible; O64477; 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; -; 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; IPR000858; S_locus_glycoprot_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR024171; SRK-like_kinase.
DR Pfam; PF01453; B_lectin; 1.
DR Pfam; PF08276; PAN_2; 1.
DR Pfam; PF00069; Pkinase; 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 2: Evidence at transcript 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..828
FT /note="G-type lectin S-receptor-like serine/threonine-
FT protein kinase At2g19130"
FT /id="PRO_0000401326"
FT TOPO_DOM 23..439
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 440..460
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 461..828
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 23..146
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DOMAIN 286..322
FT /note="EGF-like"
FT DOMAIN 341..422
FT /note="PAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 493..770
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 582..600
FT /note="CaM-binding"
FT /evidence="ECO:0000250"
FT REGION 796..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 619
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 499..507
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 521
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 653
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 815
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 290..302
FT /evidence="ECO:0000250"
FT DISULFID 296..310
FT /evidence="ECO:0000250"
FT DISULFID 372..394
FT /evidence="ECO:0000250"
FT DISULFID 376..382
FT /evidence="ECO:0000250"
SQ SEQUENCE 828 AA; 92342 MW; 467A9ADCFF8CA945 CRC64;
MVSFLTLTSF FFICFFIHGS SAVDTISGDF TLSGDQTIVS SDGTYEMGFF KPGSSSNFYI
GMWYKQLSQT ILWVANRDKA VSDKNSSVFK ISNGNLILLD GNYQTPVWST GLNSTSSVSA
LEAVLQDDGN LVLRTGGSSL SANVLWQSFD HPGDTWLPGV KIRLDKRTGK SQRLTSWKSL
EDPSPGLFSL ELDESTAYKI LWNGSNEYWS SGPWNPQSRI FDSVPEMRLN YIYNFSFFSN
TTDSYFTYSI YNQLNVSRFV MDVSGQIKQF TWLEGNKAWN LFWSQPRQQC QVYRYCGSFG
ICSDKSEPFC RCPQGFRPMS QKDWDLKDYS AGCVRKTELQ CSRGDINQFF RLPNMKLADN
SEVLTRTSLS ICASACQGDC SCKAYAYDEG SSKCLVWSKD VLNLQQLEDE NSEGNIFYLR
LAASDVPNVG ASGKSNNKGL IFGAVLGSLG VIVLVLLVVI LILRYRRRKR MRGEKGDGTL
SAFSYRELQN ATKNFSDKLG GGGFGSVFKG ALPDSSDIAV KRLEGISQGE KQFRTEVVTI
GTIQHVNLVR LRGFCSEGSK KLLVYDYMPN GSLDSHLFLN QVEEKIVLGW KLRFQIALGT
ARGLAYLHDE CRDCIIHCDI KPENILLDSQ FCPKVADFGL AKLVGRDFSR VLTTMRGTRG
YLAPEWISGV AITAKADVYS YGMMLFELVS GRRNTEQSEN EKVRFFPSWA ATILTKDGDI
RSLVDPRLEG DAVDIEEVTR ACKVACWCIQ DEESHRPAMS QVVQILEGVL EVNPPPFPRS
IQALVVSDED VVFFTESSSS SSHNSSQNHK HSSSSSSSKK MTNDNSSA
