RKS1_ARATH
ID RKS1_ARATH Reviewed; 833 AA.
AC Q9ZT07; F4I8U7; Q9LQ00; Q9SXB9;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 3.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=G-type lectin S-receptor-like serine/threonine-protein kinase RKS1;
DE EC=2.7.11.1;
DE AltName: Full=Receptor-like protein kinase 1;
DE Flags: Precursor;
GN Name=RKS1; OrderedLocusNames=At1g11340; ORFNames=T23J18.1, T28P6.1;
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 [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11100776; DOI=10.1093/pcp/pcd028;
RA Ohtake Y., Takahashi T., Komeda Y.;
RT "Salicylic acid induces the expression of a number of receptor-like kinase
RT genes in Arabidopsis thaliana.";
RL Plant Cell Physiol. 41:1038-1044(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC95352.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAD49988.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF16651.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF084035; AAC95352.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC007259; AAD49988.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC011661; AAF16651.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28720.2; -; Genomic_DNA.
DR PIR; E86247; E86247.
DR RefSeq; NP_172601.3; NM_101007.3.
DR AlphaFoldDB; Q9ZT07; -.
DR SMR; Q9ZT07; -.
DR STRING; 3702.AT1G11340.1; -.
DR PaxDb; Q9ZT07; -.
DR PRIDE; Q9ZT07; -.
DR EnsemblPlants; AT1G11340.1; AT1G11340.1; AT1G11340.
DR GeneID; 837676; -.
DR Gramene; AT1G11340.1; AT1G11340.1; AT1G11340.
DR KEGG; ath:AT1G11340; -.
DR Araport; AT1G11340; -.
DR eggNOG; ENOG502QUDG; Eukaryota.
DR HOGENOM; CLU_000288_116_5_1; -.
DR InParanoid; Q9ZT07; -.
DR OMA; MDQESYN; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9ZT07; -.
DR PRO; PR:Q9ZT07; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9ZT07; baseline and differential.
DR Genevisible; Q9ZT07; 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: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; 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; IPR000742; EGF-like_dom.
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; 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; 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; PS50026; EGF_3; 1.
DR PROSITE; PS50948; PAN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..833
FT /note="G-type lectin S-receptor-like serine/threonine-
FT protein kinase RKS1"
FT /id="PRO_0000401299"
FT TOPO_DOM 19..440
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..461
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 462..833
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 19..144
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DOMAIN 280..330
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 338..421
FT /note="PAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 515..800
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 604..621
FT /note="CaM-binding"
FT /evidence="ECO:0000250"
FT ACT_SITE 640
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 521..529
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 543
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 549
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 564
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 644
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 657
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 674
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 717
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 821
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 284..296
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 290..306
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 308..329
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 369..396
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DISULFID 373..379
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
SQ SEQUENCE 833 AA; 94891 MW; B115D57CD2D95B7D CRC64;
MKVVFVIFFF FLFQFCISVD TIMRRQSLRD GEVILSAGKR FAFGFFSLGD SELRYVGIWY
AQISQQTIVW VANRDHPIND TSGMVKFSNR GNLSVYASDN ETELIWSTNV SDSMLEPTLV
ATLSDLGNLV LFDPVTGRSF WESFDHPTDT FLPFMRLGFT RKDGLDRSLT SWKSHGDPGS
GDLILRMERR GFPQLILYKG VTPWWRMGSW TGHRWSGVPE MPIGYIFNNS FVNNEDEVSF
TYGVTDASVI TRTMVNETGT MHRFTWIARD KRWNDFWSVP KEQCDNYAHC GPNGYCDSPS
SKTFECTCLP GFEPKFPRHW FLRDSSGGCT KKKRASICSE KDGFVKLKRM KIPDTSDASV
DMNITLKECK QRCLKNCSCV AYASAYHESK RGAIGCLKWH GGMLDARTYL NSGQDFYIRV
DKEELARWNR NGLSGKRRVL LILISLIAAV MLLTVILFCV VRERRKSNRH RSSSANFAPV
PFDFDESFRF EQDKARNREL PLFDLNTIVA ATNNFSSQNK LGAGGFGPVY KGVLQNRMEI
AVKRLSRNSG QGMEEFKNEV KLISKLQHRN LVRILGCCVE LEEKMLVYEY LPNKSLDYFI
FHEEQRAELD WPKRMEIVRG IARGILYLHQ DSRLRIIHRD LKASNILLDS EMIPKISDFG
MARIFGGNQM EGCTSRVVGT FGYMAPEYAM EGQFSIKSDV YSFGVLMLEI ITGKKNSAFH
EESSNLVGHI WDLWENGEAT EIIDNLMDQE TYDEREVMKC IQIGLLCVQE NASDRVDMSS
VVIMLGHNAT NLPNPKHPAF TSARRRGGEN GACLKGQTGI SVNDVTFSDI QGR
