GenomeNet

Database: UniProt
Entry: Q9ZT07
LinkDB: Q9ZT07
Original site: Q9ZT07 
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   16-JAN-2019, entry version 122.
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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
RT   kinase 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.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   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.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   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
RT   reference 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,
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   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC       protein 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};
CC   -!- WEB RESOURCE: Name=PlantP kinase Classification PPC;
CC       URL="http://plantsp.genomics.purdue.edu/family/class.html";
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   UniGene; At.51566; -.
DR   ProteinModelPortal; 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; ENOG410IGVG; Eukaryota.
DR   eggNOG; COG0515; LUCA.
DR   HOGENOM; HOG000116559; -.
DR   InParanoid; Q9ZT07; -.
DR   OMA; NASICKH; -.
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:0004674; F:protein serine/threonine kinase activity; ISS: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; 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; 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; 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; 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     18       {ECO:0000255}.
FT   CHAIN        19    833       G-type lectin S-receptor-like
FT                                serine/threonine-protein kinase RKS1.
FT                                /FTId=PRO_0000401299.
FT   TOPO_DOM     19    440       Extracellular. {ECO:0000255}.
FT   TRANSMEM    441    461       Helical. {ECO:0000255}.
FT   TOPO_DOM    462    833       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       19    144       Bulb-type lectin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00038}.
FT   DOMAIN      280    330       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      338    421       PAN. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00315}.
FT   DOMAIN      515    800       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND     521    529       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   REGION      604    621       CaM-binding. {ECO:0000250}.
FT   COMPBIAS      8     15       Poly-Phe.
FT   ACT_SITE    640    640       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159, ECO:0000255|PROSITE-
FT                                ProRule:PRU10027}.
FT   BINDING     543    543       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   MOD_RES     549    549       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9LPZ9}.
FT   MOD_RES     564    564       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9LPZ9}.
FT   MOD_RES     644    644       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9LPZ9}.
FT   MOD_RES     657    657       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9LPZ9}.
FT   MOD_RES     674    674       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9LPZ9}.
FT   MOD_RES     717    717       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9LPZ9}.
FT   MOD_RES     821    821       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9LPZ9}.
FT   CARBOHYD     79     79       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     92     92       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    100    100       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    109    109       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    228    228       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    256    256       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    363    363       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    376    376       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    284    296       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    290    306       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    308    329       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    369    396       {ECO:0000255|PROSITE-ProRule:PRU00315}.
FT   DISULFID    373    379       {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
//
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