GenomeNet

Database: UniProt
Entry: Q9T058
LinkDB: Q9T058
Original site: Q9T058 
ID   Y4119_ARATH             Reviewed;         849 AA.
AC   Q9T058; Q682D0;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   10-APR-2019, entry version 141.
DE   RecName: Full=G-type lectin S-receptor-like serine/threonine-protein kinase At4g11900;
DE            EC=2.7.11.1;
DE   Flags: Precursor;
GN   OrderedLocusNames=At4g11900; ORFNames=T26M18.110;
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
RA   Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
RA   Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
RA   Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
RA   Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
RA   Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
RA   Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
RA   Langham S.-A., McCullagh B., Bilham L., Robben J.,
RA   van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
RA   Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA   Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
RA   Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
RA   De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
RA   van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
RA   Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
RA   Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
RA   Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
RA   Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA   Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
RA   Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
RA   Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
RA   Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
RA   Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
RA   Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
RA   Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
RA   Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
RA   Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
RA   Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
RA   Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
RA   Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
RA   Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
RA   Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
RA   Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
RA   Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
RA   Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
RA   Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
RA   Chen E., Marra M.A., Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:769-777(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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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.,
RA   Hayashizaki Y., Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (SEP-2004) 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,
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9T058-1; Sequence=Displayed;
CC         Note=Derived from EST data. No experimental confirmation
CC         available.;
CC       Name=2;
CC         IsoId=Q9T058-2; Sequence=VSP_040157, VSP_040158;
CC         Note=No experimental confirmation available.;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC       protein kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- WEB RESOURCE: Name=PlantP kinase Classification PPC;
CC       URL="http://plantsp.genomics.purdue.edu/family/class.html";
DR   EMBL; AL078606; CAB44328.1; -; Genomic_DNA.
DR   EMBL; AL161533; CAB78233.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE83067.1; -; Genomic_DNA.
DR   EMBL; CP002687; ANM67245.1; -; Genomic_DNA.
DR   EMBL; CP002687; ANM67251.1; -; Genomic_DNA.
DR   EMBL; AK175437; BAD43200.1; -; mRNA.
DR   PIR; T09349; T09349.
DR   RefSeq; NP_001329085.1; NM_001340743.1. [Q9T058-2]
DR   RefSeq; NP_001329091.1; NM_001340747.1. [Q9T058-2]
DR   RefSeq; NP_192927.5; NM_117260.8. [Q9T058-1]
DR   UniGene; At.63693; -.
DR   ProteinModelPortal; Q9T058; -.
DR   SMR; Q9T058; -.
DR   STRING; 3702.AT4G11900.1; -.
DR   PaxDb; Q9T058; -.
DR   EnsemblPlants; AT4G11900.10; AT4G11900.10; AT4G11900. [Q9T058-2]
DR   EnsemblPlants; AT4G11900.1; AT4G11900.1; AT4G11900. [Q9T058-1]
DR   EnsemblPlants; AT4G11900.5; AT4G11900.5; AT4G11900. [Q9T058-2]
DR   GeneID; 826797; -.
DR   Gramene; AT4G11900.10; AT4G11900.10; AT4G11900. [Q9T058-2]
DR   Gramene; AT4G11900.1; AT4G11900.1; AT4G11900. [Q9T058-1]
DR   Gramene; AT4G11900.5; AT4G11900.5; AT4G11900. [Q9T058-2]
DR   KEGG; ath:AT4G11900; -.
DR   Araport; AT4G11900; -.
DR   TAIR; locus:2137010; AT4G11900.
DR   eggNOG; COG0515; LUCA.
DR   HOGENOM; HOG000116559; -.
DR   InParanoid; Q9T058; -.
DR   OrthoDB; 684563at2759; -.
DR   PhylomeDB; Q9T058; -.
DR   PRO; PR:Q9T058; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9T058; baseline and differential.
DR   Genevisible; Q9T058; 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:0045087; P:innate immune response; 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; -; 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; 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; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Cell membrane; Complete proteome;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Kinase; Lectin;
KW   Membrane; Nucleotide-binding; Phosphoprotein; Receptor;
KW   Reference proteome; Serine/threonine-protein kinase; Signal;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     26       {ECO:0000255}.
FT   CHAIN        27    849       G-type lectin S-receptor-like
FT                                serine/threonine-protein kinase
FT                                At4g11900.
FT                                /FTId=PRO_0000401327.
FT   TOPO_DOM     27    466       Extracellular. {ECO:0000255}.
FT   TRANSMEM    467    487       Helical. {ECO:0000255}.
FT   TOPO_DOM    488    849       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       27    180       Bulb-type lectin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00038}.
FT   DOMAIN      311    348       EGF-like.
FT   DOMAIN      368    447       PAN. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00315}.
FT   DOMAIN      537    822       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND     543    551       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   REGION      626    643       CaM-binding. {ECO:0000250}.
FT   ACT_SITE    662    662       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159, ECO:0000255|PROSITE-
FT                                ProRule:PRU10027}.
FT   BINDING     565    565       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   MOD_RES     571    571       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9LPZ9}.
FT   MOD_RES     666    666       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9LPZ9}.
FT   MOD_RES     679    679       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9LPZ9}.
FT   MOD_RES     696    696       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9LPZ9}.
FT   MOD_RES     837    837       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9LPZ9}.
FT   MOD_RES     844    844       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9LPZ9}.
FT   CARBOHYD    111    111       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    148    148       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    172    172       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    232    232       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    450    450       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    315    327       {ECO:0000250}.
FT   DISULFID    321    336       {ECO:0000250}.
FT   DISULFID    401    421       {ECO:0000250}.
FT   DISULFID    405    411       {ECO:0000250}.
FT   VAR_SEQ     624    626       DSL -> GEW (in isoform 2).
FT                                {ECO:0000303|Ref.3}.
FT                                /FTId=VSP_040157.
FT   VAR_SEQ     627    849       Missing (in isoform 2).
FT                                {ECO:0000303|Ref.3}.
FT                                /FTId=VSP_040158.
SQ   SEQUENCE   849 AA;  95816 MW;  E7D3DA5D0CA5D3DE CRC64;
     MQICKKNVFL LYYGVLVFLS FQVSSSTDTI STNQPLSGFE TIVSSGDIFE LGLFTPTPDT
     YDHRNYYIGM WYRHVSPQTI VWVANRESPL GGDASTYLLK ILDGNLILHD NISATRKSHT
     EGTSRRSPQK ISEGNLLFHE TVWSTGVNSS MSKDVQAVLF DSGNLVLRDG PNSSAAVLWQ
     SFDHPSDTWL PGGKIRLGSQ LFTSWESLID PSPGRYSLEF DPKLHSLVTV WNRSKSYWSS
     GPLYDWLQSF KGFPELQGTK LSFTLNMDES YITFSVDPQS RYRLVMGVSG QFMLQVWHVD
     LQSWRVILSQ PDNRCDVYNS CGSFGICNEN REPPPCRCVP GFKREFSQGS DDSNDYSGGC
     KRETYLHCYK RNDEFLPIEN MKLATDPTTA SVLTSGTFRT CASRCVADCS CQAYANDGNK
     CLVWTKDAFN LQQLDANKGH TFFLRLASSN ISTANNRKTE HSKGKSIVLP LVLASLVATA
     ACFVGLYCCI SSRIRRKKKQ RDEKHSRELL EGGLIDDAGE NMCYLNLHDI MVATNSFSRK
     KKLGEGGFGP VYKGKLPNGM EVAIKRLSKK SSQGLTEFKN EVVLIIKLQH KNLVRLLGYC
     VEGDEKLLIY EYMSNKSLDG LLFDSLKSRE LDWETRMKIV NGTTRGLQYL HEYSRLRIIH
     RDLKASNILL DDEMNPKISD FGTARIFGCK QIDDSTQRIV GTFGYMSPEY ALGGVISEKS
     DIYSFGVLLL EIISGKKATR FVHNDQKHSL IAYEWESWCE TKGVSIIDEP MCCSYSLEEA
     MRCIHIALLC VQDHPKDRPM ISQIVYMLSN DNTLPIPKQP TFSNVLNGDQ QLDYVFSINE
     ATQTELEAR
//
DBGET integrated database retrieval system