GenomeNet

Database: UniProt
Entry: Q9XID3
LinkDB: Q9XID3
Original site: Q9XID3 
ID   Y1343_ARATH             Reviewed;         829 AA.
AC   Q9XID3;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   13-FEB-2019, entry version 152.
DE   RecName: Full=G-type lectin S-receptor-like serine/threonine-protein kinase At1g34300;
DE            EC=2.7.11.1;
DE   Flags: Precursor;
GN   OrderedLocusNames=At1g34300; ORFNames=F23M19.5;
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=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   [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].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE
RP   SCALE ANALYSIS].
RX   PubMed=17644812; DOI=10.1074/mcp.M700099-MCP200;
RA   Marmagne A., Ferro M., Meinnel T., Bruley C., Kuhn L., Garin J.,
RA   Barbier-Brygoo H., Ephritikhine G.;
RT   "A high content in lipid-modified peripheral proteins and integral
RT   receptor kinases features in the arabidopsis plasma membrane
RT   proteome.";
RL   Mol. Cell. Proteomics 6:1980-1996(2007).
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:0000305|PubMed:17644812};
CC       Single-pass type I membrane protein {ECO:0000305|PubMed:17644812}.
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; AC007454; AAD39605.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE31694.1; -; Genomic_DNA.
DR   EMBL; AY090246; AAL90909.1; -; mRNA.
DR   EMBL; BT001084; AAN46865.1; -; mRNA.
DR   PIR; B86467; B86467.
DR   RefSeq; NP_174690.1; NM_103152.4.
DR   UniGene; At.39767; -.
DR   ProteinModelPortal; Q9XID3; -.
DR   IntAct; Q9XID3; 2.
DR   STRING; 3702.AT1G34300.1; -.
DR   iPTMnet; Q9XID3; -.
DR   PaxDb; Q9XID3; -.
DR   PRIDE; Q9XID3; -.
DR   EnsemblPlants; AT1G34300.1; AT1G34300.1; AT1G34300.
DR   GeneID; 840330; -.
DR   Gramene; AT1G34300.1; AT1G34300.1; AT1G34300.
DR   KEGG; ath:AT1G34300; -.
DR   Araport; AT1G34300; -.
DR   TAIR; locus:2026155; AT1G34300.
DR   eggNOG; ENOG410IIJF; Eukaryota.
DR   eggNOG; COG0515; LUCA.
DR   HOGENOM; HOG000116559; -.
DR   InParanoid; Q9XID3; -.
DR   OMA; PWPTRFA; -.
DR   OrthoDB; 684563at2759; -.
DR   PhylomeDB; Q9XID3; -.
DR   PRO; PR:Q9XID3; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   Genevisible; Q9XID3; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
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   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; 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; PF00069; Pkinase; 1.
DR   Pfam; PF00954; S_locus_glycop; 1.
DR   PIRSF; PIRSF000641; SRK; 1.
DR   SMART; SM00108; B_lectin; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF51110; SSF51110; 2.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50927; BULB_LECTIN; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
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   Repeat; Serine/threonine-protein kinase; Signal; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     25       {ECO:0000255}.
FT   CHAIN        26    829       G-type lectin S-receptor-like
FT                                serine/threonine-protein kinase
FT                                At1g34300.
FT                                /FTId=PRO_0000401314.
FT   TOPO_DOM     26    421       Extracellular. {ECO:0000255}.
FT   TRANSMEM    422    442       Helical. {ECO:0000255}.
FT   TOPO_DOM    443    829       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       26    140       Bulb-type lectin 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00038}.
FT   DOMAIN      143    260       Bulb-type lectin 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00038}.
FT   DOMAIN      264    301       EGF-like.
FT   DOMAIN      317    399       Apple.
FT   DOMAIN      484    759       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND     490    498       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   REGION      572    589       CaM-binding. {ECO:0000250}.
FT   ACT_SITE    608    608       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159, ECO:0000255|PROSITE-
FT                                ProRule:PRU10027}.
FT   BINDING     512    512       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   MOD_RES     532    532       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9LPZ9}.
FT   MOD_RES     625    625       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9LPZ9}.
FT   MOD_RES     799    799       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9LPZ9}.
FT   CARBOHYD     46     46       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     98     98       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    130    130       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    151    151       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    172    172       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    178    178       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    189    189       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    195    195       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    283    283       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    320    320       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    416    416       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    268    280       {ECO:0000255|PROSITE-ProRule:PRU00038}.
FT   DISULFID    274    289       {ECO:0000255|PROSITE-ProRule:PRU00038}.
FT   DISULFID    317    399       {ECO:0000255|PROSITE-ProRule:PRU00038}.
FT   DISULFID    350    373       {ECO:0000255|PROSITE-ProRule:PRU00038}.
FT   DISULFID    354    360       {ECO:0000255|PROSITE-ProRule:PRU00038}.
SQ   SEQUENCE   829 AA;  91293 MW;  908A5438F177D197 CRC64;
     MAVKTPFLKL LPLLLLLLHF PFSFSTIPLG SVIYASGSNQ NWPSPNSTFS VSFVPSPSPN
     SFLAAVSFAG SVPIWSAGTV DSRGSLRLHT SGSLRLTNGS GTTVWDSKTD RLGVTSGSIE
     DTGEFILLNN RSVPVWSSFD NPTDTIVQSQ NFTAGKILRS GLYSFQLERS GNLTLRWNTS
     AIYWNHGLNS SFSSNLSSPR LSLQTNGVVS IFESNLLGGA EIVYSGDYGD SNTFRFLKLD
     DDGNLRIYSS ASRNSGPVNA HWSAVDQCLV YGYCGNFGIC SYNDTNPICS CPSRNFDFVD
     VNDRRKGCKR KVELSDCSGN TTMLDLVHTR LFTYEDDPNS ESFFAGSSPC RANCLSSVLC
     LASVSMSDGS GNCWQKHPGS FFTGYQWPSV PSTSYVKVCG PVVANTLERA TKGDDNNSKV
     HLWIVAVAVI AGLLGLVAVE IGLWWCCCRK NPRFGTLSSH YTLLEYASGA PVQFTYKELQ
     RCTKSFKEKL GAGGFGTVYR GVLTNRTVVA VKQLEGIEQG EKQFRMEVAT ISSTHHLNLV
     RLIGFCSQGR HRLLVYEFMR NGSLDNFLFT TDSAKFLTWE YRFNIALGTA KGITYLHEEC
     RDCIVHCDIK PENILVDDNF AAKVSDFGLA KLLNPKDNRY NMSSVRGTRG YLAPEWLANL
     PITSKSDVYS YGMVLLELVS GKRNFDVSEK TNHKKFSIWA YEEFEKGNTK AILDTRLSED
     QTVDMEQVMR MVKTSFWCIQ EQPLQRPTMG KVVQMLEGIT EIKNPLCPKT ISEVSFSGNS
     MSTSHASMFV ASGPTRSSSF SATRSFQTMG ITSSGPASTR ISEGSMLGS
//
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