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Database: UniProt
Entry: O64477
LinkDB: O64477
Original site: O64477 
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   10-APR-2019, entry version 145.
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; 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=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.,
RA   Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
RA   Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
RA   Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
RA   Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
RA   Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis
RT   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
RT   reference 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.,
RA   Hayashizaki Y., 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,
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   -!- WEB RESOURCE: Name=PlantP kinase Classification PPC;
CC       URL="http://plantsp.genomics.purdue.edu/family/class.html";
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   UniGene; At.39891; -.
DR   ProteinModelPortal; 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   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; ENOG410IFSD; Eukaryota.
DR   eggNOG; ENOG410YEQP; LUCA.
DR   HOGENOM; HOG000116559; -.
DR   InParanoid; O64477; -.
DR   OMA; YLLLWNG; -.
DR   OrthoDB; 316208at2759; -.
DR   PhylomeDB; O64477; -.
DR   PRO; PR:O64477; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   Genevisible; O64477; 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; 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; 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     22       {ECO:0000255}.
FT   CHAIN        23    828       G-type lectin S-receptor-like
FT                                serine/threonine-protein kinase
FT                                At2g19130.
FT                                /FTId=PRO_0000401326.
FT   TOPO_DOM     23    439       Extracellular. {ECO:0000255}.
FT   TRANSMEM    440    460       Helical. {ECO:0000255}.
FT   TOPO_DOM    461    828       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       23    146       Bulb-type lectin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00038}.
FT   DOMAIN      286    322       EGF-like.
FT   DOMAIN      341    422       PAN. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00315}.
FT   DOMAIN      493    770       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND     499    507       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   REGION      582    600       CaM-binding. {ECO:0000250}.
FT   COMPBIAS    797    827       Ser-rich.
FT   ACT_SITE    619    619       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159, ECO:0000255|PROSITE-
FT                                ProRule:PRU10027}.
FT   BINDING     521    521       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   MOD_RES     527    527       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9LPZ9}.
FT   MOD_RES     653    653       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9LPZ9}.
FT   MOD_RES     815    815       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9LPZ9}.
FT   CARBOHYD     85     85       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    113    113       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    203    203       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    234    234       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    240    240       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    255    255       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    290    302       {ECO:0000250}.
FT   DISULFID    296    310       {ECO:0000250}.
FT   DISULFID    372    394       {ECO:0000250}.
FT   DISULFID    376    382       {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
//
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