GenomeNet

Database: UniProt
Entry: Q9LMN8
LinkDB: Q9LMN8
Original site: Q9LMN8 
ID   WAK3_ARATH              Reviewed;         741 AA.
AC   Q9LMN8;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 2.
DT   13-FEB-2019, entry version 130.
DE   RecName: Full=Wall-associated receptor kinase 3;
DE            EC=2.7.11.-;
DE   Flags: Precursor;
GN   Name=WAK3; OrderedLocusNames=At1g21240; ORFNames=F16F4.8;
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   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=10380805; DOI=10.1023/A:1006197318246;
RA   He Z.-H., Cheeseman I., He D., Kohorn B.D.;
RT   "A cluster of five cell wall-associated receptor kinase genes, Wak1-5,
RT   are expressed in specific organs of Arabidopsis.";
RL   Plant Mol. Biol. 39:1189-1196(1999).
RN   [4]
RP   GENE FAMILY ORGANIZATION.
RX   PubMed=12068092; DOI=10.1104/pp.011028;
RA   Verica J.A., He Z.-H.;
RT   "The cell wall-associated kinase (WAK) and WAK-like kinase gene
RT   family.";
RL   Plant Physiol. 129:455-459(2002).
CC   -!- FUNCTION: Serine/threonine-protein kinase that may function as a
CC       signaling receptor of extracellular matrix component. Binding to
CC       pectin may have significance in the control of cell expansion,
CC       morphogenesis and development.
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   -!- 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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in green tissues such
CC       as stems and leaves. {ECO:0000269|PubMed:10380805}.
CC   -!- INDUCTION: Induced by INA. {ECO:0000269|PubMed:10380805}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC       protein kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF81358.1; 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; AC036104; AAF81358.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE30077.1; -; Genomic_DNA.
DR   PIR; F86345; F86345.
DR   RefSeq; NP_173547.1; NM_101977.2.
DR   ProteinModelPortal; Q9LMN8; -.
DR   SMR; Q9LMN8; -.
DR   BioGrid; 23958; 152.
DR   IntAct; Q9LMN8; 153.
DR   STRING; 3702.AT1G21240.1; -.
DR   PaxDb; Q9LMN8; -.
DR   PRIDE; Q9LMN8; -.
DR   EnsemblPlants; AT1G21240.1; AT1G21240.1; AT1G21240.
DR   GeneID; 838719; -.
DR   Gramene; AT1G21240.1; AT1G21240.1; AT1G21240.
DR   KEGG; ath:AT1G21240; -.
DR   Araport; AT1G21240; -.
DR   TAIR; locus:2014897; AT1G21240.
DR   eggNOG; ENOG410IM0I; Eukaryota.
DR   eggNOG; COG0515; LUCA.
DR   HOGENOM; HOG000116550; -.
DR   InParanoid; Q9LMN8; -.
DR   OMA; ISWEHRL; -.
DR   OrthoDB; 496739at2759; -.
DR   PhylomeDB; Q9LMN8; -.
DR   PRO; PR:Q9LMN8; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9LMN8; baseline and differential.
DR   Genevisible; Q9LMN8; 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:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR025287; WAK_GUB.
DR   Pfam; PF07645; EGF_CA; 1.
DR   Pfam; PF13947; GUB_WAK_bind; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00179; EGF_CA; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Calcium; Complete proteome; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Repeat;
KW   Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     23       {ECO:0000255}.
FT   CHAIN        24    741       Wall-associated receptor kinase 3.
FT                                /FTId=PRO_0000253302.
FT   TOPO_DOM     24    342       Extracellular. {ECO:0000255}.
FT   TRANSMEM    343    363       Helical. {ECO:0000255}.
FT   TOPO_DOM    364    741       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      245    292       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      293    334       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      415    698       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND     421    429       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   ACT_SITE    540    540       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159, ECO:0000255|PROSITE-
FT                                ProRule:PRU10027}.
FT   BINDING     443    443       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   MOD_RES     404    404       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:O48814}.
FT   MOD_RES     488    488       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:O48814}.
FT   MOD_RES     574    574       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:O48814}.
FT   MOD_RES     579    579       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:O48814}.
FT   MOD_RES     587    587       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:O48814}.
FT   CARBOHYD     37     37       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     59     59       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     78     78       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    100    100       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    103    103       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    141    141       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    192    192       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    199    199       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    232    232       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    246    246       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    261    261       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    266    266       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    303    303       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    328    328       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    249    264       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    258    275       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    277    291       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    297    310       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    304    319       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    321    333       {ECO:0000255|PROSITE-ProRule:PRU00076}.
SQ   SEQUENCE   741 AA;  82701 MW;  F647CFAB601503F3 CRC64;
     MKFQEGVFLV VIFFLAYTQL VKGQHQPRED CKLKCGNVTI EYPFGISTGC YYPGDDNFNL
     TCVVEEKLLL FGIIQVTNIS HSGHVSVLFE RFSECYEQKN ETNGTALGYQ LGSSFSLSSN
     NKFTLVGCNA LSLLSTFGKQ NYSTGCLSLC NSQPEANGRC NGVGCCTTED FSVPFDSDTF
     QFGSVRLRNQ VNNSLDLFNT SVYQFNPCTY AFLVEDGKFN FDSSKDLKNL RNVTRFPVAL
     DWSIGNQTCE QAGSTRICGK NSSCYNSTTR NGYICKCNEG YDGNPYRSEG CKDIDECISD
     THNCSDPKTC RNRDGGFDCK CPSGYDLNSS MSCTRPEYKR TRIFLVIIIG VLVLLLAAIC
     IQHATKQRKY TKLRRQFFEQ NGGGMLIQRL SGAGLSNIDF KIFTEEGMKE ATNGYDESRI
     LGQGGQGTVY KGILPDNTIV AIKKARLADS RQVDQFIHEV LVLSQINHRN VVKILGCCLE
     TEVPLLVYEF ITNGTLFDHL HGSIFDSSLT WEHRLRIAIE VAGTLAYLHS SASIPIIHRD
     IKTANILLDE NLTAKVADFG ASKLIPMDKE QLTTMVQGTL GYLDPEYYTT GLLNEKSDVY
     SFGVVLMELL SGQKALCFER PQASKHLVSY FVSATEENRL HEIIDDQVLN EDNLKEIQEA
     ARIAAECTRL MGEERPRMKE VAAKLEALRV EKTKHKWSDQ YPEENEHLIG GHILSAQGET
     SSSIGYDSIK NVAILDIETG R
//
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