GenomeNet

Database: UniProt
Entry: Q9LMP1
LinkDB: Q9LMP1
Original site: Q9LMP1 
ID   WAK2_ARATH              Reviewed;         732 AA.
AC   Q9LMP1; Q9XGN2;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   13-FEB-2019, entry version 137.
DE   RecName: Full=Wall-associated receptor kinase 2;
DE            EC=2.7.11.-;
DE   Flags: Precursor;
GN   Name=WAK2; OrderedLocusNames=At1g21270; ORFNames=F16F4.5;
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 [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC   STRAIN=cv. Columbia;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Stracke R., Palme K.;
RT   "Signal peptide selection derived cDNAs from Arabidopsis thaliana
RT   leaves and guard cells.";
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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   [4]
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   [5]
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   [6]
RP   FUNCTION, INDUCTION, DEVELOPMENTAL STAGE, AND INTERACTION WITH PECTIN.
RX   PubMed=11226187; DOI=10.1105/tpc.13.2.303;
RA   Wagner T.A., Kohorn B.D.;
RT   "Wall-associated kinases are expressed throughout plant development
RT   and are required for cell expansion.";
RL   Plant Cell 13:303-318(2001).
RN   [7]
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. {ECO:0000269|PubMed:11226187}.
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. Detected at organ junctions.
CC       {ECO:0000269|PubMed:10380805}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in shoot and root apical meristems,
CC       and in expanding leaves and sepals. {ECO:0000269|PubMed:11226187}.
CC   -!- INDUCTION: Induced by INA and wounding.
CC       {ECO:0000269|PubMed:10380805, ECO:0000269|PubMed:11226187}.
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; AJ012423; CAB42872.1; -; mRNA.
DR   EMBL; AF083722; AAN60280.1; -; mRNA.
DR   EMBL; AC036104; AAF81355.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE30080.1; -; Genomic_DNA.
DR   EMBL; AY062531; AAL32609.1; -; mRNA.
DR   EMBL; BT010335; AAQ56778.1; -; mRNA.
DR   PIR; T52588; T52588.
DR   RefSeq; NP_173549.1; NM_101979.4.
DR   UniGene; At.21118; -.
DR   UniGene; At.23880; -.
DR   UniGene; At.69963; -.
DR   ProteinModelPortal; Q9LMP1; -.
DR   SMR; Q9LMP1; -.
DR   BioGrid; 23962; 6.
DR   IntAct; Q9LMP1; 2.
DR   STRING; 3702.AT1G21270.1; -.
DR   PaxDb; Q9LMP1; -.
DR   PRIDE; Q9LMP1; -.
DR   EnsemblPlants; AT1G21270.1; AT1G21270.1; AT1G21270.
DR   GeneID; 838723; -.
DR   Gramene; AT1G21270.1; AT1G21270.1; AT1G21270.
DR   KEGG; ath:AT1G21270; -.
DR   Araport; AT1G21270; -.
DR   TAIR; locus:2014912; AT1G21270.
DR   eggNOG; ENOG410IM0I; Eukaryota.
DR   eggNOG; COG0515; LUCA.
DR   HOGENOM; HOG000116550; -.
DR   InParanoid; Q9LMP1; -.
DR   OMA; CSASSIC; -.
DR   OrthoDB; 496739at2759; -.
DR   PhylomeDB; Q9LMP1; -.
DR   PRO; PR:Q9LMP1; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   Genevisible; Q9LMP1; 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   GO; GO:0009992; P:cellular water homeostasis; IDA:TAIR.
DR   GO; GO:0009311; P:oligosaccharide metabolic process; IMP:TAIR.
DR   GO; GO:0009751; P:response to salicylic acid; IDA:TAIR.
DR   GO; GO:0009826; P:unidimensional cell growth; IMP:TAIR.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
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   1: Evidence at protein 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    732       Wall-associated receptor kinase 2.
FT                                /FTId=PRO_0000253301.
FT   TOPO_DOM     24    329       Extracellular. {ECO:0000255}.
FT   TRANSMEM    330    350       Helical. {ECO:0000255}.
FT   TOPO_DOM    351    732       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      230    277       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      278    319       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      404    677       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND     410    418       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   ACT_SITE    529    529       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159, ECO:0000255|PROSITE-
FT                                ProRule:PRU10027}.
FT   BINDING     432    432       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   MOD_RES     393    393       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:O48814}.
FT   MOD_RES     477    477       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:O48814}.
FT   MOD_RES     563    563       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:O48814}.
FT   MOD_RES     568    568       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:O48814}.
FT   MOD_RES     576    576       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:O48814}.
FT   CARBOHYD     57     57       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     75     75       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    111    111       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    154    154       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    217    217       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    246    246       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    288    288       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    234    249       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    243    260       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    262    276       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    282    295       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    289    304       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    306    318       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   CONFLICT    105    105       Q -> R (in Ref. 1 and 2). {ECO:0000305}.
FT   CONFLICT    545    545       V -> A (in Ref. 1 and 2). {ECO:0000305}.
SQ   SEQUENCE   732 AA;  81644 MW;  5B1817EF8CA0BEF5 CRC64;
     MKVQEGLFVV AVFYLAYTQL VKGQPRKECQ TRCGNVAVEY PFGTSPGCYY PGDESFNLTC
     NEQEKLFFGN MPVINMSLSG QLRVRLVRSR VCYDSQGKQT DYIAQRTTLG NFTLSELNRF
     TVVGCNSYAF LRTSGVEKYS TGCISICDSA TTKNGSCSGE GCCQIPVPRG YSFVRVKPHS
     FHNHPTVHLF NPCTYAFLVE DGMFDFHALE DLNNLRNVTT FPVVLDWSIG DKTCKQVEYR
     GVCGGNSTCF DSTGGTGYNC KCLEGFEGNP YLPNGCQDIN ECISSRHNCS EHSTCENTKG
     SFNCNCPSGY RKDSLNSCTR KVRPEYFRWT QIFLGTTIGF SVIMLGISCL QQKIKHRKNT
     ELRQKFFEQN GGGMLIQRVS GAGPSNVDVK IFTEKGMKEA TNGYHESRIL GQGGQGTVYK
     GILPDNSIVA IKKARLGNRS QVEQFINEVL VLSQINHRNV VKVLGCCLET EVPLLVYEFI
     NSGTLFDHLH GSLYDSSLTW EHRLRIATEV AGSLAYLHSS ASIPIIHRDI KTANILLDKN
     LTAKVADFGA SRLIPMDKEQ LTTIVQGTLG YLDPEYYNTG LLNEKSDVYS FGVVLMELLS
     GQKALCFERP HCPKNLVSCF ASATKNNRFH EIIDGQVMNE DNQREIQEAA RIAAECTRLM
     GEERPRMKEV AAELEALRVK TTKYKWSDQY RETGEIEHLL GVQILSAQGE TSSSIGYDSI
     RNVTTLDIEA GR
//
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