WAK2_ARATH
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 03-AUG-2022, entry version 155.
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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; 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, are
RT 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 leaves
RT 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., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., 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., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis 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 reference
RT 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., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA 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=10.2307/3871278;
RA Wagner T.A., Kohorn B.D.;
RT "Wall-associated kinases are expressed throughout plant development and are
RT 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 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 pectin
CC may have significance in the control of cell expansion, morphogenesis
CC 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, ChEBI:CHEBI:30616,
CC 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 as
CC stems and leaves. Detected at organ junctions.
CC {ECO:0000269|PubMed:10380805}.
CC -!- DEVELOPMENTAL STAGE: Expressed in shoot and root apical meristems, and
CC in expanding leaves and sepals. {ECO:0000269|PubMed:11226187}.
CC -!- INDUCTION: Induced by INA and wounding. {ECO:0000269|PubMed:10380805,
CC ECO:0000269|PubMed:11226187}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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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 AlphaFoldDB; Q9LMP1; -.
DR SMR; Q9LMP1; -.
DR BioGRID; 23962; 6.
DR IntAct; Q9LMP1; 3.
DR STRING; 3702.AT1G21270.1; -.
DR PaxDb; Q9LMP1; -.
DR PRIDE; Q9LMP1; -.
DR ProteomicsDB; 242763; -.
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; ENOG502QQPF; Eukaryota.
DR HOGENOM; CLU_000288_43_5_1; -.
DR InParanoid; Q9LMP1; -.
DR OMA; KNITRTH; -.
DR OrthoDB; 496739at2759; -.
DR PhylomeDB; Q9LMP1; -.
DR PRO; PR:Q9LMP1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LMP1; baseline and differential.
DR Genevisible; Q9LMP1; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
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:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; 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:0006468; P:protein phosphorylation; IEA:InterPro.
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; 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; IPR045274; WAK-like.
DR InterPro; IPR025287; WAK_GUB.
DR PANTHER; PTHR27005; PTHR27005; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF13947; GUB_WAK_bind; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 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; Disulfide bond; EGF-like domain; Glycoprotein;
KW Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; Signal; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..732
FT /note="Wall-associated receptor kinase 2"
FT /id="PRO_0000253301"
FT TOPO_DOM 24..329
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 351..732
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 230..277
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 278..319
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 404..677
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 529
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 410..418
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 432
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 393
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 477
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 563
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 568
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 576
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 234..249
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 243..260
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 262..276
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 282..295
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 289..304
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 306..318
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CONFLICT 105
FT /note="Q -> R (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 545
FT /note="V -> A (in Ref. 1 and 2)"
FT /evidence="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
