WAK3_ARATH
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 03-AUG-2022, entry version 146.
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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; 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., 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 [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 reference
RT 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, are
RT 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 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.
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. {ECO:0000269|PubMed:10380805}.
CC -!- INDUCTION: Induced by INA. {ECO:0000269|PubMed:10380805}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF81358.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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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 AlphaFoldDB; Q9LMN8; -.
DR SMR; Q9LMN8; -.
DR BioGRID; 23958; 152.
DR IntAct; Q9LMN8; 153.
DR STRING; 3702.AT1G21240.1; -.
DR PaxDb; Q9LMN8; -.
DR PRIDE; Q9LMN8; -.
DR ProteomicsDB; 242674; -.
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; ENOG502QQPF; Eukaryota.
DR HOGENOM; CLU_000288_43_5_1; -.
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: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:0006468; P:protein phosphorylation; IEA:InterPro.
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 2: Evidence at transcript 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..741
FT /note="Wall-associated receptor kinase 3"
FT /id="PRO_0000253302"
FT TOPO_DOM 24..342
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 364..741
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 245..292
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 293..334
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 415..698
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 540
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 421..429
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 443
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 404
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 488
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 574
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 579
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 587
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 232
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 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 249..264
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 258..275
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 277..291
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 297..310
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 304..319
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 321..333
FT /evidence="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
