WAK5_ARATH
ID WAK5_ARATH Reviewed; 733 AA.
AC Q9LMN7;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Wall-associated receptor kinase 5;
DE EC=2.7.11.-;
DE Flags: Precursor;
GN Name=WAK5; OrderedLocusNames=At1g21230; ORFNames=F16F4.9;
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}.
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DR EMBL; AC036104; AAF81359.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30076.1; -; Genomic_DNA.
DR PIR; E86345; E86345.
DR RefSeq; NP_173546.1; NM_101976.2.
DR AlphaFoldDB; Q9LMN7; -.
DR SMR; Q9LMN7; -.
DR BioGRID; 23957; 1.
DR IntAct; Q9LMN7; 1.
DR STRING; 3702.AT1G21230.1; -.
DR PaxDb; Q9LMN7; -.
DR PRIDE; Q9LMN7; -.
DR ProteomicsDB; 242650; -.
DR EnsemblPlants; AT1G21230.1; AT1G21230.1; AT1G21230.
DR GeneID; 838718; -.
DR Gramene; AT1G21230.1; AT1G21230.1; AT1G21230.
DR KEGG; ath:AT1G21230; -.
DR Araport; AT1G21230; -.
DR TAIR; locus:2014962; AT1G21230.
DR eggNOG; ENOG502QQPF; Eukaryota.
DR HOGENOM; CLU_000288_43_5_1; -.
DR InParanoid; Q9LMN7; -.
DR OMA; SANICGW; -.
DR OrthoDB; 496739at2759; -.
DR PhylomeDB; Q9LMN7; -.
DR PRO; PR:Q9LMN7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LMN7; differential.
DR Genevisible; Q9LMN7; 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; 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..733
FT /note="Wall-associated receptor kinase 5"
FT /id="PRO_0000253304"
FT TOPO_DOM 24..330
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..351
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 352..733
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 231..278
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 279..321
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 408..691
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 533
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 414..422
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 436
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 397
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 481
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 567
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 572
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 580
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 218
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 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 235..250
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 244..261
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 263..277
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 283..296
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 290..305
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 307..320
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 733 AA; 82206 MW; 8040BFC89D3D39A7 CRC64;
MKVHSLFLMA IFFYLAYTQL VKAQPRDDCQ TRCGDVPIDY PFGISTGCYY PGDDSFNITC
EEDKPNVLSN IEVLNFNHSG QLRGLIPRST VCYDQQTNND FESLWFRLDN LSFSPNNKFT
LVGCNAWALL STFGIQNYST GCMSLCDTPP PPNSKCNGVG CCRTEVSIPL DSHRIETQPS
RFENMTSVEH FNPCSYAFFV EDGMFNFSSL EDLKDLRNVT RFPVLLDWSI GNQTCEQVVG
RNICGGNSTC FDSTRGKGYN CKCLQGFDGN PYLSDGCQDI NECTTRIHNC SDTSTCENTL
GSFHCQCPSG SDLNTTTMSC IDTPKEEPKY LGWTTVLLGT TIGFLIILLT ISYIQQKMRH
RKNTELRQQF FEQNGGGMLI QRLSGAGPSN VDVKIFTEEG MKEATDGYNE SRILGQGGQG
TVYKGILQDN SIVAIKKARL GDRSQVEQFI NEVLVLSQIN HRNVVKLLGC CLETEVPLLV
YEFISSGTLF DHLHGSMFDS SLTWEHRLRI AIEVAGTLAY LHSYASIPII HRDVKTANIL
LDENLTAKVA DFGASRLIPM DQEQLTTMVQ GTLGYLDPEY YNTGLLNEKS DVYSFGVVLM
ELLSGEKALC FERPQSSKHL VSYFVSAMKE NRLHEIIDGQ VMNEYNQREI QESARIAVEC
TRIMGEERPS MKEVAAELEA LRVKTTKHQW SDQYPKEVEH LLGVQILSTQ GDTSSIGYDS
IQNVTRLDIE TGR
