WAK4_ARATH
ID WAK4_ARATH Reviewed; 738 AA.
AC Q9LMN6; O81819;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Wall-associated receptor kinase 4;
DE EC=2.7.11.-;
DE Flags: Precursor;
GN Name=WAK4; OrderedLocusNames=At1g21210; ORFNames=F16F4.10;
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 [GENOMIC DNA], AND TISSUE SPECIFICITY.
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 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 [3]
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 [4]
RP FUNCTION.
RX PubMed=11402163; DOI=10.2307/3871298;
RA Lally D., Ingmire P., Tong H.-Y., He Z.-H.;
RT "Antisense expression of a cell wall-associated protein kinase, WAK4,
RT inhibits cell elongation and alters morphology.";
RL Plant Cell 13:1317-1331(2001).
RN [5]
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:11402163}.
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: Strictly expressed in siliques.
CC {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; AJ009695; CAA08793.1; -; Genomic_DNA.
DR EMBL; AC036104; AAF81361.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30075.1; -; Genomic_DNA.
DR PIR; D86345; D86345.
DR RefSeq; NP_173544.1; NM_101974.3.
DR AlphaFoldDB; Q9LMN6; -.
DR SMR; Q9LMN6; -.
DR BioGRID; 23955; 8.
DR IntAct; Q9LMN6; 8.
DR STRING; 3702.AT1G21210.1; -.
DR PaxDb; Q9LMN6; -.
DR PRIDE; Q9LMN6; -.
DR EnsemblPlants; AT1G21210.1; AT1G21210.1; AT1G21210.
DR GeneID; 838716; -.
DR Gramene; AT1G21210.1; AT1G21210.1; AT1G21210.
DR KEGG; ath:AT1G21210; -.
DR Araport; AT1G21210; -.
DR TAIR; locus:2014952; AT1G21210.
DR eggNOG; ENOG502QQPF; Eukaryota.
DR HOGENOM; CLU_000288_43_5_1; -.
DR InParanoid; Q9LMN6; -.
DR OMA; CSASSIC; -.
DR OrthoDB; 496739at2759; -.
DR PhylomeDB; Q9LMN6; -.
DR PRO; PR:Q9LMN6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LMN6; baseline and differential.
DR Genevisible; Q9LMN6; 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:0048527; P:lateral root development; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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; 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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..738
FT /note="Wall-associated receptor kinase 4"
FT /id="PRO_0000253303"
FT TOPO_DOM 23..335
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 357..738
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 232..278
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 279..325
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 410..693
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 535
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 416..424
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 438
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 399
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 483
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 569
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 574
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 582
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 236..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..300
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 294..309
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 311..324
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 738 AA; 81704 MW; 3927EBC7C7F57267 CRC64;
MKVQRLFLVA IFCLSYMQLV KGQTLPRCPE KCGNVTLEYP FGFSPGCWRA EDPSFNLSCV
NENLFYKGLE VVEISHSSQL RVLYPASYIC YNSKGKFAKG TYYWSNLGNL TLSGNNTITA
LGCNSYAFVS SNGTRRNSVG CISACDALSH EANGECNGEG CCQNPVPAGN NWLIVRSYRF
DNDTSVQPIS EGQCIYAFLV ENGKFKYNAS DKYSYLQNRN VGFPVVLDWS IRGETCGQVG
EKKCGVNGIC SNSASGIGYT CKCKGGFQGN PYLQNGCQDI NECTTANPIH KHNCSGDSTC
ENKLGHFRCN CRSRYELNTT TNTCKPKGNP EYVEWTTIVL GTTIGFLVIL LAISCIEHKM
KNTKDTELRQ QFFEQNGGGM LMQRLSGAGP SNVDVKIFTE EGMKEATDGY DENRILGQGG
QGTVYKGILP DNSIVAIKKA RLGDNSQVEQ FINEVLVLSQ INHRNVVKLL GCCLETEVPL
LVYEFISSGT LFDHLHGSMF DSSLTWEHRL RMAVEIAGTL AYLHSSASIP IIHRDIKTAN
ILLDENLTAK VADFGASRLI PMDKEDLATM VQGTLGYLDP EYYNTGLLNE KSDVYSFGVV
LMELLSGQKA LCFERPQTSK HIVSYFASAT KENRLHEIID GQVMNENNQR EIQKAARIAV
ECTRLTGEER PGMKEVAAEL EALRVTKTKH KWSDEYPEQE DTEHLVGVQK LSAQGETSSS
IGYDSIRNVA ILDIEAGR
