WAKLD_ARATH
ID WAKLD_ARATH Reviewed; 761 AA.
AC Q9S9M2; F4I2T9;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Wall-associated receptor kinase-like 4;
DE EC=2.7.11.-;
DE Flags: Precursor;
GN Name=WAKL4; OrderedLocusNames=At1g16150; ORFNames=T24D18.23;
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 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).
RN [4]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=14576286; DOI=10.1104/pp.103.028530;
RA Verica J.A., Chae L., Tong H.-Y., Ingmire P., He Z.-H.;
RT "Tissue-specific and developmentally regulated expression of a cluster of
RT tandemly arrayed cell wall-associated kinase-like kinase genes in
RT Arabidopsis.";
RL Plant Physiol. 133:1732-1746(2003).
RN [5]
RP INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16286448; DOI=10.1104/pp.105.066910;
RA Hou X., Tong H.-Y., Selby J., Dewitt J., Peng X., He Z.-H.;
RT "Involvement of a cell wall-associated kinase, WAKL4, in Arabidopsis
RT mineral responses.";
RL Plant Physiol. 139:1704-1716(2005).
CC -!- FUNCTION: Serine/threonine-protein kinase that may function as a
CC signaling receptor of extracellular matrix component. Plays a role in
CC plant mineral nutrients response.
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:0000269|PubMed:16286448}; Single-
CC pass type I membrane protein {ECO:0000269|PubMed:16286448}.
CC -!- TISSUE SPECIFICITY: Expressed in the whole plant. Detected in root-
CC shoot junctions and lateral root initiation sites.
CC {ECO:0000269|PubMed:14576286}.
CC -!- INDUCTION: Induced by INA. Up-regulated in vascular tissues after
CC Na(+), K(+), Cu(2+), Ni(2+) or Zn(2+) exposure.
CC {ECO:0000269|PubMed:14576286, ECO:0000269|PubMed:16286448}.
CC -!- DOMAIN: The EGF-like region is specific to this family of proteins and
CC seems to consist of the C-terminal of an EGF-like domain fused to the
CC N-terminal of another one.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF18510.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC010924; AAF18510.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29413.2; -; Genomic_DNA.
DR PIR; C86296; C86296.
DR RefSeq; NP_001319018.1; NM_001332211.1.
DR AlphaFoldDB; Q9S9M2; -.
DR SMR; Q9S9M2; -.
DR BioGRID; 23424; 10.
DR IntAct; Q9S9M2; 10.
DR STRING; 3702.AT1G16150.1; -.
DR PaxDb; Q9S9M2; -.
DR PRIDE; Q9S9M2; -.
DR ProteomicsDB; 242686; -.
DR EnsemblPlants; AT1G16150.1; AT1G16150.1; AT1G16150.
DR GeneID; 838184; -.
DR Gramene; AT1G16150.1; AT1G16150.1; AT1G16150.
DR KEGG; ath:AT1G16150; -.
DR Araport; AT1G16150; -.
DR eggNOG; ENOG502RMXX; Eukaryota.
DR HOGENOM; CLU_000288_43_5_1; -.
DR InParanoid; Q9S9M2; -.
DR OMA; RSCYCNS; -.
DR OrthoDB; 478727at2759; -.
DR PhylomeDB; Q9S9M2; -.
DR PRO; PR:Q9S9M2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9S9M2; baseline and differential.
DR Genevisible; Q9S9M2; 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; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR013695; WAK.
DR InterPro; IPR045274; WAK-like.
DR InterPro; IPR025287; WAK_GUB.
DR PANTHER; PTHR27005; PTHR27005; 1.
DR Pfam; PF13947; GUB_WAK_bind; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF08488; WAK; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS01186; EGF_2; 1.
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; Disulfide bond; Glycoprotein; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..761
FT /note="Wall-associated receptor kinase-like 4"
FT /id="PRO_0000253308"
FT TOPO_DOM 27..349
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 371..761
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 424..697
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 278..339
FT /note="Atypical EGF-like"
FT REGION 701..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..727
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 549
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 430..438
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 452
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 497
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 583
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 588
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 596
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
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 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 280..293
FT /evidence="ECO:0000250"
FT DISULFID 316..330
FT /evidence="ECO:0000250"
FT DISULFID 325..339
FT /evidence="ECO:0000250"
SQ SEQUENCE 761 AA; 84670 MW; B7F497D254A61B26 CRC64;
MKKETQNLQC IPLVISVLSL FGVSSARKPP YLCNRVCGGI SIPFPFGIGG KECYLNPWYE
VVCNTTTSVP FLSRINRELV NIYLPDPTEY YSNGVVHIKG PVTSSGCSTG TSQPLTPQPL
NVAGQGSPYF LTDKNLLMAV GCNVKAVMMD VKSQIIGCES SCDERNSSSQ VVRNKICSGN
KCCQTRIPEG QPQVIGVNIE IPENKNTTEG GCKVAFLTSN KYSSLNVTEP EEFHSDGYAV
VELGWYFDTS DSRVLSPIGC MNVSDASQDG GYGSETICVC SYGYFSGFSY RSCYCNSMGY
AGNPFLPGGC VDIDECKLEI GRKRCKDQSC VNKPGWFTCE PKKPGQIKPV FQGVLIGSAL
LLFAFGIFGL YKFIKKQRRS SRMRVFFRRN GGMLLKQQLA RKEGNVEMSK IFSSNELEKA
TDNFNTNRVL GQGGQGTVYK GMLVDGRIVA VKRSKAMDED KVEEFINEVV VLAQINHRNI
VKLLGCCLET EVPVLVYEFV PNGDLCKRLR DECDDYIMTW EVRLHIAIEI AGALSYLHSA
ASFPIYHRDI KTTNILLDEK YQVKVSDFGT SRSVTIDQTH LTTQVAGTFG YVDPEYFQSS
KFTDKSDVYS FGVVLVELIT GKNPSSRVQS EENRGFAAHF VAAVKENRFL DIVDERIKDE
CNLDQVMAVA KLAKRCLNRK GKKRPNMREV SVELERIRSS SYKSEIHNDD DDDDDDDDED
DQAMELNIEE TWDVGMTAPA SMFNNGSPAS DVEPLVPLRT W
