WAKLE_ARATH
ID WAKLE_ARATH Reviewed; 731 AA.
AC Q9S9M1; F4I2U0;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Wall-associated receptor kinase-like 5;
DE EC=2.7.11.-;
DE Flags: Precursor;
GN Name=WAKL5; OrderedLocusNames=At1g16160; ORFNames=T24D18.24;
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, INDUCTION, AND FUNCTION.
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).
CC -!- FUNCTION: Serine/threonine-protein kinase that may function as a
CC signaling receptor of extracellular matrix component. May be involved
CC in plant's response to pathogen infection.
CC {ECO:0000269|PubMed:14576286}.
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: Preferentially expressed in roots and flowers.
CC {ECO:0000269|PubMed:14576286}.
CC -!- INDUCTION: Induced by INA and wounding. {ECO:0000269|PubMed:14576286}.
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=AAF18511.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC010924; AAF18511.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE29414.2; -; Genomic_DNA.
DR PIR; D86296; D86296.
DR RefSeq; NP_173067.2; NM_101483.2.
DR AlphaFoldDB; Q9S9M1; -.
DR SMR; Q9S9M1; -.
DR STRING; 3702.AT1G16160.1; -.
DR PaxDb; Q9S9M1; -.
DR PRIDE; Q9S9M1; -.
DR ProteomicsDB; 242758; -.
DR EnsemblPlants; AT1G16160.1; AT1G16160.1; AT1G16160.
DR GeneID; 838185; -.
DR Gramene; AT1G16160.1; AT1G16160.1; AT1G16160.
DR KEGG; ath:AT1G16160; -.
DR Araport; AT1G16160; -.
DR eggNOG; ENOG502RMXX; Eukaryota.
DR HOGENOM; CLU_000288_43_5_1; -.
DR InParanoid; Q9S9M1; -.
DR OMA; PICENVA; -.
DR OrthoDB; 478727at2759; -.
DR PhylomeDB; Q9S9M1; -.
DR PRO; PR:Q9S9M1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9S9M1; baseline and differential.
DR Genevisible; Q9S9M1; 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..731
FT /note="Wall-associated receptor kinase-like 5"
FT /id="PRO_0000253309"
FT TOPO_DOM 27..360
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 382..731
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 432..705
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 285..342
FT /note="Atypical EGF-like"
FT REGION 709..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 557
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 438..446
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 460
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 505
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 591
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 596
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 604
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 124
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 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 287..300
FT /evidence="ECO:0000250"
FT DISULFID 322..333
FT /evidence="ECO:0000250"
FT DISULFID 328..342
FT /evidence="ECO:0000250"
SQ SEQUENCE 731 AA; 80741 MW; 7EE0CCBEDD93672A CRC64;
MKTKTYRFVC LVASVLTLQL MNGSSAATPP PPPNSKNSST SCNRTCGGIS IPFPFGIGGK
DCYLNGWYEV VCNATTSGSS GTTVPFLSRI NREVVNISLP EGNNEQYGVV HIKGPVTSLG
CSSNTSQVPQ KSLPDLNVTG KGSPYFITDE NRLVAVGCGT KALMTDIESE ILGCESSCKD
SKSSQEVTNL LCDGYKCCQA RIPVERPQAV GVNIESSGGD GCKVAFLSSK RYSPSNVTIP
EQFHAGGYVV VELGWYFATT DSRFRNPLGC INLTYSGSYL SGDSCLCEYG YFSEMSYRNC
YCSLGFTGNP YLRGGCIDND DCKGPNICEE GTCVNVPGGY RCDPKPKIIK PAKPLVLQGV
LLGLMGLLFL VVGTLGLIIF IKKRRRIISS RKFFKRNGGL LLKQQLTTTN DGNVDMSRLF
SSEELKKATD NFSVKRVLGK GSQGTVYKGM MVDGKIIAVK RSKVVDEDKL EKFINEIILL
SQINHRNIVK LIGCCLETEV PILVYEYIPN GDMFKRLHDE SDDYAMTWEV RLRIAIEIAG
ALTYMHSAAS FPIYHRDIKT TNILLDEKYG AKVSDFGTSR SVTIDQTHLT TMVAGTFGYM
DPEYFLSSQY TDKSDVYSFG VVLVELITGE KPLSRIRSEE GRGLATHFLE AMKENRVIDI
IDIRIKEESK LDQLMAVAKL ARKCLSRKGI KRPNMREASL ELERIRSSPE DLEAHIENDD
EEDQVMEISR E
