WAKLF_ARATH
ID WAKLF_ARATH Reviewed; 642 AA.
AC Q8GXQ3; Q9S9M6;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Wall-associated receptor kinase-like 6;
DE EC=2.7.11.-;
DE Flags: Precursor;
GN Name=WAKL6; OrderedLocusNames=At1g16110; ORFNames=T24D18.19, T24D18_30;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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).
RN [5]
RP TISSUE SPECIFICITY, INDUCTION, AND SUBCELLULAR LOCATION.
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.
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:14576286}; Single-
CC pass type I membrane protein {ECO:0000269|PubMed:14576286}.
CC -!- TISSUE SPECIFICITY: Slightly expressed in the whole plant.
CC {ECO:0000269|PubMed:14576286}.
CC -!- INDUCTION: Induced by INA. {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=AAF18506.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC010924; AAF18506.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29410.1; -; Genomic_DNA.
DR EMBL; AK118105; BAC42733.1; -; mRNA.
DR PIR; G86295; G86295.
DR RefSeq; NP_173062.1; NM_101478.3.
DR AlphaFoldDB; Q8GXQ3; -.
DR SMR; Q8GXQ3; -.
DR STRING; 3702.AT1G16110.1; -.
DR PaxDb; Q8GXQ3; -.
DR PRIDE; Q8GXQ3; -.
DR EnsemblPlants; AT1G16110.1; AT1G16110.1; AT1G16110.
DR GeneID; 838180; -.
DR Gramene; AT1G16110.1; AT1G16110.1; AT1G16110.
DR KEGG; ath:AT1G16110; -.
DR Araport; AT1G16110; -.
DR TAIR; locus:2200527; AT1G16110.
DR eggNOG; ENOG502RMXX; Eukaryota.
DR HOGENOM; CLU_000288_43_5_1; -.
DR InParanoid; Q8GXQ3; -.
DR OMA; MIGCESS; -.
DR OrthoDB; 478727at2759; -.
DR PRO; PR:Q8GXQ3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8GXQ3; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009505; C:plant-type cell wall; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 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; 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..28
FT /evidence="ECO:0000255"
FT CHAIN 29..642
FT /note="Wall-associated receptor kinase-like 6"
FT /id="PRO_0000253310"
FT TOPO_DOM 29..357
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 358..378
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 379..642
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 432..642
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 289..346
FT /note="Atypical EGF-like"
FT ACT_SITE 559
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 593
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 598
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 606
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
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 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 291..304
FT /evidence="ECO:0000250"
FT DISULFID 326..337
FT /evidence="ECO:0000250"
FT DISULFID 332..346
FT /evidence="ECO:0000250"
FT CONFLICT 497
FT /note="E -> G (in Ref. 3; BAC42733)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 642 AA; 70817 MW; 9A8B76AC33DC89C1 CRC64;
MKKTKTYQVF CIAALSVLTL QLINGSSAAT PPPPNSNSST SCNRACGGVS IPFPFGIGKD
CYLNGWYEVI CNTSTSGSSG TTVPFLSRIN SEVVNISLPD GKKLYGVVHI KGPVTSLGCS
SSSSSSQVSE MSLPNLNVTG RGSPYFLTDE NCLVMVGCGT KALMKDIESE ILGCESSCED
SKSSEEVTNS KCDGYKCCQA RIPLERPQVI GINIENTSAT RGKEGCSVAF LTNKRYAPMN
VTEPEQFHAG GYAVVELGWY FDTSDSRYRN PLGCRNMTRY SSYSSFDKCS CEYDYFSGMS
YRICYCNYGY TGNPYLRHGC IDIDECEGHH NCGEGTCVNM PGTHSCEPKI TKPEKASVLQ
GVLISLGVLL FVLGILGLYK FIKKRTRIIR NKNFFKRNGG LLLKQQLITK NGNVDMSRIF
SSKELKKATD NFSMNRVLGQ GGQGTVYKGM LAEGRIVAVK RSKVVGEGKM EEFINEVVLL
SQINHRNIVK LLGCCLETEV PVLVYEYIPN GDLFKRLHEK SESNDYTMTW EVRLRIAIEI
AGALSYMHSA ASIPIYHRDI KTTNILLDEK YRAKVSDFGT SRSITIAQTH LTTLVAGTFG
YMDPEYFLSS QYTDKSDVYS FGVVLVELIT GEKPLSRKRI GN
