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WAKLM_ARATH
ID   WAKLM_ARATH             Reviewed;         786 AA.
AC   Q9M092;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 2.
DT   03-AUG-2022, entry version 154.
DE   RecName: Full=Wall-associated receptor kinase-like 17;
DE            EC=2.7.11.-;
DE   Flags: Precursor;
GN   Name=WAKL17; OrderedLocusNames=At4g31100; ORFNames=F6E21.20;
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
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).
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:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
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=CAB79828.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL049914; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL161578; CAB79828.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE85856.1; -; Genomic_DNA.
DR   PIR; T10664; T10664.
DR   RefSeq; NP_194839.2; NM_119260.4.
DR   AlphaFoldDB; Q9M092; -.
DR   SMR; Q9M092; -.
DR   BioGRID; 14524; 3.
DR   IntAct; Q9M092; 2.
DR   STRING; 3702.AT4G31100.1; -.
DR   iPTMnet; Q9M092; -.
DR   PaxDb; Q9M092; -.
DR   PRIDE; Q9M092; -.
DR   ProteomicsDB; 242572; -.
DR   EnsemblPlants; AT4G31100.1; AT4G31100.1; AT4G31100.
DR   GeneID; 829237; -.
DR   Gramene; AT4G31100.1; AT4G31100.1; AT4G31100.
DR   KEGG; ath:AT4G31100; -.
DR   Araport; AT4G31100; -.
DR   TAIR; locus:2126316; AT4G31100.
DR   eggNOG; ENOG502RMXX; Eukaryota.
DR   HOGENOM; CLU_000288_43_5_1; -.
DR   InParanoid; Q9M092; -.
DR   OMA; RYANCEC; -.
DR   OrthoDB; 478727at2759; -.
DR   PhylomeDB; Q9M092; -.
DR   PRO; PR:Q9M092; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9M092; baseline and differential.
DR   Genevisible; Q9M092; 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: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; 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   PANTHER; PTHR27005; PTHR27005; 1.
DR   Pfam; PF07645; EGF_CA; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF08488; WAK; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
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..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..786
FT                   /note="Wall-associated receptor kinase-like 17"
FT                   /id="PRO_0000253317"
FT   TOPO_DOM        31..369
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        370..390
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        391..786
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          444..719
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          301..362
FT                   /note="Atypical EGF-like"
FT   REGION          766..786
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        570
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         450..458
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         472
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         433
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   MOD_RES         517
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   MOD_RES         604
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   MOD_RES         609
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   MOD_RES         617
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   CARBOHYD        69
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        122
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        160
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        165
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        274
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        303..318
FT                   /evidence="ECO:0000250"
FT   DISULFID        340..353
FT                   /evidence="ECO:0000250"
FT   DISULFID        347..362
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   786 AA;  87304 MW;  1B2B4270326837A9 CRC64;
     MSYKNTNNSH LILFKLLLLL ILYSADLTAS SSCRSECGGC KCGGIAIPYP FGIGKGCYLE
     KSYEIECLNT SGKLVPFLSV ISKEVVSIHL PGRQSFGSVR VRSPITSAGC SSDGKDSAPV
     MNLTDSPFFV SDINNLVGVG CSSKVSLEHI KQNMVGCELN CSTTNASDSN SIPFFDKTGC
     SFSYTFAQVC TGNKPEDMGC DGRGCCQASL PREPQQVIGI RIESNDGKST TSGDCRVAFL
     TDEFFSLSKL TKPEQLHAKR YATLSLGWIM QTRNTSFVNS LACKIRKDTD TAYSNDQSIK
     CICDYTMSII SDIRYANCEC NLGYKGNPYD SDGCRDIDEC KENPKYCKET DTCVNFEGGY
     RCVGDKTKAI MIGAGTGFGV LVLVGGVWWL RKFLVKRRMA KRKKKFFKRN GGLLLQQELN
     TRQGVVEKAR IFTSKELEKA TENFSENRVL GHGGQGTVYK GMLVDGRTVA VKKSKVIDED
     KLQEFINEVV ILSQINHRHV VKLLGCCLET EVPILVYEFI INGNLFKHIH EEEADDYTMI
     WGMRLRIAVD IAGALSYLHS AASSPIYHRD IKSTNILLDE KYRAKVADFG TSRSVTIDQT
     HWTTVISGTV GYVDPEYYRS SQYTEKSDVY SFGVILAELI TGDKPVIMVQ NTQEIIALAE
     HFRVAMKERR LSDIMDARIR DDSKPEQVMA VANLAMKCLS SRGRNRPNMR EVFTELERIC
     TSPEDSQVQN RIDEEEEEDG VEEEEEVVTI VHRGDSWSIG VTAPASSIVA SPPSSDVEPL
     NPLLTW
 
 
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