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WAKLP_ARATH
ID   WAKLP_ARATH             Reviewed;         639 AA.
AC   Q9M342;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 2.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Wall-associated receptor kinase-like 15;
DE            EC=2.7.11.-;
DE   Flags: Precursor;
GN   Name=WAKL15; OrderedLocusNames=At3g53840; ORFNames=F5K20_140;
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=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(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] OF 32-541.
RC   STRAIN=cv. Columbia;
RX   PubMed=14993207; DOI=10.1101/gr.1515604;
RA   Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA   Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA   Weissenbach J., Salanoubat M.;
RT   "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT   combined approach to evaluate and improve Arabidopsis genome annotation.";
RL   Genome Res. 14:406-413(2004).
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).
CC   -!- FUNCTION: Putative serine/threonine-protein kinase that may function as
CC       a 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   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- CAUTION: Lacks the calcium-binding EGF-like domain which is a conserved
CC       feature of the wall-associated receptor kinase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BX822802; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR   EMBL; AL132960; CAB88346.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE79149.1; -; Genomic_DNA.
DR   EMBL; BX822802; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; T45924; T45924.
DR   RefSeq; NP_190952.2; NM_115244.3.
DR   AlphaFoldDB; Q9M342; -.
DR   SMR; Q9M342; -.
DR   STRING; 3702.AT3G53840.1; -.
DR   PaxDb; Q9M342; -.
DR   PRIDE; Q9M342; -.
DR   EnsemblPlants; AT3G53840.1; AT3G53840.1; AT3G53840.
DR   GeneID; 824551; -.
DR   Gramene; AT3G53840.1; AT3G53840.1; AT3G53840.
DR   KEGG; ath:AT3G53840; -.
DR   Araport; AT3G53840; -.
DR   TAIR; locus:2084425; AT3G53840.
DR   eggNOG; KOG1187; Eukaryota.
DR   HOGENOM; CLU_000288_43_5_1; -.
DR   InParanoid; Q9M342; -.
DR   OMA; LHEHIYC; -.
DR   OrthoDB; 684563at2759; -.
DR   PhylomeDB; Q9M342; -.
DR   PRO; PR:Q9M342; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9M342; baseline and differential.
DR   Genevisible; Q9M342; 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: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; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR045274; WAK-like.
DR   PANTHER; PTHR27005; PTHR27005; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Glycoprotein; Kinase; Membrane; Nucleotide-binding;
KW   Reference proteome; Serine/threonine-protein kinase; Signal; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..639
FT                   /note="Wall-associated receptor kinase-like 15"
FT                   /id="PRO_0000253320"
FT   TOPO_DOM        26..282
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        283..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        304..639
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          354..639
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        484
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         360..368
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         382
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   CARBOHYD        68
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        126
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        141
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        241
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   639 AA;  70690 MW;  AA3CD2D4BA4003B6 CRC64;
     MELPWLSLTT FTLSLLIYFS STTQAFKRCP NCGSTRVPYP LSTGLDCGDP GYRIRCDNYG
     SLWFDTLNGS TNPIKTIDPS GQRFVLRPPG FEQNKCVSVD IKYHGIQLDL NLPFNVSCSN
     TVIIMNCTKD GLDAYSSQGF NCSDNSLCHK FLNANLEARG NCRGVTSCCW YKTGASVNTY
     KVYRARPDMC SAYQSFMNLD LTIPVSKWGE PAVEILWEAP REPVCKSQGD CRDLLNSVCS
     NDSTNLGQKR CFCKKGFQWD SVNAVCEVNR CSKRKSCKRW SNLPLLGGLA GGVGAILIAG
     FITKTIVSKQ NRRIAGNQSW ASVRKLHRNL LSINSTGLDR IFTGKEIVKA TDNFAKSNLL
     GFGGFGEVFK GNLDDGTTVA VKRAKLGNEK SIYQIVNEVQ ILCQVSHKNL VKLLGCCIEL
     EMPVLVYEFV PNGTLFEHIY GGGGGGGGLY DHLPLRRRLM IAHQTAQGLD YLHSSSSPPI
     YHRDVKSSNI LLDENLDVKV ADFGLSRLGV SDVSHVTTCA QGTLGYLDPE YYLNFQLTDK
     SDVYSFGVVL FELLTCKKAI DFNREEEDVN LVVFVRKALK EGRLMDVIDP VIGIGATEKE
     IESMKALGVL AELCVKETRQ CRPTMQVAAK EIENILHGI
 
 
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