WAKLQ_ARATH
ID WAKLQ_ARATH Reviewed; 657 AA.
AC Q9LZM4;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Wall-associated receptor kinase-like 20;
DE EC=2.7.11.-;
DE Flags: Precursor;
GN Name=WAKL20; OrderedLocusNames=At5g02070; ORFNames=T7H20_120;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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).
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 -!- 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}.
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DR EMBL; AL162508; CAB82980.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90428.1; -; Genomic_DNA.
DR PIR; T48228; T48228.
DR RefSeq; NP_195827.1; NM_120285.1.
DR AlphaFoldDB; Q9LZM4; -.
DR SMR; Q9LZM4; -.
DR STRING; 3702.AT5G02070.1; -.
DR PaxDb; Q9LZM4; -.
DR PRIDE; Q9LZM4; -.
DR ProteomicsDB; 242651; -.
DR EnsemblPlants; AT5G02070.1; AT5G02070.1; AT5G02070.
DR GeneID; 831776; -.
DR Gramene; AT5G02070.1; AT5G02070.1; AT5G02070.
DR KEGG; ath:AT5G02070; -.
DR Araport; AT5G02070; -.
DR TAIR; locus:2185118; AT5G02070.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_43_5_1; -.
DR InParanoid; Q9LZM4; -.
DR OMA; EPVCKTD; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9LZM4; -.
DR PRO; PR:Q9LZM4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LZM4; differential.
DR Genevisible; Q9LZM4; 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; 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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..657
FT /note="Wall-associated receptor kinase-like 20"
FT /id="PRO_0000253321"
FT TOPO_DOM 24..293
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..657
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 363..646
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 490
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 369..377
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 391
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 657 AA; 72348 MW; 18A310302377547D CRC64;
MEKKRSYYAL LIPTLLTVWL ACAGHSCARH AKAKPPMAGP PRCPNCGPMV VPYPLSTGPT
CGDQAYRINC VGGKLYFGAL HGSSYVITSI NSVTQRIVLR PPGLASSVSC ISADVSKQGL
ELDPHLPFSI TSSNTILLLN CSQAMLQAPI DCSPTSLCYS YIKNNASPCS KAPLCCTFRT
DGSQTAYTIR INGGGCLAYQ SFVGLNPNKE VPPPGKKWPD TGLELQWALP KEPVCKTDVD
CNLLLGKSKC LPDPTSLGLK RCSCKKGLEW DPVNAICGKC RHGKHCKKKK KTVVFAGAAV
AVVGVTLAIA VAVIGTKHSH QKVKKDIHKN IVKEREEMLS ANSTGKSSRI FTGREITKAT
NNFSKDNLIG TGGFGEVFKA VLEDGTITAI KRAKLNNTKG TDQILNEVRI LCQVNHRSLV
RLLGCCVDLE LPLLIYEFIP NGTLFEHLHG SSDRTWKPLT WRRRLQIAYQ TAEGLAYLHS
AAQPPIYHRD VKSSNILLDE KLNAKVSDFG LSRLVDLTET ANNESHIFTG AQGTLGYLDP
EYYRNFQLTD KSDVYSFGVV LLEMVTSKKA IDFTREEEDV NLVMYINKMM DQERLTECID
PLLKKTANKI DMQTIQQLGN LASACLNERR QNRPSMKEVA DEIEYIINIL SQEVTET
