WAKLR_ARATH
ID WAKLR_ARATH Reviewed; 622 AA.
AC Q8GYF5; F4K248; Q9FL01;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Wall-associated receptor kinase-like 21;
DE EC=2.7.11.-;
DE Flags: Precursor;
GN Name=WAKL21; OrderedLocusNames=At5g66790; ORFNames=MUD21_3;
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=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
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 3-622.
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).
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; AB010700; BAB08621.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98263.1; -; Genomic_DNA.
DR EMBL; AK117669; BAC42322.1; -; mRNA.
DR RefSeq; NP_201480.3; NM_126077.5.
DR AlphaFoldDB; Q8GYF5; -.
DR SMR; Q8GYF5; -.
DR BioGRID; 22054; 7.
DR IntAct; Q8GYF5; 8.
DR STRING; 3702.AT5G66790.1; -.
DR iPTMnet; Q8GYF5; -.
DR PaxDb; Q8GYF5; -.
DR PRIDE; Q8GYF5; -.
DR ProteomicsDB; 242760; -.
DR EnsemblPlants; AT5G66790.1; AT5G66790.1; AT5G66790.
DR GeneID; 836812; -.
DR Gramene; AT5G66790.1; AT5G66790.1; AT5G66790.
DR KEGG; ath:AT5G66790; -.
DR Araport; AT5G66790; -.
DR TAIR; locus:2174994; AT5G66790.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_43_5_1; -.
DR InParanoid; Q8GYF5; -.
DR OMA; IRFNCSE; -.
DR OrthoDB; 684563at2759; -.
DR PRO; PR:Q8GYF5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8GYF5; baseline and differential.
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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045274; WAK-like.
DR PANTHER; PTHR27005; PTHR27005; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..622
FT /note="Wall-associated receptor kinase-like 21"
FT /id="PRO_0000253322"
FT TOPO_DOM 22..247
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..622
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 314..594
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 439
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 320..328
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 342
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 131
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 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 3..6
FT /note="ETPQ -> MTRE (in Ref. 3; BAC42322)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="G -> E (in Ref. 3; BAC42322)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 622 AA; 69270 MW; 7B4831EB40084A74 CRC64;
MAETPQPYLI FVFFVFTLTV ATQTTGSVKC KTSLLRYPFG FSDGYPIRFN CSEITGEAVI
GEFAVQEVTN SNIYVEIPPV CKRNIRKIEQ LFRENLAPSK LQNIILVQGC KKQNKSSNCL
IRNKFVENRL NLSKCKSPVS CLDGATTTTA DVMSLGDVVN GSGCKYWFSS ISQSQVSVNL
GRLKLDWWLK GSCSNTTCSE NADCAKVKLD DGGLGHRCTC REGFSGKAFT VPGGCHRLVY
KRKGLHKLVV LGTAGILVGV LVIVVLIATY FFRNKQSASS ERASIANRLL CELAGNSSVP
FYTYKEIEKA TDSFSDKNML GTGAYGTVYA GEFPNSSCVA IKRLKHKDTT SIDQVVNEIK
LLSSVSHPNL VRLLGCCFAD GEPFLVYEFM PNGTLYQHLQ HERGQPPLSW QLRLAIACQT
ANAIAHLHSS VNPPIYHRDI KSSNILLDHE FNSKISDFGL SRLGMSTDFE ASHISTAPQG
TPGYLDPQYH QDFQLSDKSD VYSFGVVLVE IISGFKVIDF TRPYSEVNLA SLAVDRIGRG
RVVDIIDPCL NKEINPKMFA SIHNLAELAF RCLSFHRNMR PTMVEITEDL HRIKLMHYGT
ESGKFKNRSE IDMKRQQSFP RE
