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WAKLS_ARATH
ID   WAKLS_ARATH             Reviewed;         433 AA.
AC   Q9LSV3;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Putative wall-associated receptor kinase-like 16;
DE            EC=2.7.11.-;
DE   Flags: Precursor;
GN   Name=WAKL16; OrderedLocusNames=At3g25490; ORFNames=MWL2.11;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(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: 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}.
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DR   EMBL; AB025639; BAB01318.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE77016.1; -; Genomic_DNA.
DR   RefSeq; NP_189176.1; NM_113445.2.
DR   AlphaFoldDB; Q9LSV3; -.
DR   SMR; Q9LSV3; -.
DR   STRING; 3702.AT3G25490.1; -.
DR   PaxDb; Q9LSV3; -.
DR   PRIDE; Q9LSV3; -.
DR   ProteomicsDB; 242688; -.
DR   EnsemblPlants; AT3G25490.1; AT3G25490.1; AT3G25490.
DR   GeneID; 822134; -.
DR   Gramene; AT3G25490.1; AT3G25490.1; AT3G25490.
DR   KEGG; ath:AT3G25490; -.
DR   Araport; AT3G25490; -.
DR   TAIR; locus:2094468; AT3G25490.
DR   eggNOG; KOG1187; Eukaryota.
DR   HOGENOM; CLU_000288_21_4_1; -.
DR   InParanoid; Q9LSV3; -.
DR   OMA; IACIEEN; -.
DR   OrthoDB; 496739at2759; -.
DR   PhylomeDB; Q9LSV3; -.
DR   PRO; PR:Q9LSV3; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LSV3; differential.
DR   Genevisible; Q9LSV3; 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; 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; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Signal; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..433
FT                   /note="Putative wall-associated receptor kinase-like 16"
FT                   /id="PRO_0000253323"
FT   TOPO_DOM        23..29
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        51..433
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          108..391
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        233
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         114..122
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         136
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         97
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   MOD_RES         181
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   MOD_RES         267
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   MOD_RES         272
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   MOD_RES         280
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
SQ   SEQUENCE   433 AA;  49073 MW;  77650AEADAF081E7 CRC64;
     MKLQHVVYLV AIFFVVAIFV IACIEENKYL VWIMIILANT TNILSLVRSI SYIKNIRKHQ
     KDTKIQRQLF FEKNGGGMLI ERLSGAGSSN IDFKIFTEED MKEATNGYDV SRILGQGGQW
     TVYKGILPDN SIVAIKKTRL GDNNQVEQFI NEVLVLSQIN HRNVVKLLGC CLETEVPLLV
     YEFITGGSLF DHLHGSMFVS SLTWEHRLEI AIEVAGAIAY LHSGASIPII HRDIKTENIL
     LDENLTAKVA DFGASKLKPM DKEQLTTMVQ GTLGYLDPEY YTTWLLNEKS DVYSFGVVLM
     ELISGQKALC FERPETSKHL VSYFVLATKE NRLHEIIDDQ VLNEENQREI HEAARVAVEC
     TRLKGEERPR MIEVAAELET LRAKTTKHNW LDQYPEENVH LLGSNIVSAQ GHTSSRGYDN
     NKNVARFDIE AGR
 
 
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