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WAKLO_ARATH
ID   WAKLO_ARATH             Reviewed;         708 AA.
AC   Q8RY67; O80461;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 2.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Wall-associated receptor kinase-like 14;
DE            EC=2.7.11.-;
DE   Flags: Precursor;
GN   Name=WAKL14; OrderedLocusNames=At2g23450; ORFNames=F26B6.10;
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
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; AC003040; AAC23760.2; -; Genomic_DNA.
DR   EMBL; CP002685; AEC07456.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC07457.1; -; Genomic_DNA.
DR   EMBL; AY075606; AAL91622.1; -; mRNA.
DR   EMBL; BT000817; AAN33192.1; -; mRNA.
DR   PIR; T01134; T01134.
DR   RefSeq; NP_565552.1; NM_127909.2.
DR   RefSeq; NP_850041.1; NM_179710.3.
DR   AlphaFoldDB; Q8RY67; -.
DR   SMR; Q8RY67; -.
DR   BioGRID; 2229; 8.
DR   IntAct; Q8RY67; 7.
DR   STRING; 3702.AT2G23450.2; -.
DR   PaxDb; Q8RY67; -.
DR   PRIDE; Q8RY67; -.
DR   ProteomicsDB; 242744; -.
DR   EnsemblPlants; AT2G23450.1; AT2G23450.1; AT2G23450.
DR   EnsemblPlants; AT2G23450.2; AT2G23450.2; AT2G23450.
DR   GeneID; 816877; -.
DR   Gramene; AT2G23450.1; AT2G23450.1; AT2G23450.
DR   Gramene; AT2G23450.2; AT2G23450.2; AT2G23450.
DR   KEGG; ath:AT2G23450; -.
DR   Araport; AT2G23450; -.
DR   TAIR; locus:2046728; AT2G23450.
DR   eggNOG; KOG1187; Eukaryota.
DR   HOGENOM; CLU_000288_43_5_1; -.
DR   InParanoid; Q8RY67; -.
DR   OMA; SCYSEAR; -.
DR   OrthoDB; 684563at2759; -.
DR   PhylomeDB; Q8RY67; -.
DR   PRO; PR:Q8RY67; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q8RY67; baseline and differential.
DR   Genevisible; Q8RY67; 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..42
FT                   /evidence="ECO:0000255"
FT   CHAIN           43..708
FT                   /note="Wall-associated receptor kinase-like 14"
FT                   /id="PRO_0000253319"
FT   TOPO_DOM        43..285
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        286..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        307..708
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          348..629
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          636..659
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          686..708
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        472
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         354..362
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         376
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   CARBOHYD        43
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        88
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        101
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        158
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        167
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        184
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        89
FT                   /note="V -> A (in Ref. 3; AAL91622/AAN33192)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   708 AA;  77873 MW;  FE11B114AE3E469A CRC64;
     MLRSIFDFNQ RSTKMVMISH KLDLILVFII VIGGSIFRRV SANFTVPCNG RCGGLTLPYP
     FGFSNGCSIR FDCSAAEKPM IGDFSVQNVT ENSIFVGLSH NCTRKIEDMN PLFGENFAPT
     SENSFLMENC NRTTDGCSIK QKFLENVLKL KSCDATGNIS CFSLDSNSSS KNSAKFFSMK
     TLRNSSCSLL FSSIAFESVG VNAGIALEFE RVRLGWWLKG GCESGTCAAN TDCTDVETPH
     GYAGHRCSCL DGFHGDGYTN PCQRALPECR GSKLVWRHCR SNLITIVGGT VGGAFLLAAL
     AFFFFCKRRR STPLRSHLSA KRLLSEAAGN SSVAFFPYKE IEKATDGFSE KQKLGIGAYG
     TVYRGKLQND EWVAIKRLRH RDSESLDQVM NEIKLLSSVS HPNLVRLLGC CIEQGDPVLV
     YEYMPNGTLS EHLQRDRGSG LPWTLRLTVA TQTAKAIAYL HSSMNPPIYH RDIKSTNILL
     DYDFNSKVAD FGLSRLGMTE SSHISTAPQG TPGYLDPQYH QCFHLSDKSD VYSFGVVLAE
     IITGLKVVDF TRPHTEINLA ALAVDKIGSG CIDEIIDPIL DLDLDAWTLS SIHTVAELAF
     RCLAFHSDMR PTMTEVADEL EQIRLSGWIP SMSLDSPAGS LRSSDRGSER SVKQSSIGSR
     RVVIPQKQPD CLASVEEISD SSPISVQDPW LSAQSSPSTN TLLGNIPR
 
 
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