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WAKLJ_ARATH
ID   WAKLJ_ARATH             Reviewed;         769 AA.
AC   Q8VYA3; Q9MA08;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Wall-associated receptor kinase-like 10;
DE            EC=2.7.11.-;
DE   Flags: Precursor;
GN   Name=WAKL10; OrderedLocusNames=At1g79680; ORFNames=F20B17.10;
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(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].
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   -!- DOMAIN: The EGF-like region is specific to this family of proteins and
CC       seems to consist of the C-terminal of an EGF-like domain fused to the
CC       N-terminal of another one.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF68122.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC010793; AAF68122.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE36286.1; -; Genomic_DNA.
DR   EMBL; AY072320; AAL61927.1; -; mRNA.
DR   EMBL; AY128732; AAM91132.1; -; mRNA.
DR   PIR; G96827; G96827.
DR   RefSeq; NP_178086.1; NM_106617.4.
DR   AlphaFoldDB; Q8VYA3; -.
DR   SMR; Q8VYA3; -.
DR   BioGRID; 29525; 6.
DR   IntAct; Q8VYA3; 6.
DR   STRING; 3702.AT1G79680.1; -.
DR   PaxDb; Q8VYA3; -.
DR   PRIDE; Q8VYA3; -.
DR   ProteomicsDB; 242716; -.
DR   EnsemblPlants; AT1G79680.1; AT1G79680.1; AT1G79680.
DR   GeneID; 844307; -.
DR   Gramene; AT1G79680.1; AT1G79680.1; AT1G79680.
DR   KEGG; ath:AT1G79680; -.
DR   Araport; AT1G79680; -.
DR   TAIR; locus:2019843; AT1G79680.
DR   eggNOG; ENOG502RMXX; Eukaryota.
DR   HOGENOM; CLU_000288_43_5_1; -.
DR   InParanoid; Q8VYA3; -.
DR   OMA; CESACIG; -.
DR   OrthoDB; 478727at2759; -.
DR   PhylomeDB; Q8VYA3; -.
DR   PRO; PR:Q8VYA3; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q8VYA3; baseline and differential.
DR   Genevisible; Q8VYA3; 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:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004383; F:guanylate cyclase activity; IDA:TAIR.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
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:0006952; P:defense response; IEP:TAIR.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0009617; P:response to bacterium; IEP:TAIR.
DR   GO; GO:0009620; P:response to fungus; IEP:TAIR.
DR   GO; GO:0009751; P:response to salicylic acid; IEP:TAIR.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR013695; WAK.
DR   InterPro; IPR045274; WAK-like.
DR   InterPro; IPR025287; WAK_GUB.
DR   PANTHER; PTHR27005; PTHR27005; 1.
DR   Pfam; PF13947; GUB_WAK_bind; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF08488; WAK; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Disulfide bond; Glycoprotein; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..769
FT                   /note="Wall-associated receptor kinase-like 10"
FT                   /id="PRO_0000253314"
FT   TOPO_DOM        25..358
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        359..379
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        380..769
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          433..718
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          291..351
FT                   /note="Atypical EGF-like"
FT   ACT_SITE        559
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         439..447
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         461
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         506
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   MOD_RES         593
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   MOD_RES         598
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   MOD_RES         606
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   CARBOHYD        58
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        134
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        182
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        187
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        237
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        262
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        296
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        293..305
FT                   /evidence="ECO:0000250"
FT   DISULFID        327..342
FT                   /evidence="ECO:0000250"
FT   DISULFID        337..351
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   769 AA;  85704 MW;  05516EA26CB55090 CRC64;
     MSSNCSCSLL SLFSLLLIID LTVASSCPKT CGGIDIPYPF GIGTGCYLEK WYEIICVNNS
     VPFLSIINRE VVSISFSDMY RRFFNVGYGS IRIRNPIASK GCSSGGQEFG SLLNMTGYPF
     YLGDNNMLIA VGCNNTASLT NVEPSIVGCE STCSTNQDIP INDYLGVLYC NARYGDSEYC
     KNISIMNDTS CNGIGCCKAS LPARYQQIIG VEIDDSNTES KGCKVAFITD EEYFLSNGSD
     PERLHANGYD TVDLRWFIHT ANHSFIGSLG CKSIDEYTIL RRDNREYGIG CLCDYNSTTT
     GYATCSCASG FEGNPYIPGE CKDINECVRG IDGNPVCTAG KCVNLLGGYT CEYTNHRPLV
     IGLSTSFSTL VFIGGIYWLY KFIRRQRRLN QKKKFFKRNG GLLLQQQLTT TEGNVDSTRV
     FNSRELEKAT ENFSLTRILG EGGQGTVYKG MLVDGRIVAV KKSKVVDEDK LEEFINEVVI
     LSQINHRNIV KLLGCCLETD VPILVYEFIP NGNLFEHLHD DSDDYTMTTW EVRLRIAVDI
     AGALSYLHSA ASSPIYHRDI KSTNIMLDEK HRAKVSDFGT SRTVTVDHTH LTTVVSGTVG
     YMDPEYFQSS QFTDKSDVYS FGVVLAELIT GEKSVSFLRS QEYRTLATYF TLAMKENRLS
     DIIDARIRDG CKLNQVTAAA KIARKCLNMK GRKRPSMRQV SMELEKIRSY SEDMQPYEYA
     SENEEEKKET LVDVNVESRN YVSVTAASSQ YSIATTSSSR SDVEPLFPR
 
 
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