WAKLI_ARATH
ID WAKLI_ARATH Reviewed; 751 AA.
AC Q8RY17; Q4JQ55; Q9MA08;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Wall-associated receptor kinase-like 22;
DE EC=2.7.11.-;
DE Flags: Precursor;
GN Name=WAKL22; Synonyms=RFO1; OrderedLocusNames=At1g79670;
GN ORFNames=F20B17_27;
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 [GENOMIC DNA], AND FUNCTION.
RC STRAIN=cv. Ty-0;
RX PubMed=15965251; DOI=10.1534/genetics.105.042218;
RA Diener A.C., Ausubel F.M.;
RT "RESISTANCE TO FUSARIUM OXYSPORUM 1, a dominant Arabidopsis disease-
RT resistance gene, is not race specific.";
RL Genetics 171:305-321(2005).
RN [2]
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 [3]
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 [4]
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 [5]
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. Required during
CC plant's response to pathogen infection. {ECO:0000269|PubMed:15965251}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q8RY17-1; Sequence=Displayed;
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; DQ023268; AAY86486.1; -; Genomic_DNA.
DR EMBL; AC010793; AAF68122.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE36284.1; -; Genomic_DNA.
DR EMBL; AY078961; AAL84959.1; -; mRNA.
DR PIR; G96827; G96827.
DR RefSeq; NP_178085.1; NM_106616.5. [Q8RY17-1]
DR AlphaFoldDB; Q8RY17; -.
DR SMR; Q8RY17; -.
DR BioGRID; 29524; 2.
DR IntAct; Q8RY17; 2.
DR STRING; 3702.AT1G79670.1; -.
DR PaxDb; Q8RY17; -.
DR PRIDE; Q8RY17; -.
DR ProteomicsDB; 242325; -. [Q8RY17-1]
DR EnsemblPlants; AT1G79670.1; AT1G79670.1; AT1G79670. [Q8RY17-1]
DR GeneID; 844306; -.
DR Gramene; AT1G79670.1; AT1G79670.1; AT1G79670. [Q8RY17-1]
DR KEGG; ath:AT1G79670; -.
DR Araport; AT1G79670; -.
DR TAIR; locus:2019893; AT1G79670.
DR eggNOG; ENOG502RMXX; Eukaryota.
DR InParanoid; Q8RY17; -.
DR OMA; GQITEPW; -.
DR PhylomeDB; Q8RY17; -.
DR PRO; PR:Q8RY17; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8RY17; baseline and differential.
DR Genevisible; Q8RY17; 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: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:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0009620; P:response to fungus; IMP:TAIR.
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; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Disulfide bond; Glycoprotein; Kinase;
KW Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..751
FT /note="Wall-associated receptor kinase-like 22"
FT /id="PRO_0000253313"
FT TOPO_DOM 28..347
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 369..751
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 421..694
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 275..336
FT /note="Atypical EGF-like"
FT ACT_SITE 546
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 427..435
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 449
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 494
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 580
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 585
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 593
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
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 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 277..290
FT /evidence="ECO:0000250"
FT DISULFID 313..327
FT /evidence="ECO:0000250"
FT DISULFID 322..336
FT /evidence="ECO:0000250"
FT CONFLICT 9
FT /note="S -> C (in Ref. 1; AAY86486)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="I -> V (in Ref. 1; AAY86486)"
FT /evidence="ECO:0000305"
FT CONFLICT 34
FT /note="Missing (in Ref. 1; AAY86486)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="G -> R (in Ref. 1; AAY86486)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="G -> R (in Ref. 1; AAY86486)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="N -> Y (in Ref. 1; AAY86486)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="Missing (in Ref. 1; AAY86486)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="P -> T (in Ref. 1; AAY86486)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="Q -> E (in Ref. 1; AAY86486)"
FT /evidence="ECO:0000305"
FT CONFLICT 486
FT /note="E -> Q (in Ref. 1; AAY86486)"
FT /evidence="ECO:0000305"
FT CONFLICT 524
FT /note="S -> A (in Ref. 1; AAY86486)"
FT /evidence="ECO:0000305"
FT CONFLICT 689
FT /note="V -> I (in Ref. 1; AAY86486)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 751 AA; 83384 MW; 3837B8B160D0B34B CRC64;
MKRRRLFFSV LLSILTLFIN GPLITTAQSP PSSSTSCNRI CGGIEIPFPF GIGRRDCFLN
DWYEVVCNST TSGKSLAPFL YKINRELVSI TLRSSIDSSY GVVHIKSPVT SSGCSQRPVK
PLPLNLTGKG SPFFITDSNR LVSVGCDNRA LITDIESQIT GCESSCDGDK SRLDKICGGY
TCCQAKIPAD RPQVIGVDLE SSGGNTTQGG NCKVAFLTNE TYSPANVTEP EQFYTNGFTV
IELGWYFDTS DSRLTNPVGC VNLTETGIYT SAPSCVCEYG NFSGFGYSNC YCNQIGYRGN
PYLPGGCIDI DECEEGKGLS SCGELTCVNV PGSWRCELNG VGKIKPLFPG LVLGFPLLFL
VLGIWGLIKF VKKRRKIIRK RMFFKRNGGL LLKQQLTTRG GNVQSSKIFS SKELEKATDN
FNMNRVLGQG GQGTVYKGML VDGRIVAVKR SKVLDEDKVE EFINEVGVLS QINHRNIVKL
MGCCLETEVP ILVYEHIPNG DLFKRLHHDS DDYTMTWDVR LRISVEIAGA LAYLHSAAST
PVYHRDVKTT NILLDEKYRA KVSDFGTSRS INVDQTHLTT LVAGTFGYLD PEYFQTSQFT
DKSDVYSFGV VLVELITGEK PFSVMRPEEN RGLVSHFNEA MKQNRVLDIV DSRIKEGCTL
EQVLAVAKLA RRCLSLKGKK RPNMREVSVE LERIRSSPED LELHIEEEDE EECAMEINMD
DSWSVDMTAP ASLFDLSPKL DVEPLVPQRT W
