WAKLA_ARATH
ID WAKLA_ARATH Reviewed; 730 AA.
AC Q9S9M5;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Wall-associated receptor kinase-like 1;
DE EC=2.7.11.-;
DE Flags: Precursor;
GN Name=WAKL1; OrderedLocusNames=At1g16120; ORFNames=T24D18.20;
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 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).
RN [4]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=14576286; DOI=10.1104/pp.103.028530;
RA Verica J.A., Chae L., Tong H.-Y., Ingmire P., He Z.-H.;
RT "Tissue-specific and developmentally regulated expression of a cluster of
RT tandemly arrayed cell wall-associated kinase-like kinase genes in
RT Arabidopsis.";
RL Plant Physiol. 133:1732-1746(2003).
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 -!- TISSUE SPECIFICITY: Preferentially expressed in roots and flowers.
CC {ECO:0000269|PubMed:14576286}.
CC -!- INDUCTION: Induced by INA. {ECO:0000269|PubMed:14576286}.
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}.
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DR EMBL; AC010924; AAF18507.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29411.1; -; Genomic_DNA.
DR PIR; H86295; H86295.
DR RefSeq; NP_173063.1; NM_101479.2.
DR AlphaFoldDB; Q9S9M5; -.
DR SMR; Q9S9M5; -.
DR STRING; 3702.AT1G16120.1; -.
DR iPTMnet; Q9S9M5; -.
DR PaxDb; Q9S9M5; -.
DR PRIDE; Q9S9M5; -.
DR ProteomicsDB; 242685; -.
DR EnsemblPlants; AT1G16120.1; AT1G16120.1; AT1G16120.
DR GeneID; 838181; -.
DR Gramene; AT1G16120.1; AT1G16120.1; AT1G16120.
DR KEGG; ath:AT1G16120; -.
DR Araport; AT1G16120; -.
DR TAIR; locus:2200552; AT1G16120.
DR eggNOG; ENOG502RMXX; Eukaryota.
DR HOGENOM; CLU_000288_43_5_1; -.
DR InParanoid; Q9S9M5; -.
DR OMA; RNICSIE; -.
DR OrthoDB; 478727at2759; -.
DR PhylomeDB; Q9S9M5; -.
DR PRO; PR:Q9S9M5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9S9M5; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009505; C:plant-type cell wall; ISS:TAIR.
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 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 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..25
FT /evidence="ECO:0000255"
FT CHAIN 26..730
FT /note="Wall-associated receptor kinase-like 1"
FT /id="PRO_0000253305"
FT TOPO_DOM 26..358
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..379
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 380..730
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 429..702
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 282..341
FT /note="Atypical EGF-like"
FT REGION 685..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..710
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 554
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 435..443
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 457
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 502
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 588
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 593
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 601
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
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 284..297
FT /evidence="ECO:0000250"
FT DISULFID 319..331
FT /evidence="ECO:0000250"
FT DISULFID 325..341
FT /evidence="ECO:0000250"
SQ SEQUENCE 730 AA; 81210 MW; B51DB48D995C73B5 CRC64;
MKTKTSIFQF IVASVLTLLI NDSSAATPPP PISNSSTSCN KTCGGISIPF PFGIGGKDCY
LNGWYEVICN TTTSDSNTTV PLLSMINREV VNISLPDSNE PYGLVQIKGP VTSLGCSSNT
SEGPQNSLPV LNVTGKGSPY FLTDENRLVA VGCGIKALMT DTESEILGCE SSCEHRKSGE
EVTNLICTGY RCCQARLPVG RPQAITVNIE NSSGGEETCK VAFLTDKRYS PSNVTEPEQF
HNNGYVVLEL GWYFATSNSR FKSLLGCTNM SRKGSGFSDD NCSCEYDYFS GMSYRNCYCD
YGYTGNPYLR GGCVDTDSCE GNHNCGEDAH CVNMPGPMSM CRPNPKITKP TKPPVLQGIL
IGLSGLVFFV GLFWLFKLIK KRRNINRSKK FFKRNGGLLL KQQLTTKDGN VEMSKIFSSK
ELRKATDNFS IDRVLGQGGQ GTVYKGMLVD GSIVAVKRSK VVDEDKMEEF INEIVLLSQI
NHRNIVKLLG CCLETEVPIL VYEYIPNGDL FKRLHDESDD YTMTWEVRLR IAIEIAGALT
YMHSAASFPI FHRDIKTTNI LLDEKYRAKV SDFGTSRSVT LDQTHLTTLV AGTFGYMDPE
YFLSSQYTHK SDVYSFGVVL VELITGEKPL SRVRSEEGRG LATHFLEAMK ENRVIDIIDI
RIKDESKLEQ VMAVAKLARK CLNRKGKNRP NMKEVSNELE RIRSSPEDLD VRTENEDEEE
DQPMAINNKR
