ID WAKLG_ARATH Reviewed; 720 AA.
AC Q9SA25;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 152.
DE RecName: Full=Wall-associated receptor kinase-like 8;
DE EC=2.7.11.-;
DE Flags: Precursor;
GN Name=WAKL8; OrderedLocusNames=At1g16260; ORFNames=F3O9.6;
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;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; AC006341; AAD34678.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29427.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29428.1; -; Genomic_DNA.
DR EMBL; AK229828; BAF01658.1; -; mRNA.
DR PIR; E86297; E86297.
DR RefSeq; NP_001185009.1; NM_001198080.1.
DR RefSeq; NP_173076.1; NM_101492.3.
DR AlphaFoldDB; Q9SA25; -.
DR SMR; Q9SA25; -.
DR BioGRID; 23435; 2.
DR IntAct; Q9SA25; 2.
DR STRING; 3702.Q9SA25; -.
DR GlyCosmos; Q9SA25; 4 sites, No reported glycans.
DR PaxDb; 3702-AT1G16260-1; -.
DR EnsemblPlants; AT1G16260.1; AT1G16260.1; AT1G16260.
DR EnsemblPlants; AT1G16260.2; AT1G16260.2; AT1G16260.
DR GeneID; 838195; -.
DR Gramene; AT1G16260.1; AT1G16260.1; AT1G16260.
DR Gramene; AT1G16260.2; AT1G16260.2; AT1G16260.
DR KEGG; ath:AT1G16260; -.
DR Araport; AT1G16260; -.
DR TAIR; AT1G16260; -.
DR eggNOG; ENOG502RMXX; Eukaryota.
DR HOGENOM; CLU_000288_43_5_1; -.
DR InParanoid; Q9SA25; -.
DR OMA; VGCEATC; -.
DR OrthoDB; 5479005at2759; -.
DR PhylomeDB; Q9SA25; -.
DR PRO; PR:Q9SA25; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SA25; baseline and differential.
DR Genevisible; Q9SA25; AT.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
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; IPR013695; WAK.
DR InterPro; IPR045274; WAK-like.
DR InterPro; IPR025287; WAK_GUB.
DR PANTHER; PTHR27005; WALL-ASSOCIATED RECEPTOR KINASE-LIKE 21; 1.
DR PANTHER; PTHR27005:SF541; WALL-ASSOCIATED RECEPTOR KINASE-LIKE 8; 1.
DR Pfam; PF13947; GUB_WAK_bind; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF08488; WAK; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..720
FT /note="Wall-associated receptor kinase-like 8"
FT /id="PRO_0000253311"
FT TOPO_DOM 24..315
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 337..720
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 390..663
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 252..310
FT /note="Atypical EGF-like"
FT ACT_SITE 515
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 396..404
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 418
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 463
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 549
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 554
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 562
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 254..266
FT /evidence="ECO:0000250"
FT DISULFID 288..301
FT /evidence="ECO:0000250"
FT DISULFID 296..310
FT /evidence="ECO:0000250"
SQ SEQUENCE 720 AA; 81160 MW; 092C5A060657F7A2 CRC64;
MGVDVKRFLV VMLLLRICEY AAASTFPLAL RNCSDHCGNV SVPYPFGIGK GCYKNKWFEI
VCKSSSDQQP ILLLPRIRRA VTSFNLGDPF SISVYNKFYI QSPLKHSGCP NRDGYSSSSL
NLKGSPFFIS ENNKFTAVGC NNKAFMNVTG LQIVGCETTC GNEIRSYKGA NTSCVGYKCC
QMTIPPLLQL QVFDATVEKL EPNKQGCQVA FLTQFTLSGS LFTPPELMEY SEYTTIELEW
RLDLSYMTSK RVLCKGNTFF EDSYQCSCHN GYEGNPYIPG GCQDIDECRD PHLNKCGKRK
CVNVLGSYRC EKTWPAILSG TLSSGLLLLI FGMWLLCKAN RKRKVAKQKR KFFQRNGGLL
LQQQTSFLHG SVNRTKVFSS NDLENATDRF NASRILGQGG QGTVYKGMLE DGMIVAVKKS
KALKEENLEE FINEIILLSQ INHRNVVKIL GCCLETEVPI LVYEFIPNRN LFDHLHNPSE
DFPMSWEVRL CIACEVADAL SYLHSAVSIP IYHRDVKSTN ILLDEKHRAK VSDFGISRSV
AIDDTHLTTI VQGTIGYVDP EYLQSNHFTG KSDVYSFGVL LIELLTGEKP VSLLRRQEVR
MLGAYFLEAM RNDRLHEILD ARIKEECDRE EVLAVAKLAR RCLSLNSEHR PTMRDVFIEL
DRMQSKRKGT QSQAQNGEEH AHIQIAMPES MSLSYSSPNI VVENSSFSLD TKPLMPHKTQ
//
