WAKLB_ARATH
ID WAKLB_ARATH Reviewed; 748 AA.
AC Q7X8C5; Q9S9M4;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Wall-associated receptor kinase-like 2;
DE EC=2.7.11.-;
DE Flags: Precursor;
GN Name=WAKL2; OrderedLocusNames=At1g16130; ORFNames=T24D18.21;
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 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 [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).
RN [6]
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: Slightly expressed in the whole plant.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF18508.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC010924; AAF18508.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29412.1; -; Genomic_DNA.
DR EMBL; BT008569; AAP40396.1; -; mRNA.
DR EMBL; BT008657; AAP40469.1; -; mRNA.
DR EMBL; AK229684; BAF01525.1; -; mRNA.
DR PIR; A86296; A86296.
DR RefSeq; NP_173064.1; NM_101480.3.
DR AlphaFoldDB; Q7X8C5; -.
DR SMR; Q7X8C5; -.
DR BioGRID; 23422; 1.
DR STRING; 3702.AT1G16130.1; -.
DR PaxDb; Q7X8C5; -.
DR PRIDE; Q7X8C5; -.
DR ProteomicsDB; 242755; -.
DR EnsemblPlants; AT1G16130.1; AT1G16130.1; AT1G16130.
DR GeneID; 838182; -.
DR Gramene; AT1G16130.1; AT1G16130.1; AT1G16130.
DR KEGG; ath:AT1G16130; -.
DR Araport; AT1G16130; -.
DR TAIR; locus:2200562; AT1G16130.
DR eggNOG; ENOG502RMXX; Eukaryota.
DR HOGENOM; CLU_000288_43_5_1; -.
DR InParanoid; Q7X8C5; -.
DR OMA; KIRSATH; -.
DR OrthoDB; 478727at2759; -.
DR PhylomeDB; Q7X8C5; -.
DR PRO; PR:Q7X8C5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q7X8C5; baseline and differential.
DR Genevisible; Q7X8C5; AT.
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: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; HDA:TAIR.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; HDA: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; PS01186; EGF_2; 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..27
FT /evidence="ECO:0000255"
FT CHAIN 28..748
FT /note="Wall-associated receptor kinase-like 2"
FT /id="PRO_0000253306"
FT TOPO_DOM 28..341
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 363..748
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 416..689
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 270..331
FT /note="Atypical EGF-like"
FT REGION 727..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 541
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 422..430
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 444
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 489
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 575
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 580
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 588
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 272..285
FT /evidence="ECO:0000250"
FT DISULFID 308..322
FT /evidence="ECO:0000250"
FT DISULFID 317..331
FT /evidence="ECO:0000250"
SQ SEQUENCE 748 AA; 83357 MW; 39B2DFDE7549E135 CRC64;
MKTETHNRQC IPLAISVLSL FINGVSSARQ PPDRCNRVCG EISIPFPFGI GGKDCYLNPW
YEVVCNSTNS VPFLSRINRE LVNISLNGVV HIKAPVTSSG CSTGTSQPLT PPPLNVAGQG
SPYFLTDKNL LVAVGCKFKA VMAGITSQIT SCESSCNERN SSSQEGRNKI CNGYKCCQTR
IPEGQPQVIS VDIEIPQGNN TTGEGGCRVA FLTSDKYSSL NVTEPEKFHG HGYAAVELGW
FFDTSDSRDT QPISCKNASD TTPYTSDTRC SCSYGYFSGF SYRDCYCNSP GYKGNPFLPG
GCVDVDECKL DIGRNQCKDQ SCVNLPGWFD CQPKKPEQLK RVIQGVLIGS ALLLFAFGIF
GLYKFVQKRR KLIRMRKFFR RNGGMLLKQQ LARKEGNVEM SRIFSSHELE KATDNFNKNR
VLGQGGQGTV YKGMLVDGRI VAVKRSKAVD EDRVEEFINE VVVLAQINHR NIVKLLGCCL
ETEVPVLVYE FVPNGDLCKR LHDESDDYTM TWEVRLHIAI EIAGALSYLH SAASFPIYHR
DIKTTNILLD ERNRAKVSDF GTSRSVTIDQ THLTTQVAGT FGYVDPEYFQ SSKFTEKSDV
YSFGVVLVEL LTGEKPSSRV RSEENRGLAA HFVEAVKENR VLDIVDDRIK DECNMDQVMS
VANLARRCLN RKGKKRPNMR EVSIELEMIR SSHYDSGIHI EDDDEEDDQA MELNFNDTWE
VGATAPASMF NNASPTSDAE PLVPLRTW
