WAKLC_ARATH
ID WAKLC_ARATH Reviewed; 730 AA.
AC Q9S9M3;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Wall-associated receptor kinase-like 3;
DE EC=2.7.11.-;
DE Flags: Precursor;
GN Name=WAKL3; OrderedLocusNames=At1g16140; ORFNames=T24D18.22;
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.
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 -!- 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=AAF18509.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC010924; AAF18509.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; B86296; B86296.
DR AlphaFoldDB; Q9S9M3; -.
DR SMR; Q9S9M3; -.
DR PeptideAtlas; Q9S9M3; -.
DR PRIDE; Q9S9M3; -.
DR Araport; AT1G16140; -.
DR InParanoid; Q9S9M3; -.
DR PRO; PR:Q9S9M3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9S9M3; baseline and differential.
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: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; 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 PANTHER; PTHR27005; PTHR27005; 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; Reference proteome; Serine/threonine-protein kinase;
KW Signal; Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..730
FT /note="Wall-associated receptor kinase-like 3"
FT /id="PRO_0000253307"
FT TOPO_DOM 26..357
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 358..378
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 379..730
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 428..699
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 283..340
FT /note="Atypical EGF-like"
FT REGION 703..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 553
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 434..442
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 456
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
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 212
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 DISULFID 285..298
FT /evidence="ECO:0000250"
FT DISULFID 320..331
FT /evidence="ECO:0000250"
FT DISULFID 326..340
FT /evidence="ECO:0000250"
SQ SEQUENCE 730 AA; 81928 MW; 208013B286EC9FBD CRC64;
MKTKTYNFRY IVASVLTLLM NGSSAATPPN SNSSSSCNRT FGGISIPFPF GIGGKDCYLN
SWYEVVCNST TSGSCKTVPF LTRINREVVN ISLPKSDFFS PYGVVHIKGP VTSLGCSSNI
SQGLQKTLPD LNITGRGSPY FLTDENRLVA VGCGTKALMT DIESEILGCE SSCKDTKSNE
VGNSLCNGYK CCQARLPVER PQAVGVNIES NNDTRGEGCK AAFLTSMKYF PSNITKPEWF
QADGYAVVEL GWYFDTSDSR FRNPLGCTNL TRSSGSYFLT DICLCRYGYF SRMSYRSCYC
GSGYRGNPYI RGGCIDIDEC EVPNKCGEDT CVNMAGRYSC VPKITKPAKL AHVLRGVLIG
LLGLLFFVIG IFGLYKFIRK RRRIIRSMKF FKRNGGLLLK QQLTTKDGSV EMSKIFSSRE
LEKATDNFSI DRVLGQGGQG TVYKRMLVDG SIVAVKRSKV VDEDKMEEFI NEIVLLSQIN
HRNIVKLLGC CLETEVPILV YEYIPNGDLF KRLHDEYDDY MMTWEVRLRI AVEIAGALSY
MHSAASFPIF HRDIKTTNIL LDEKYRAKIS DFGTSRSVAT DQTHLTTLVA GTFGYMDPEY
FLSSQYTHKS DVYSFGVVLV ELITGEKPMS RVRSEEGIGL ATYFLEAMKE NRAVDIIDIR
IKDESKQVMA VAKLARRCLN RKGNKRPNMR EVSIKLERIR SSPKDLDVHT ENEEEEEEDQ
LMEINRIYDS
