ID D7KJZ3_ARALL Unreviewed; 573 AA.
AC D7KJZ3;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Wall-associated receptor kinase-like {ECO:0000256|RuleBase:RU369027};
DE EC=2.7.11.- {ECO:0000256|RuleBase:RU369027};
GN ORFNames=ARALYDRAFT_679893 {ECO:0000313|EMBL:EFH66690.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
CC -!- FUNCTION: Serine/threonine-protein kinase that may function as a
CC signaling receptor of extracellular matrix component.
CC {ECO:0000256|RuleBase:RU369027}.
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 Evidence={ECO:0000256|ARBA:ARBA00000327,
CC ECO:0000256|RuleBase:RU369027};
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 Evidence={ECO:0000256|ARBA:ARBA00000671,
CC ECO:0000256|RuleBase:RU369027};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU369027}; Single-
CC pass type I membrane protein {ECO:0000256|RuleBase:RU369027}.
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. {ECO:0000256|RuleBase:RU369027}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|RuleBase:RU369027}.
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DR EMBL; GL348713; EFH66690.1; -; Genomic_DNA.
DR RefSeq; XP_002890431.1; XM_002890385.1.
DR AlphaFoldDB; D7KJZ3; -.
DR EnsemblPlants; Al_scaffold_0001_2216; Al_scaffold_0001_2216; Al_scaffold_0001_2216.
DR Gramene; Al_scaffold_0001_2216; Al_scaffold_0001_2216; Al_scaffold_0001_2216.
DR eggNOG; ENOG502QQPF; Eukaryota.
DR HOGENOM; CLU_000288_43_5_1; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; IPR045274; WAK-like.
DR InterPro; IPR025287; WAK_GUB.
DR PANTHER; PTHR27005:SF283; WALL-ASSOCIATED RECEPTOR KINASE 1-RELATED; 1.
DR PANTHER; PTHR27005; WALL-ASSOCIATED RECEPTOR KINASE-LIKE 21; 1.
DR Pfam; PF13947; GUB_WAK_bind; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU369027};
KW Kinase {ECO:0000256|RuleBase:RU369027};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU369027};
KW Reference proteome {ECO:0000313|Proteomes:UP000008694};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|RuleBase:RU369027}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..573
FT /note="Wall-associated receptor kinase-like"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003101551"
FT DOMAIN 362..573
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
SQ SEQUENCE 573 AA; 63934 MW; 2DAEEEC31B5FB1C8 CRC64;
MKFQEGVFLV AIFFFLGYTQ LVKGQHQPRH DCQTRCGNLT IDYPFGISTG CYYPGDDSFN
INCEEDKPNV LRNIEVRDFN HSGQLRVMLN RSTVCYDEER NNEFNAYQYK LDNLSLSPNN
KFTLVGCNAW ALLSTFGIQN YSTGCMSLCD SPPPPNSKCN GVGCCRTDVS IPLDSNRVVT
RPSRFENMSS VEHFNPCSYA FLVEDGMFNF SALEDLKNLR NVKQFPVVLD WSIGNQTCEQ
VVGRNICGGN SRCFNSSRGK GYNCKCLDGF DGNPYLSDSD GRCKDPDTCR NKVGGFYCKC
PFGYKLIATT ESTMRCKRPE YIIWTQIFLG KLPALRLSGA GPSNVDVKIF TEEGMKEATN
GYDESRILGQ GGQGTVYKGI LPDNSIVAIK KARLGDNSQV EQFINEVLVL SQINHRNVVK
LLGCCLETEV PLLVYEFIAS GTLYDHLHGS MFDSSLTWEH RLRIAIEIAG TLAYLHSSAS
IPIIHRDVKT ANILLDENLT AKVADFGASR LIPMDKEELA TMTTKHGKLD QFPEPEEIKH
LPGGHIFSAQ NDTSCSNYDS INNVPNLDIE AGR
//
