RLK1_ARATH
ID RLK1_ARATH Reviewed; 832 AA.
AC Q39202; F4K0I9; Q8H7E0; Q9SAR9;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=G-type lectin S-receptor-like serine/threonine-protein kinase RLK1;
DE EC=2.7.11.1;
DE AltName: Full=Receptor-like protein kinase 1;
DE Flags: Precursor;
GN Name=RLK1; OrderedLocusNames=At5g60900; ORFNames=MSL3.2;
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 [MRNA], AND NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF
RP 733-832.
RC STRAIN=cv. Columbia;
RX PubMed=8220453; DOI=10.1111/j.1365-313x.1993.tb00164.x;
RA Walker J.C.;
RT "Receptor-like protein kinase genes of Arabidopsis thaliana.";
RL Plant J. 3:451-456(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-243.
RA Stracke R., Palme K.;
RT "Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves
RT and guard cells.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
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; EC=2.7.11.1;
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 EC=2.7.11.1;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AB008269; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M84658; AAA32857.1; -; mRNA.
DR EMBL; U66462; AAC16898.1; -; Genomic_DNA.
DR EMBL; AB008269; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED97394.2; -; Genomic_DNA.
DR EMBL; AF083720; AAN60278.1; -; mRNA.
DR PIR; S27754; S27754.
DR RefSeq; NP_001318851.1; NM_001345434.1.
DR AlphaFoldDB; Q39202; -.
DR SMR; Q39202; -.
DR PeptideAtlas; Q39202; -.
DR PRIDE; Q39202; -.
DR GeneID; 836211; -.
DR KEGG; ath:AT5G60900; -.
DR Araport; AT5G60900; -.
DR InParanoid; Q39202; -.
DR OrthoDB; 137887at2759; -.
DR PRO; PR:Q39202; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q39202; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:UniProt.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR CDD; cd00028; B_lectin; 1.
DR Gene3D; 2.90.10.10; -; 2.
DR InterPro; IPR001480; Bulb-type_lectin_dom.
DR InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003609; Pan_app.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR024171; SRK-like_kinase.
DR Pfam; PF01453; B_lectin; 1.
DR Pfam; PF08276; PAN_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF000641; SRK; 1.
DR SMART; SM00108; B_lectin; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF51110; SSF51110; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50927; BULB_LECTIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Disulfide bond; EGF-like domain; Glycoprotein;
KW Kinase; Lectin; Membrane; Nucleotide-binding; Receptor; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..832
FT /note="G-type lectin S-receptor-like serine/threonine-
FT protein kinase RLK1"
FT /id="PRO_5000143617"
FT TOPO_DOM 25..461
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 462..482
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 483..832
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 37..157
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DOMAIN 299..349
FT /note="EGF-like; atypical"
FT /evidence="ECO:0000305"
FT DOMAIN 357..446
FT /note="PAN"
FT DOMAIN 531..803
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 622..638
FT /note="CaM-binding"
FT /evidence="ECO:0000250"
FT ACT_SITE 657
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 537..545
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 563
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 29
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 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 446
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 303..320
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 314..330
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 332..348
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 397..420
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DISULFID 401..407
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT CONFLICT 84
FT /note="I -> M (in Ref. 4; AAN60278)"
FT /evidence="ECO:0000305"
FT CONFLICT 696
FT /note="T -> R (in Ref. 1; AAA32857)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 832 AA; 93751 MW; 8BEB346BDE8E6DC0 CRC64;
MGSLSCSIIH LVLILQLQTF FVFSQNIRNG SVPVGESLTA SESQQISSSW RSPSGDFAFG
FRKIQPNDGF TLSIWFDKIS DKTIVWHAQA VNTTTGLVPN GSKVTLTADG GLVIADPRGQ
ELWRALSGGS VSRGRFTDDG NFVLFRDGSE DSDEVLWSSF ENPTDTLLPN QNIEVGRNLS
SRRTETSFKK GRFSLRLEDD GNLQLHSLNA ETASESDIYS QYYESNTNDP NNPGIQLVFN
QSGEIYVLQR NNSRFVVKDR DPDFSIAAPF YISTGFLLST IIPKEARRIV GGCLLGLCRD
NMCSPDDALG NMACGYNNIC SLGNNKRPKC ECPERFVLKD PSNEYGDCLP DFEMQTCRPE
NQTANSDVNL YEFITLEKTN WPFGDYESYA NYDEERCKAS CLSDCLCAAV IFGTNRDLKC
WKKKFPLSHG ERSPRGDSDT FIKVRNRSIA DVPVTGNRAK KLDWLIIACS VLLGTSAFVI
FDTSCSYRKT KKSKNMMKNQ ARDIGRTTAT TTANELNLRV FTYGELAEAT RDFTEELGRG
AFGIVYKGYL EVAGGSEVTV AVKKLDRLDL DNEKEFKNEV KVIGQIHHKN LVRLIGFCNE
GQSQMIVYEF LPQGTLANFL FRRPRPSWED RKNIAVAIAR GILYLHEECS EQIIHCDIKP
QNILLDEYYT PRISDFGLAK LLLMNQTYTL TNIRGTKGYV APEWFRNSPI TSKVDVYSYG
VMLLEIVCCK KAVDLEDNVI LINWAYDCFR QGRLEDLTED DSEAMNDMET VERYVKIAIW
CIQEEHGMRP NMRNVTQMLE GVIQVFDPPN PSPYSTFTWS DESLSSDPVS LV
