Y5838_ARATH
ID Y5838_ARATH Reviewed; 620 AA.
AC Q9ASS4; Q8H771; Q8W4H2; Q9LV74;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Probably inactive leucine-rich repeat receptor-like protein kinase At5g48380;
DE Flags: Precursor;
GN OrderedLocusNames=At5g48380; ORFNames=K23F3.10, MJE7.1;
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].
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.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
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 [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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=20064227; DOI=10.1186/1471-2164-11-19;
RA Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.;
RT "Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-
RT like protein kinase genes in Arabidopsis thaliana.";
RL BMC Genomics 11:19-19(2010).
RN [6]
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. La-0;
RX PubMed=14506206; DOI=10.1074/mcp.t300006-mcp200;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Large-scale analysis of in vivo phosphorylated membrane proteins by
RT immobilized metal ion affinity chromatography and mass spectrometry.";
RL Mol. Cell. Proteomics 2:1234-1243(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=17644812; DOI=10.1074/mcp.m700099-mcp200;
RA Marmagne A., Ferro M., Meinnel T., Bruley C., Kuhn L., Garin J.,
RA Barbier-Brygoo H., Ephritikhine G.;
RT "A high content in lipid-modified peripheral proteins and integral receptor
RT kinases features in the arabidopsis plasma membrane proteome.";
RL Mol. Cell. Proteomics 6:1980-1996(2007).
CC -!- INTERACTION:
CC Q9ASS4; O04567: At1g27190; NbExp=2; IntAct=EBI-6298290, EBI-1238687;
CC Q9ASS4; Q9ZQR3: At2g14510; NbExp=2; IntAct=EBI-6298290, EBI-20651957;
CC Q9ASS4; Q8VYT3: At4g30520; NbExp=2; IntAct=EBI-6298290, EBI-16902452;
CC Q9ASS4; Q9ASS4: At5g48380; NbExp=2; IntAct=EBI-6298290, EBI-6298290;
CC Q9ASS4; Q94F62: BAK1; NbExp=6; IntAct=EBI-6298290, EBI-617138;
CC Q9ASS4; O65440-2: BAM3; NbExp=2; IntAct=EBI-6298290, EBI-20653325;
CC Q9ASS4; Q6XAT2: ERL2; NbExp=2; IntAct=EBI-6298290, EBI-16895926;
CC Q9ASS4; Q9C8I6: IOS1; NbExp=2; IntAct=EBI-6298290, EBI-16924837;
CC Q9ASS4; Q9ZVD4: LRR-RLK; NbExp=2; IntAct=EBI-6298290, EBI-20651739;
CC Q9ASS4; Q9LFS4: NIK1; NbExp=2; IntAct=EBI-6298290, EBI-16146189;
CC Q9ASS4; Q9ZRF9: RPK1; NbExp=2; IntAct=EBI-6298290, EBI-1238953;
CC Q9ASS4; Q94AG2: SERK1; NbExp=2; IntAct=EBI-6298290, EBI-1555537;
CC Q9ASS4; Q9SKG5: SERK4; NbExp=2; IntAct=EBI-6298290, EBI-6290483;
CC Q9ASS4; Q9C8M9: SRF6; NbExp=2; IntAct=EBI-6298290, EBI-16954301;
CC Q9ASS4; Q8RWZ1: SUB; NbExp=2; IntAct=EBI-6298290, EBI-17072125;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14506206,
CC ECO:0000305|PubMed:17644812}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:14506206, ECO:0000305|PubMed:17644812}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. Lacks the conserved Asp active site at position 429, which is
CC replaced by an Asn residue.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA96958.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF083807; AAN60365.1; -; mRNA.
DR EMBL; AB020745; BAA96958.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED95662.1; -; Genomic_DNA.
DR EMBL; AF367312; AAK32899.1; -; mRNA.
DR EMBL; AY062559; AAL32637.1; -; mRNA.
DR EMBL; AY074386; AAL67082.1; -; mRNA.
DR EMBL; FJ708793; ACN59384.1; -; mRNA.
DR RefSeq; NP_568696.1; NM_124213.5.
DR AlphaFoldDB; Q9ASS4; -.
DR SMR; Q9ASS4; -.
DR BioGRID; 20138; 74.
DR IntAct; Q9ASS4; 61.
DR STRING; 3702.AT5G48380.1; -.
DR iPTMnet; Q9ASS4; -.
DR PaxDb; Q9ASS4; -.
DR PRIDE; Q9ASS4; -.
DR ProteomicsDB; 243120; -.
DR EnsemblPlants; AT5G48380.1; AT5G48380.1; AT5G48380.
DR GeneID; 834892; -.
DR Gramene; AT5G48380.1; AT5G48380.1; AT5G48380.
DR KEGG; ath:AT5G48380; -.
DR Araport; AT5G48380; -.
DR TAIR; locus:2165981; AT5G48380.
DR eggNOG; ENOG502QSSB; Eukaryota.
DR HOGENOM; CLU_000288_92_6_1; -.
DR InParanoid; Q9ASS4; -.
DR OMA; KALEWPL; -.
DR OrthoDB; 339942at2759; -.
DR PhylomeDB; Q9ASS4; -.
DR PRO; PR:Q9ASS4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9ASS4; baseline and differential.
DR Genevisible; Q9ASS4; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0016301; F:kinase activity; IDA:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
DR GO; GO:0033612; F:receptor serine/threonine kinase binding; IPI:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IDA:UniProtKB.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:UniProtKB.
DR GO; GO:0031348; P:negative regulation of defense response; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Glycoprotein; Leucine-rich repeat; Membrane;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..620
FT /note="Probably inactive leucine-rich repeat receptor-like
FT protein kinase At5g48380"
FT /id="PRO_0000389464"
FT TOPO_DOM 28..228
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 250..620
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 101..124
FT /note="LRR 1"
FT REPEAT 126..148
FT /note="LRR 2"
FT REPEAT 150..172
FT /note="LRR 3"
FT REPEAT 174..196
FT /note="LRR 4"
FT DOMAIN 303..596
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 309..317
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 331
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 300
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9LSI9"
FT MOD_RES 463
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 479
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 482
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 111
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 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 214
FT /note="L -> I (in Ref. 1; AAN60365)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="G -> R (in Ref. 4; AAL32637)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 620 AA; 69142 MW; FF2CD5BCF319D385 CRC64;
MMMGRLVFVI WLYNCLCLLL LSSLVDADQA NIDCLRTFKS QVEDPNRYLS TWVFGNETAG
YICKFSGVTC WHDDENRVLS IKLSGYGLRG VFPPAVKLCA DLTGLDLSRN NFSGPLPANI
STLIPLVTIL DLSYNSFSGE IPMLISNITF LNTLMLQHNQ FTGTLPPQLA QLGRLKTFSV
SDNRLVGPIP NFNQTLQFKQ ELFANNLDLC GKPLDDCKSA SSSRGKVVII AAVGGLTAAA
LVVGVVLFFY FRKLGAVRKK QDDPEGNRWA KSLKGQKGVK VFMFKKSVSK MKLSDLMKAT
EEFKKDNIIA TGRTGTMYKG RLEDGSLLMI KRLQDSQRSE KEFDAEMKTL GSVKNRNLVP
LLGYCVANKE RLLMYEYMAN GYLYDQLHPA DEESFKPLDW PSRLKIAIGT AKGLAWLHHS
CNPRIIHRNI SSKCILLTAE FEPKISDFGL ARLMNPIDTH LSTFVNGEFG DFGYVAPEYS
RTMVATPKGD VYSFGVVLLE LVTGQKATSV TKVSEEKAEE ENFKGNLVEW ITKLSSESKL
QEAIDRSLLG NGVDDEIFKV LKVACNCVLP EIAKQRPTMF EVYQLLRAIG ESYNFTADDD
ILIPSESGEG DFIEELIVAR
