Y5815_ARATH
ID Y5815_ARATH Reviewed; 785 AA.
AC Q9LVN2;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Probably inactive leucine-rich repeat receptor-like protein kinase At5g58150;
DE Flags: Precursor;
GN OrderedLocusNames=At5g58150; ORFNames=MCK7.2;
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 [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 [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;
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 [5]
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).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14506206};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:14506206}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. Lacks the conserved Asp active site at position 645, which is
CC replaced by a Glu residue.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB019228; BAA96906.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97005.1; -; Genomic_DNA.
DR EMBL; AY091097; AAM14048.1; -; mRNA.
DR EMBL; AY123035; AAM67568.1; -; mRNA.
DR EMBL; FJ708804; ACN59395.1; -; mRNA.
DR RefSeq; NP_200623.1; NM_125200.2.
DR AlphaFoldDB; Q9LVN2; -.
DR SMR; Q9LVN2; -.
DR BioGRID; 21171; 17.
DR IntAct; Q9LVN2; 17.
DR STRING; 3702.AT5G58150.1; -.
DR iPTMnet; Q9LVN2; -.
DR PaxDb; Q9LVN2; -.
DR PRIDE; Q9LVN2; -.
DR ProteomicsDB; 242935; -.
DR EnsemblPlants; AT5G58150.1; AT5G58150.1; AT5G58150.
DR GeneID; 835927; -.
DR Gramene; AT5G58150.1; AT5G58150.1; AT5G58150.
DR KEGG; ath:AT5G58150; -.
DR Araport; AT5G58150; -.
DR TAIR; locus:2161303; AT5G58150.
DR eggNOG; ENOG502QTEF; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; Q9LVN2; -.
DR OMA; SAHKLGH; -.
DR OrthoDB; 136642at2759; -.
DR PhylomeDB; Q9LVN2; -.
DR PRO; PR:Q9LVN2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LVN2; differential.
DR Genevisible; Q9LVN2; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 3.80.10.10; -; 4.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13516; LRR_6; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00369; LRR_TYP; 6.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 11.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 2: Evidence at transcript 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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..785
FT /note="Probably inactive leucine-rich repeat receptor-like
FT protein kinase At5g58150"
FT /id="PRO_0000389467"
FT TOPO_DOM 22..436
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 437..457
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 458..785
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 64..88
FT /note="LRR 1"
FT REPEAT 89..112
FT /note="LRR 2"
FT REPEAT 114..136
FT /note="LRR 3"
FT REPEAT 138..160
FT /note="LRR 4"
FT REPEAT 161..184
FT /note="LRR 5"
FT REPEAT 186..208
FT /note="LRR 6"
FT REPEAT 210..232
FT /note="LRR 7"
FT REPEAT 236..258
FT /note="LRR 8"
FT REPEAT 259..283
FT /note="LRR 9"
FT REPEAT 284..306
FT /note="LRR 10"
FT REPEAT 307..330
FT /note="LRR 11"
FT REPEAT 331..355
FT /note="LRR 12"
FT REPEAT 357..377
FT /note="LRR 13"
FT REPEAT 379..405
FT /note="LRR 14"
FT DOMAIN 521..785
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 527..535
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 549
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 510
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 518
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 594
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 683
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 785 AA; 86611 MW; 3328A3586E0E3E5E CRC64;
MRLSLWGSLL FFSFFVKHLT SLDPNTDAYH LSSFFSAMRL PNSPQAHTFS SLCSWPGVVV
CDSSENVLHI SASGLDLSGS IPDNTIGKMS KLQTLDLSGN KITSLPSDLW SLSLLESLNL
SSNRISEPLP SNIGNFMSLH TLDLSFNSIS GKIPAAISNL VNLTTLKLHN NDFQFGVPPE
LVHCRSLLSI DLSSNRLNES LPVGFGSAFP LLKSLNLSRN LFQGSLIGVL HENVETVDLS
ENRFDGHILQ LIPGHKHNWS SLIHLDLSDN SFVGHIFNGL SSAHKLGHLN LACNRFRAQE
FPEIGKLSAL HYLNLSRTNL TNIIPREISR LSHLKVLDLS SNNLTGHVPM LSVKNIEVLD
LSLNKLDGDI PRPLLEKLAM MQRFNFSFNN LTFCNPNFSQ ETIQRSFINI RNNCPFAAKP
IITKGKKVNK KNTGLKIGLG LAISMAFLLI GLLLILVALR VRRKSRTWAT KLAINNTEPN
SPDQHDSTTD IKQATQIPVV MIDKPLMKMT LADLKAATFN FDRGTMLWEG KSGPTYGAVL
PGGFRAALKV IPSGTTLTDT EVSIAFERLA RINHPNLFPL CGYCIATEQR IAIYEDLDMV
NLQSLLHNNG DDSAPWRLRH KIALGTARAL AFLHHGCIPP MVHGEVKAAT ILLDSSQEPR
LADFGLVKLL DEQFPGSESL DGYTPPEQER NASPTLESDV YSFGVVLLEL VSGKKPEGDL
VNWVRGLVRQ GQGLRAIDPT MQETVPEDEI AEAVKIGYLC TADLPWKRPT MQQVVGLLKD
ISPNY