Y5188_ARATH
ID Y5188_ARATH Reviewed; 872 AA.
AC Q9FZB1; F4IB72;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Probable LRR receptor-like serine/threonine-protein kinase At1g51880;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At1g51880; ORFNames=T14L22.9;
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 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).
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: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AC015448; AAF99858.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32728.2; -; Genomic_DNA.
DR EMBL; FJ708654; ACN59250.1; -; mRNA.
DR PIR; C96558; C96558.
DR RefSeq; NP_001319201.1; NM_001333514.1.
DR AlphaFoldDB; Q9FZB1; -.
DR SMR; Q9FZB1; -.
DR BioGRID; 26840; 22.
DR IntAct; Q9FZB1; 22.
DR STRING; 3702.AT1G51880.1; -.
DR PaxDb; Q9FZB1; -.
DR PRIDE; Q9FZB1; -.
DR EnsemblPlants; AT1G51880.1; AT1G51880.1; AT1G51880.
DR GeneID; 841615; -.
DR Gramene; AT1G51880.1; AT1G51880.1; AT1G51880.
DR KEGG; ath:AT1G51880; -.
DR Araport; AT1G51880; -.
DR HOGENOM; CLU_000288_41_1_1; -.
DR InParanoid; Q9FZB1; -.
DR PhylomeDB; Q9FZB1; -.
DR PRO; PR:Q9FZB1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FZB1; baseline and differential.
DR Genevisible; Q9FZB1; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP 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; IEA:UniProtKB-KW.
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; IPR024788; Malectin-like_Carb-bd_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF12819; Malectin_like; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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; Glycoprotein; Kinase; Leucine-rich repeat; Membrane;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..872
FT /note="Probable LRR receptor-like serine/threonine-protein
FT kinase At1g51880"
FT /id="PRO_0000387531"
FT TOPO_DOM 24..513
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 514..534
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 535..872
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 411..434
FT /note="LRR 1"
FT REPEAT 435..457
FT /note="LRR 2"
FT REPEAT 459..482
FT /note="LRR 3"
FT DOMAIN 566..838
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 690
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 572..580
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 593
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 557
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 638
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 724
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 725
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 730
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 738
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 872 AA; 97284 MW; 52203C4B2DC2E1BE CRC64;
MKSIHGFLLF LITAYVILES VQAQDQLGFI SLDCGLVPKN ATYTEKTTNI TYKSDANYID
SGLVGRISAE YKAQLQQQTW TVRSFPEGER NCYNFNLTAK SRYLIRATFT YGNYDGLRQV
PKFDIHIGPS KWTSVKLDGV GNGAVLEMIH VLTQDRLQIC LVKTGKGIPF ISSLELRPLN
NNTYLTQSGS LIGFARVFFS ATPTFIRYDE DIHDRVWVRQ FGNGLKSIST DLLVDTSNPY
DVPQAVAKTA CVPSNASQPL IFDWTLDNIT SQSYVYMHFA EIQTLKDNDI REFNITYNGG
QNVYSYLRPE KFEISTLFDS KPLSSPDGSF SLSFTKTGNS TLPPLINGLE IYKVLDLLEL
ETDQDEVSAM INIKATYDLS KKVSWQGDPC APKSYQWEGL NCSYPNSDQP RIISLNLAEN
KLTGTITPEI SKLTQLIELD LSKNDLSGEI PEFFADMKLL KLINLSGNLG LNSTIPDSIQ
QRLDSKSLIL ILSKTVTKTV TLKGKSKKVP MIPIVASVAG VFALLVILAI FFVVRRKNGE
SNKGTNPSII TKERRITYPE VLKMTNNFER VLGKGGFGTV YHGNLEDTQV AVKMLSHSSA
QGYKEFKAEV ELLLRVHHRN LVGLVGYCDD GDNLALIYEY MANGDLKENM SGKRGGNVLT
WENRMQIAVE AAQGLEYLHN GCTPPMVHRD VKTTNILLNE RYGAKLADFG LSRSFPVDGE
SHVSTVVAGT PGYLDPEYYR TNWLSEKSDV YSFGVVLLEI VTNQPVTDKT RERTHINEWV
GSMLTKGDIK SILDPKLMGD YDTNGAWKIV ELALACVNPS SNRRPTMAHV VTELNECVAL
ENARRQGREE MHTSGYVDFS RSSASEFSPG AR
