Y3471_ARATH
ID Y3471_ARATH Reviewed; 1025 AA.
AC Q9SD62;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Putative receptor-like protein kinase At3g47110;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At3g47110; ORFNames=F13I12.160;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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).
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 ---------------------------------------------------------------------------
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; AL133292; CAB61957.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78244.1; -; Genomic_DNA.
DR PIR; T45647; T45647.
DR RefSeq; NP_190295.1; NM_114578.2.
DR AlphaFoldDB; Q9SD62; -.
DR SMR; Q9SD62; -.
DR BioGRID; 9184; 10.
DR IntAct; Q9SD62; 9.
DR STRING; 3702.AT3G47110.1; -.
DR PaxDb; Q9SD62; -.
DR PRIDE; Q9SD62; -.
DR EnsemblPlants; AT3G47110.1; AT3G47110.1; AT3G47110.
DR GeneID; 823864; -.
DR Gramene; AT3G47110.1; AT3G47110.1; AT3G47110.
DR KEGG; ath:AT3G47110; -.
DR Araport; AT3G47110; -.
DR TAIR; locus:2075661; AT3G47110.
DR eggNOG; ENOG502QPYS; Eukaryota.
DR HOGENOM; CLU_000288_22_0_1; -.
DR InParanoid; Q9SD62; -.
DR OMA; VYLHTYC; -.
DR OrthoDB; 335055at2759; -.
DR PhylomeDB; Q9SD62; -.
DR PRO; PR:Q9SD62; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SD62; baseline and differential.
DR Genevisible; Q9SD62; AT.
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: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; -; 2.
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; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 8.
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 3: Inferred from homology;
KW ATP-binding; Cell membrane; Glycoprotein; Kinase; Leucine-rich repeat;
KW Membrane; Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; Signal; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..1025
FT /note="Putative receptor-like protein kinase At3g47110"
FT /id="PRO_0000401355"
FT TOPO_DOM 31..653
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 654..674
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 675..1025
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 104..128
FT /note="LRR 1"
FT REPEAT 130..151
FT /note="LRR 2"
FT REPEAT 152..175
FT /note="LRR 3"
FT REPEAT 176..200
FT /note="LRR 4"
FT REPEAT 202..224
FT /note="LRR 5"
FT REPEAT 226..248
FT /note="LRR 6"
FT REPEAT 249..271
FT /note="LRR 7"
FT REPEAT 273..297
FT /note="LRR 8"
FT REPEAT 298..323
FT /note="LRR 9"
FT REPEAT 325..344
FT /note="LRR 10"
FT REPEAT 351..374
FT /note="LRR 11"
FT REPEAT 376..400
FT /note="LRR 12"
FT REPEAT 401..424
FT /note="LRR 13"
FT REPEAT 426..448
FT /note="LRR 14"
FT REPEAT 449..472
FT /note="LRR 15"
FT REPEAT 473..496
FT /note="LRR 16"
FT REPEAT 498..520
FT /note="LRR 17"
FT REPEAT 521..544
FT /note="LRR 18"
FT REPEAT 546..567
FT /note="LRR 19"
FT REPEAT 568..593
FT /note="LRR 20"
FT REPEAT 595..616
FT /note="LRR 21"
FT DOMAIN 719..1020
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 856
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 725..733
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 748
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 716
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 798
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 843
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 904
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 486
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 503
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 579
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 590
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 598
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 616
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1025 AA; 111538 MW; F88FAC687B8DFEA2 CRC64;
MGVPCIVMRL ILVSALLVSV SLEHSDMVCA QTIRLTEETD KQALLEFKSQ VSETSRVVLG
SWNDSLPLCS WTGVKCGLKH RRVTGVDLGG LKLTGVVSPF VGNLSFLRSL NLADNFFHGA
IPSEVGNLFR LQYLNMSNNL FGGVIPVVLS NCSSLSTLDL SSNHLEQGVP LEFGSLSKLV
LLSLGRNNLT GKFPASLGNL TSLQMLDFIY NQIEGEIPGD IARLKQMIFF RIALNKFNGV
FPPPIYNLSS LIFLSITGNS FSGTLRPDFG SLLPNLQILY MGINSFTGTI PETLSNISSL
RQLDIPSNHL TGKIPLSFGR LQNLLLLGLN NNSLGNYSSG DLDFLGALTN CSQLQYLNVG
FNKLGGQLPV FIANLSTQLT ELSLGGNLIS GSIPHGIGNL VSLQTLDLGE NLLTGKLPPS
LGELSELRKV LLYSNGLSGE IPSSLGNISG LTYLYLLNNS FEGSIPSSLG SCSYLLDLNL
GTNKLNGSIP HELMELPSLV VLNVSFNLLV GPLRQDIGKL KFLLALDVSY NKLSGQIPQT
LANCLSLEFL LLQGNSFVGP IPDIRGLTGL RFLDLSKNNL SGTIPEYMAN FSKLQNLNLS
LNNFDGAVPT EGVFRNTSAM SVFGNINLCG GIPSLQLQPC SVELPRRHSS VRKIITICVS
AVMAALLLLC LCVVYLCWYK LRVKSVRANN NENDRSFSPV KSFYEKISYD ELYKTTGGFS
SSNLIGSGNF GAVFKGFLGS KNKAVAIKVL NLCKRGAAKS FIAECEALGG IRHRNLVKLV
TICSSSDFEG NDFRALVYEF MPNGNLDMWL HPDEIEETGN PSRTLGLFAR LNIAIDVASA
LVYLHTYCHN PIAHCDIKPS NILLDKDLTA HVSDFGLAQL LLKFDRDTFH IQFSSAGVRG
TIGYAAPEYG MGGHPSIMGD VYSFGIVLLE IFTGKRPTNK LFVDGLTLHS FTKSALQKRQ
ALDITDETIL RGAYAQHFNM VECLTLVFRV GVSCSEESPV NRISMAEAIS KLVSIRESFF
RDEET
