RKF3_ARATH
ID RKF3_ARATH Reviewed; 617 AA.
AC P93050;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Probable LRR receptor-like serine/threonine-protein kinase RKF3;
DE EC=2.7.11.1;
DE AltName: Full=Receptor-like kinase in flowers 3;
DE Flags: Precursor;
GN Name=RKF3; Synonyms=AT2324; OrderedLocusNames=At2g48010; ORFNames=T9J23.16;
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 [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. C24;
RX PubMed=9484433; DOI=10.1023/a:1005902730810;
RA Kertbundit S., Linacero R., Rouze P., Galis I., Macas J., Deboeck F.,
RA Renckens S., Hernalsteens J.-P., de Greve H.;
RT "Analysis of T-DNA-mediated translational beta-glucuronidase gene
RT fusions.";
RL Plant Mol. Biol. 36:205-217(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=9687063; DOI=10.1023/a:1005924817190;
RA Takahashi T., Mu J.-H., Gasch A., Chua N.-H.;
RT "Identification by PCR of receptor-like protein kinases from Arabidopsis
RT flowers.";
RL Plant Mol. Biol. 37:587-596(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
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 [5]
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 [6]
RP SUBCELLULAR LOCATION.
RX PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT phosphorylation site database.";
RL Plant Cell 16:2394-2405(2004).
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:0000269|PubMed:15308754};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:15308754}.
CC -!- TISSUE SPECIFICITY: Expressed in the whole plant at low levels.
CC {ECO:0000269|PubMed:9484433, ECO:0000269|PubMed:9687063}.
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; Z84202; CAB06335.1; -; Genomic_DNA.
DR EMBL; AF024650; AAC50045.1; -; mRNA.
DR EMBL; AC006072; AAD13705.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10923.1; -; Genomic_DNA.
DR EMBL; AY037237; AAK59837.1; -; mRNA.
DR EMBL; BT000518; AAN18087.1; -; mRNA.
DR PIR; C84922; C84922.
DR RefSeq; NP_182322.1; NM_130368.4.
DR AlphaFoldDB; P93050; -.
DR SMR; P93050; -.
DR BioGRID; 4748; 6.
DR IntAct; P93050; 7.
DR STRING; 3702.AT2G48010.1; -.
DR iPTMnet; P93050; -.
DR SwissPalm; P93050; -.
DR PaxDb; P93050; -.
DR PRIDE; P93050; -.
DR ProteomicsDB; 234716; -.
DR EnsemblPlants; AT2G48010.1; AT2G48010.1; AT2G48010.
DR GeneID; 819413; -.
DR Gramene; AT2G48010.1; AT2G48010.1; AT2G48010.
DR KEGG; ath:AT2G48010; -.
DR Araport; AT2G48010; -.
DR TAIR; locus:2066390; AT2G48010.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_0_0_1; -.
DR InParanoid; P93050; -.
DR OMA; ENSSPCA; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; P93050; -.
DR PRO; PR:P93050; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P93050; baseline and differential.
DR Genevisible; P93050; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
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; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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 InterPro; IPR043891; SPARK.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF19160; SPARK; 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; Cell membrane; Glycoprotein; Kinase; Membrane;
KW Nucleotide-binding; Receptor; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..617
FT /note="Probable LRR receptor-like serine/threonine-protein
FT kinase RKF3"
FT /id="PRO_0000387520"
FT TOPO_DOM 21..212
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..617
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 283..563
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 585..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 412
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 289..297
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 311
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 22
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 124
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 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 617 AA; 67224 MW; 295D694B8563408A CRC64;
MLFLRRIAVV FFVFTSFSAA QNSTCPLDFS VLEPFRRPKP DGATTCQYLL QGLRLLYSHH
LRQTGSFLPP PESAASCWAA LQSSVAGFLP RFDVRSTCGF QTPWISQGCM DITTRSQFES
LIPNSSLATT AMRCNTSLES NTPCASCTQS LSAFQPYLSG PSLGNVSDCA SFPSIYAAAF
ANSLGPTDKG TAKCLFQLDL ASPTSSGANK VKVLVSSFSV LLVASVLVIT AWFWYCRRKK
SKLLKPRDTS LEAGTQSRLD SMSESTTLVK FSFDEIKKAT NNFSRHNIIG RGGYGNVFKG
ALPDGTQVAF KRFKNCSAGG DANFAHEVEV IASIRHVNLL ALRGYCTATT PYEGHQRIIV
CDLVSNGSLH DHLFGDLEAQ LAWPLRQRIA LGMARGLAYL HYGAQPSIIH RDIKASNILL
DERFEAKVAD FGLAKFNPEG MTHMSTRVAG TMGYVAPEYA LYGQLTEKSD VYSFGVVLLE
LLSRRKAIVT DEEGQPVSVA DWAWSLVREG QTLDVVEDGM PEKGPPEVLE KYVLIAVLCS
HPQLHARPTM DQVVKMLESN EFTVIAIPQR PIPLVACREE IDRSVSSSSG SGKLTSPTGY
QAFSFGGDGP SGNTNTT
