RKF1_ARATH
ID RKF1_ARATH Reviewed; 1021 AA.
AC Q9FXF2; O22579; Q8RWZ9; Q9C6G6;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Probable LRR receptor-like serine/threonine-protein kinase RFK1;
DE EC=2.7.11.1;
DE AltName: Full=Receptor-like kinase in flowers 1;
DE Flags: Precursor;
GN Name=RKF1; OrderedLocusNames=At1g29750; ORFNames=F1N18.19, T3M22.1;
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] (ISOFORM 1), CATALYTIC ACTIVITY, DEVELOPMENTAL
RP STAGE, 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 [2]
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 [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] (ISOFORM 2).
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] (ISOFORM 2).
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 Evidence={ECO:0000269|PubMed:9687063};
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; Evidence={ECO:0000269|PubMed:9687063};
CC -!- INTERACTION:
CC Q9FXF2-2; Q9M9S4: At1g14390; NbExp=2; IntAct=EBI-20652553, EBI-16954682;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FXF2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FXF2-2; Sequence=VSP_038277;
CC -!- TISSUE SPECIFICITY: Mostly expressed in flower buds, especially in
CC stamens. {ECO:0000269|PubMed:9687063}.
CC -!- DEVELOPMENTAL STAGE: First detected in early flower primordia and
CC during stamen development. Later expressed in anthers and in pollen.
CC {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; AF024648; AAC50043.1; -; mRNA.
DR EMBL; AC008030; AAG10619.1; -; Genomic_DNA.
DR EMBL; AC079288; AAG50773.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31124.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31125.1; -; Genomic_DNA.
DR EMBL; AY091006; AAM14028.1; -; mRNA.
DR EMBL; AY142598; AAN13167.1; -; mRNA.
DR EMBL; FJ708642; ACN59238.1; -; mRNA.
DR PIR; A86421; A86421.
DR RefSeq; NP_174268.7; NM_102715.8. [Q9FXF2-1]
DR RefSeq; NP_850955.5; NM_180624.6. [Q9FXF2-2]
DR AlphaFoldDB; Q9FXF2; -.
DR SMR; Q9FXF2; -.
DR BioGRID; 25088; 6.
DR IntAct; Q9FXF2; 7.
DR STRING; 3702.AT1G29750.2; -.
DR PaxDb; Q9FXF2; -.
DR PRIDE; Q9FXF2; -.
DR ProteomicsDB; 234813; -. [Q9FXF2-1]
DR EnsemblPlants; AT1G29750.1; AT1G29750.1; AT1G29750. [Q9FXF2-2]
DR EnsemblPlants; AT1G29750.2; AT1G29750.2; AT1G29750. [Q9FXF2-1]
DR GeneID; 839853; -.
DR Gramene; AT1G29750.1; AT1G29750.1; AT1G29750. [Q9FXF2-2]
DR Gramene; AT1G29750.2; AT1G29750.2; AT1G29750. [Q9FXF2-1]
DR KEGG; ath:AT1G29750; -.
DR Araport; AT1G29750; -.
DR TAIR; locus:2203847; AT1G29750.
DR eggNOG; ENOG502QW9B; Eukaryota.
DR InParanoid; Q9FXF2; -.
DR OMA; WAMECED; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9FXF2; -.
DR PRO; PR:Q9FXF2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FXF2; baseline and differential.
DR Genevisible; Q9FXF2; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; IDA:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR021720; Malectin_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; PF11721; Malectin; 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 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Glycoprotein; Kinase;
KW Leucine-rich repeat; Membrane; Nucleotide-binding; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Serine/threonine-protein kinase;
KW Signal; Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..39
FT /evidence="ECO:0000255"
FT CHAIN 40..1021
FT /note="Probable LRR receptor-like serine/threonine-protein
FT kinase RFK1"
FT /id="PRO_0000387519"
FT TOPO_DOM 41..625
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 626..646
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 647..1021
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 99..122
FT /note="LRR 1"
FT REPEAT 123..146
FT /note="LRR 2"
FT REPEAT 148..168
FT /note="LRR 3"
FT REPEAT 169..192
FT /note="LRR 4"
FT REPEAT 193..216
FT /note="LRR 5"
FT REPEAT 218..240
FT /note="LRR 6"
FT REPEAT 241..266
FT /note="LRR 7"
FT REPEAT 288..312
FT /note="LRR 8"
FT REPEAT 313..336
FT /note="LRR 9"
FT REPEAT 338..359
FT /note="LRR 10"
FT REPEAT 361..381
FT /note="LRR 11"
FT DOMAIN 681..956
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 985..1021
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 986..1010
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 807
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 687..695
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 709
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 670
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 754
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 840
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 841
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 846
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 854
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 136
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 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
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 512
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 3..46
FT /note="SLYQILAEKKKKKKNDLNIFAFSVFAIICFKFYSVNAIKLPQQE -> VKAK
FT KSVILVVAQVIELIFYDVCFCVCSL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172,
FT ECO:0000303|PubMed:20064227"
FT /id="VSP_038277"
FT CONFLICT 25
FT /note="S -> P (in Ref. 1; AAC50043)"
FT /evidence="ECO:0000305"
FT CONFLICT 398..408
FT /note="KSSKFLPCIKD -> NRANFCRVSR (in Ref. 1; AAC50043)"
FT /evidence="ECO:0000305"
FT CONFLICT 434
FT /note="T -> P (in Ref. 1; AAC50043)"
FT /evidence="ECO:0000305"
FT CONFLICT 927
FT /note="V -> G (in Ref. 1; AAC50043)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1021 AA; 113463 MW; 9F35CBFEA5A1CC1A CRC64;
MISLYQILAE KKKKKKNDLN IFAFSVFAII CFKFYSVNAI KLPQQEVDAL QQIATTLGSK
FWKFDAENCK IEMVGLTETP PPTAKQEIEC ECSPTNDTDC HVVKFAFKDH NLPGTLPQIV
KLPYLREIDL AYNYINGTLP REWASSNLTF ISLLVNRLSG EIPKEFGNSS LTYLDLESNA
FSGTIPQELG NLVHLKKLLL SSNKLTGTLP ASLARLQNMT DFRINDLQLS GTIPSYIQNW
KQLERLEMIA SGLTGPIPSV ISVLSNLVNL RISDIRGPVQ PFPSLKNVTG LTKIILKNCN
ISGQIPTYLS HLKELETLDL SFNKLVGGIP SFAQAENLRF IILAGNMLEG DAPDELLRDG
ITVDLSYNNL KWQSPESRAC RPNMNLNLNL FQSTSTKKSS KFLPCIKDFK CPRYSSCLHV
NCGGSDMYVK EKKTKELYEG DGNVEGGAAK YFLKPDANWG FSSTGDFMDD NNFQNTRFTM
FVPASNQSDL YKSARIAPVS LTYFHACLEN GNYTINLDFA EIRFTNDENY NRLGRRLFDI
YIQEKLVAKD FNIMDEAKGA QTPIIKPLTA YVTNHFLTIR LSWAGKGTTR IPTRGVYGPI
ISAISIVSDS KPCERPKTGM SPGAYIAIGI GAPCLIIFIL GFLWICGCLP RCGRQRKDPY
EEELPSGTFT LRQIKFATDD FNPTNKIGEG GFGAVFKGVL ADGRVVAVKQ LSSKSRQGNR
EFLNEIGAIS CLQHPNLVKL HGFCVERAQL LLAYEYMENN SLSSALFSPK HKQIPMDWPT
RFKICCGIAK GLAFLHEESP LKFVHRDIKA TNILLDKDLT PKISDFGLAR LDEEEKTHIS
TKVAGTIGYM APEYALWGYL TFKADVYSFG VLVLEIVAGI TNSNFMGAGD SVCLLEFANE
CVESGHLMQV VDERLRPEVD RKEAEAVIKV ALVCSSASPT DRPLMSEVVA MLEGLYPVPE
STPGVSRNAG DIRFKAFKDL RRGMENNSKT QCSVKSYPSS SSTSSGAGQA VQERKKEESR
P
