Y1972_ARATH
ID Y1972_ARATH Reviewed; 1019 AA.
AC Q9ASQ6; Q9C6G3; Q9FXE9;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Probable LRR receptor-like serine/threonine-protein kinase At1g29720;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN Name=RFK1; OrderedLocusNames=At1g29720; ORFNames=F1N18.22, T3M22.6;
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] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 720-1019 (ISOFORM 1).
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] OF 720-1019 (ISOFORM 1).
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: Cell 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=Q9ASQ6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ASQ6-3; Sequence=VSP_040679, VSP_040680;
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG10622.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG50772.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAK32925.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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; AC008030; AAG10622.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC079288; AAG50772.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31121.1; -; Genomic_DNA.
DR EMBL; AF367338; AAK32925.1; ALT_INIT; mRNA.
DR EMBL; AY113170; AAM47473.1; -; mRNA.
DR EMBL; FJ708640; ACN59236.1; -; mRNA.
DR PIR; F86420; F86420.
DR RefSeq; NP_564335.3; NM_102712.4. [Q9ASQ6-1]
DR AlphaFoldDB; Q9ASQ6; -.
DR SMR; Q9ASQ6; -.
DR BioGRID; 25085; 8.
DR IntAct; Q9ASQ6; 8.
DR STRING; 3702.AT1G29720.1; -.
DR CAZy; CBM57; Carbohydrate-Binding Module Family 57.
DR PaxDb; Q9ASQ6; -.
DR PRIDE; Q9ASQ6; -.
DR ProteomicsDB; 242424; -. [Q9ASQ6-1]
DR EnsemblPlants; AT1G29720.1; AT1G29720.1; AT1G29720. [Q9ASQ6-1]
DR GeneID; 839850; -.
DR Gramene; AT1G29720.1; AT1G29720.1; AT1G29720. [Q9ASQ6-1]
DR KEGG; ath:AT1G29720; -.
DR Araport; AT1G29720; -.
DR TAIR; locus:2019337; AT1G29720.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_114_2_1; -.
DR InParanoid; Q9ASQ6; -.
DR OMA; RSIHINC; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9ASQ6; -.
DR PRO; PR:Q9ASQ6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9ASQ6; baseline and differential.
DR Genevisible; Q9ASQ6; 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; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Cell membrane; 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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1019
FT /note="Probable LRR receptor-like serine/threonine-protein
FT kinase At1g29720"
FT /id="PRO_0000403343"
FT TOPO_DOM 20..615
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 616..636
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 637..1019
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 93..117
FT /note="LRR 1"
FT REPEAT 118..141
FT /note="LRR 2"
FT REPEAT 143..165
FT /note="LRR 3"
FT REPEAT 166..189
FT /note="LRR 4"
FT REPEAT 190..212
FT /note="LRR 5"
FT REPEAT 214..236
FT /note="LRR 6"
FT REPEAT 237..261
FT /note="LRR 7"
FT REPEAT 263..283
FT /note="LRR 8"
FT REPEAT 284..307
FT /note="LRR 9"
FT REPEAT 308..330
FT /note="LRR 10"
FT REPEAT 332..351
FT /note="LRR 11"
FT REPEAT 352..374
FT /note="LRR 12"
FT REPEAT 375..398
FT /note="LRR 13"
FT DOMAIN 673..946
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 797
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 679..687
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 701
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 746
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 830
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 831
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 836
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 844
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
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 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 469
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 558
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..591
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_040679"
FT VAR_SEQ 592..604
FT /note="AISLCHSQEPLCG -> MYIYIFTFSVSFV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_040680"
SQ SEQUENCE 1019 AA; 112763 MW; DF995D95B4329275 CRC64;
MSIILWSFFL FFTIILSSLT NITTLASFSS LHADELNALK EIATTLGIKR LNLRDEDPCS
SKTLKIIQEV DFVPNLDINN TIGCDCSFNN NTICRITELA LKTMSLRGKL PPELTKLPYL
KSIELCRNYL SGTIPMEWAK MAYLTSISVC ANNLSGNLPA GLQNFKNLTF LGVEGNQFSG
PIPDELGNLT SLTGLELASN KFTGILPGTL ARLVNLERVR ICDNNFTGII PAYIGNWTRL
QKLHLYASGL TGPIPDAVVR LENLLELSLS DTTGIKSFPN LSSKGLKRLI LRNVGLSGPI
PSYIWNLTDL KILDLSFNKL NGIVQGVQNP PKNIYLTGNL LSGNIESGGL LNSQSYIDLS
YNNFSWSSSC QKGSTINTYQ SSYSKNNLTG LPPCAVPANC KKYQRFLHIN CGGEEVSIRN
SLGKITYQTD NSRQTNAASN QQFDYWGVSN TGDFTDDNSD HDEYYTSTNL TLSGDYPDLY
KTARRSALSL VYYAFCLENG NYNVKLHFME IQFSDKEVYS RLGRRIFDVY VQGKLFLRDF
NINKEANGNM KPVIKEINAT VTNHMLEIRL YWAGKGTTLI PKRGNYGPLI SAISLCHSQE
PLCGVEKTKH HIKYPLILGA SGALVTIVLL AVGIYARGIY RRDNNRRERD LRAQGLQTVC
FSWRQLQTAT NNFDQANKLG EGGFGSVFKG ELSDGTIIAV KQLSSKSSQG NREFVNEIGM
ISGLNHPNLV KLYGCCVERD QLLLVYEYME NNSLALALFG QNSLKLDWAA RQKICVGIAR
GLEFLHDGSA MRMVHRDIKT TNVLLDTDLN AKISDFGLAR LHEAEHTHIS TKVAGTIGYM
APEYALWGQL TEKADVYSFG VVAMEIVSGK SNTKQQGNAD SVSLINWALT LQQTGDILEI
VDRMLEGEFN RSEAVRMIKV ALVCTNSSPS LRPTMSEAVK MLEGEIEITQ VMSDPGIYGH
DWSISKLRDI DTHSSSSTSG VTDQTTTTMK SSVSGCDLYP LYPESMILNS TVENSSSSL
