Y1497_ARATH
ID Y1497_ARATH Reviewed; 663 AA.
AC Q9FX99; Q2V4H6; Q3ECT5; Q3ECT6;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Probable receptor-like protein kinase At1g49730;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At1g49730; ORFNames=F14J22.6;
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).
RC STRAIN=cv. Columbia; TISSUE=Root;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 13-663 (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(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:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9FX99-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FX99-2; Sequence=VSP_040165;
CC Name=3;
CC IsoId=Q9FX99-3; Sequence=VSP_040162, VSP_040163, VSP_040164;
CC Name=4;
CC IsoId=Q9FX99-4; Sequence=VSP_040163, VSP_040164;
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; AC011807; AAG13055.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32467.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32468.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32469.1; -; Genomic_DNA.
DR EMBL; AK316917; BAH19622.1; -; mRNA.
DR EMBL; BT029772; ABM06042.1; -; mRNA.
DR EMBL; BX813719; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; H96533; H96533.
DR RefSeq; NP_001031164.1; NM_001036087.2. [Q9FX99-2]
DR RefSeq; NP_564552.1; NM_103860.3. [Q9FX99-4]
DR RefSeq; NP_973997.1; NM_202268.3. [Q9FX99-3]
DR AlphaFoldDB; Q9FX99; -.
DR SMR; Q9FX99; -.
DR BioGRID; 26621; 2.
DR IntAct; Q9FX99; 2.
DR STRING; 3702.AT1G49730.1; -.
DR iPTMnet; Q9FX99; -.
DR PaxDb; Q9FX99; -.
DR ProteomicsDB; 242419; -. [Q9FX99-1]
DR EnsemblPlants; AT1G49730.1; AT1G49730.1; AT1G49730.
DR EnsemblPlants; AT1G49730.2; AT1G49730.2; AT1G49730. [Q9FX99-4]
DR EnsemblPlants; AT1G49730.3; AT1G49730.3; AT1G49730. [Q9FX99-3]
DR EnsemblPlants; AT1G49730.4; AT1G49730.4; AT1G49730. [Q9FX99-2]
DR GeneID; 841396; -.
DR Gramene; AT1G49730.1; AT1G49730.1; AT1G49730.
DR Gramene; AT1G49730.2; AT1G49730.2; AT1G49730. [Q9FX99-4]
DR Gramene; AT1G49730.3; AT1G49730.3; AT1G49730. [Q9FX99-3]
DR Gramene; AT1G49730.4; AT1G49730.4; AT1G49730. [Q9FX99-2]
DR KEGG; ath:AT1G49730; -.
DR Araport; AT1G49730; -.
DR eggNOG; KOG1187; Eukaryota.
DR InParanoid; Q9FX99; -.
DR PhylomeDB; Q9FX99; -.
DR PRO; PR:Q9FX99; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FX99; baseline and differential.
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; IEA:UniProtKB-KW.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:InterPro.
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; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR043891; SPARK.
DR InterPro; IPR045271; SRF-like.
DR PANTHER; PTHR27001; PTHR27001; 1.
DR Pfam; PF00069; Pkinase; 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 Alternative splicing; ATP-binding; Cell membrane; Glycoprotein; Kinase;
KW Membrane; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..663
FT /note="Probable receptor-like protein kinase At1g49730"
FT /id="PRO_0000401338"
FT TOPO_DOM 26..254
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 276..663
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 327..609
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 213..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..663
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 451
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 333..341
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 355
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..56
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_040162"
FT VAR_SEQ 436..450
FT /note="LEYLHFYCDPPLCHR -> LVNIPKSFIYIFSVN (in isoform 3 and
FT isoform 4)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_040163"
FT VAR_SEQ 451..663
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_040164"
FT VAR_SEQ 533..572
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_040165"
SQ SEQUENCE 663 AA; 72942 MW; FBA923AFAAEE4785 CRC64;
MVVNSQAFLL ALIALLATQL PSLMAADCPL DFSGSNFTLV ATVCSNITNR GKCCRYMNAF
VAVSVARYAN LSTNLGVTSD LSETCIASIS RAMEGYGVSR NATSFCGLGT KILVKYDCDG
RTTVTQMHQS PGFGHVSRNC RLPFSPGHQC RKCLNSGITY LRNLIGAETN NITLCTCRDA
TYATLASRID DTSALELLSC FFQVTELNIP SESFSPVASP EPSPSTVGGI SPSNSDSQMT
TSRSTNPYHL TMVPTIGIVV TAVALTMLVV LVILIRRKNR ELDESESLDR KSTKSVPSSL
PVFKIHEDDS SSAFRKFSYK EMTNATNDFN TVIGQGGFGT VYKAEFNDGL IAAVKKMNKV
SEQAEQDFCR EIGLLAKLHH RNLVALKGFC INKKERFLVY DYMKNGSLKD HLHAIGKPPP
SWGTRMKIAI DVANALEYLH FYCDPPLCHR DIKSSNILLD ENFVAKLSDF GLAHSSRDGS
VCFEPVNTDI RGTPGYVDPE YVVTQELTEK SDVYSYGVVL LELITGRRAV DEGRNLVEMS
QRFLLAKSKH LELVDPRIKD SINDAGGKQL DAVVTVVRLC TEKEGRSRPS IKQVLRLLCE
SCDPVHSAFA KAVEEEIGWD SRKRSNLRIQ RGDSRIFGPS SSTTSRSHYS RSLPHSPING
FSF
