Y1719_ARATH
ID Y1719_ARATH Reviewed; 601 AA.
AC O04567; Q0WPX0;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Probable inactive receptor kinase At1g27190;
DE Flags: Precursor;
GN OrderedLocusNames=At1g27190; ORFNames=T7N9.25;
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 1).
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-586, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
CC -!- INTERACTION:
CC O04567; Q8VYT3: At4g30520; NbExp=2; IntAct=EBI-1238687, EBI-16902452;
CC O04567; Q9ASS4: At5g48380; NbExp=2; IntAct=EBI-1238687, EBI-6298290;
CC O04567; A0A178UFM8: AXX17_At5g50380; NbExp=2; IntAct=EBI-1238687, EBI-20653342;
CC O04567; Q94F62: BAK1; NbExp=2; IntAct=EBI-1238687, EBI-617138;
CC O04567; Q6XAT2: ERL2; NbExp=2; IntAct=EBI-1238687, EBI-16895926;
CC O04567; Q9LFS4: NIK1; NbExp=2; IntAct=EBI-1238687, EBI-16146189;
CC O04567; Q9ZRF9: RPK1; NbExp=2; IntAct=EBI-1238687, EBI-1238953;
CC O04567; Q6R2K3: SRF3; NbExp=2; IntAct=EBI-1238687, EBI-20651925;
CC O04567; Q9C8M9: SRF6; NbExp=2; IntAct=EBI-1238687, EBI-16954301;
CC O04567; Q8RWZ1: SUB; NbExp=2; IntAct=EBI-1238687, EBI-17072125;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O04567-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O04567-2; Sequence=VSP_028261;
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
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; AC000348; AAF79872.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30792.1; -; Genomic_DNA.
DR EMBL; BT015801; AAU94364.1; -; mRNA.
DR EMBL; AK228940; BAF00829.1; -; mRNA.
DR RefSeq; NP_174039.1; NM_102481.4. [O04567-1]
DR PDB; 6FG8; X-ray; 1.25 A; B=1-214.
DR PDB; 6G3W; X-ray; 2.20 A; B/D=25-214.
DR PDBsum; 6FG8; -.
DR PDBsum; 6G3W; -.
DR AlphaFoldDB; O04567; -.
DR SMR; O04567; -.
DR BioGRID; 24843; 59.
DR IntAct; O04567; 69.
DR STRING; 3702.AT1G27190.1; -.
DR iPTMnet; O04567; -.
DR PaxDb; O04567; -.
DR PRIDE; O04567; -.
DR ProteomicsDB; 242988; -. [O04567-1]
DR EnsemblPlants; AT1G27190.1; AT1G27190.1; AT1G27190. [O04567-1]
DR GeneID; 839608; -.
DR Gramene; AT1G27190.1; AT1G27190.1; AT1G27190. [O04567-1]
DR KEGG; ath:AT1G27190; -.
DR Araport; AT1G27190; -.
DR TAIR; locus:2205834; AT1G27190.
DR eggNOG; ENOG502QRP1; Eukaryota.
DR HOGENOM; CLU_000288_92_6_1; -.
DR InParanoid; O04567; -.
DR OMA; ITTRTGV; -.
DR PhylomeDB; O04567; -.
DR PRO; PR:O04567; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O04567; baseline and differential.
DR Genevisible; O04567; 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:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR Pfam; PF13516; LRR_6; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Glycoprotein;
KW Leucine-rich repeat; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..601
FT /note="Probable inactive receptor kinase At1g27190"
FT /id="PRO_0000305184"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 73..95
FT /note="LRR 1"
FT REPEAT 97..119
FT /note="LRR 2"
FT REPEAT 122..144
FT /note="LRR 3"
FT REPEAT 146..169
FT /note="LRR 4"
FT REPEAT 170..192
FT /note="LRR 5"
FT DOMAIN 301..586
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 307..315
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 329
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 298
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9LSI9"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LSI9"
FT MOD_RES 399
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 476
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 478
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 479
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 586
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..294
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_028261"
FT HELIX 27..37
FT /evidence="ECO:0007829|PDB:6FG8"
FT TURN 44..47
FT /evidence="ECO:0007829|PDB:6FG8"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:6FG8"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:6FG8"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:6G3W"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:6FG8"
FT HELIX 90..94
FT /evidence="ECO:0007829|PDB:6FG8"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:6FG8"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:6FG8"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:6FG8"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:6FG8"
FT HELIX 139..143
FT /evidence="ECO:0007829|PDB:6FG8"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:6FG8"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:6FG8"
FT HELIX 163..167
FT /evidence="ECO:0007829|PDB:6FG8"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:6FG8"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:6FG8"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:6FG8"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:6FG8"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:6FG8"
SQ SEQUENCE 601 AA; 65424 MW; 7A263A3076F5D8A9 CRC64;
MKKIFITLLW LLFISSFLCS SSSAEDDVLC LQGLKNSLID PSSRLSSWSF PNSSASSICK
LTGVSCWNEK ENRIISLQLQ SMQLAGEIPE SLKLCRSLQS LDLSGNDLSG SIPSQICSWL
PYLVTLDLSG NKLGGSIPTQ IVECKFLNAL ILSDNKLSGS IPSQLSRLDR LRRLSLAGND
LSGTIPSELA RFGGDDFSGN NGLCGKPLSR CGALNGRNLS IIIVAGVLGA VGSLCVGLVI
FWWFFIREGS RKKKGYGAGK SKDDSDWIGL LRSHKLVQVT LFQKPIVKIK LGDLMAATNN
FSSGNIDVSS RTGVSYKADL PDGSALAVKR LSACGFGEKQ FRSEMNKLGE LRHPNLVPLL
GYCVVEDERL LVYKHMVNGT LFSQLHNGGL CDAVLDWPTR RAIGVGAAKG LAWLHHGCQP
PYLHQFISSN VILLDDDFDA RITDYGLAKL VGSRDSNDSS FNNGDLGELG YVAPEYSSTM
VASLKGDVYG FGIVLLELVT GQKPLSVING VEGFKGSLVD WVSQYLGTGR SKDAIDRSIC
DKGHDEEILQ FLKIACSCVV SRPKERPTMI QVYESLKNMA DKHGVSEHYD EFPLVFNKQE
A
