ATE1_ARATH
ID ATE1_ARATH Reviewed; 632 AA.
AC Q9ZT48; Q56ZQ7; Q67YK9; Q682K5;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 2.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Arginyl-tRNA--protein transferase 1 {ECO:0000305};
DE Short=Arginyltransferase 1 {ECO:0000305};
DE Short=R-transferase 1 {ECO:0000305};
DE EC=2.3.2.8 {ECO:0000305};
DE AltName: Full=Arginine-tRNA--protein transferase 1 {ECO:0000303|PubMed:9858543};
DE AltName: Full=AtATE1 {ECO:0000303|PubMed:19620738};
DE AltName: Full=Protein DELAYED-LEAF-SENESCENCE 1 {ECO:0000303|PubMed:12366806};
GN Name=ATE1 {ECO:0000303|PubMed:9858543};
GN Synonyms=DLS1 {ECO:0000303|PubMed:12366806};
GN OrderedLocusNames=At5g05700 {ECO:0000312|Araport:AT5G05700};
GN ORFNames=MJJ3.10 {ECO:0000312|EMBL:BAB09664.1};
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].
RX PubMed=9858543; DOI=10.1128/mcb.19.1.182;
RA Kwon Y.T., Kashina A.S., Varshavsky A.;
RT "Alternative splicing results in differential expression, activity, and
RT localization of the two forms of arginyl-tRNA-protein transferase, a
RT component of the N-end rule pathway.";
RL Mol. Cell. Biol. 19:182-193(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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].
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA De Los Reyes C., Quan R., Chen H., Bautista V.R., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12366806; DOI=10.1046/j.1365-313x.2002.01407.x;
RA Yoshida S., Ito M., Callis J., Nishida I., Watanabe A.;
RT "A delayed leaf senescence mutant is defective in arginyl-tRNA:protein
RT arginyltransferase, a component of the N-end rule pathway in Arabidopsis.";
RL Plant J. 32:129-137(2002).
RN [7]
RP FUNCTION.
RX PubMed=19255443; DOI=10.1073/pnas.0810280106;
RA Holman T.J., Jones P.D., Russell L., Medhurst A., Ubeda Tomas S.,
RA Talloji P., Marquez J., Schmuths H., Tung S.A., Taylor I., Footitt S.,
RA Bachmair A., Theodoulou F.L., Holdsworth M.J.;
RT "The N-end rule pathway promotes seed germination and establishment through
RT removal of ABA sensitivity in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:4549-4554(2009).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19620738; DOI=10.1073/pnas.0906404106;
RA Graciet E., Walter F., O'Maoileidigh D.S., Pollmann S., Meyerowitz E.M.,
RA Varshavsky A., Wellmer F.;
RT "The N-end rule pathway controls multiple functions during Arabidopsis
RT shoot and leaf development.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:13618-13623(2009).
RN [9]
RP FUNCTION.
RX PubMed=22020282; DOI=10.1038/nature10536;
RA Licausi F., Kosmacz M., Weits D.A., Giuntoli B., Giorgi F.M.,
RA Voesenek L.A., Perata P., van Dongen J.T.;
RT "Oxygen sensing in plants is mediated by an N-end rule pathway for protein
RT destabilization.";
RL Nature 479:419-422(2011).
RN [10]
RP FUNCTION.
RX PubMed=27173012; DOI=10.1038/srep26020;
RA de Marchi R., Sorel M., Mooney B., Fudal I., Goslin K., Kwasniewska K.,
RA Ryan P.T., Pfalz M., Kroymann J., Pollmann S., Feechan A., Wellmer F.,
RA Rivas S., Graciet E.;
RT "The N-end rule pathway regulates pathogen responses in plants.";
RL Sci. Rep. 6:26020-26020(2016).
CC -!- FUNCTION: Involved in the post-translational conjugation of arginine to
CC the N-terminal aspartate or glutamate of a protein. This arginylation
CC is required for degradation of the protein via the ubiquitin pathway.
CC Component of the N-end rule pathway with ATE2 and PRT6
CC (PubMed:19255443, PubMed:19620738, PubMed:22020282). The N-end rule
CC pathway regulates seed after-ripening, seedling sugar sensitivity,
CC seedling lipid breakdown, and abscisic acid (ABA) sensitivity of
CC germination (PubMed:19255443). The end-rule pathway regulates various
CC aspects of leaf and shoot development (PubMed:19620738). Involved in
CC the oxygen-dependent N-arginylation of RAP2-12, an activator of hypoxic
CC gene expression. This N-terminal modification leads to ubiquitination
CC by PRT6 and subsequent degradation of RAP2-12 under aerobic conditions
CC (PubMed:22020282). Has an important role in the progression of leaf
CC senescence (PubMed:12366806). Involved in disease resistance
CC (PubMed:27173012). The end-rule pathway plays a role in regulating the
CC timing and amplitude of the immune response following infection with
CC the bacterial pathogen Pseudomonas syringae pv tomato
CC (PubMed:27173012). Regulates the biosynthesis of plant-defense
CC metabolites such as glucosinolates, and the biosynthesis and response
CC to the phytohormone jasmonate (JA), which plays a key role in plant
CC immunity (PubMed:27173012). {ECO:0000269|PubMed:12366806,
CC ECO:0000269|PubMed:19255443, ECO:0000269|PubMed:19620738,
CC ECO:0000269|PubMed:22020282, ECO:0000269|PubMed:27173012}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-terminal L-alpha-aminoacyl-[protein] + L-arginyl-
CC tRNA(Arg) = H(+) + N-terminal L-arginyl-L-amino acid-[protein] +
CC tRNA(Arg); Xref=Rhea:RHEA:10208, Rhea:RHEA-COMP:9658, Rhea:RHEA-
CC COMP:9673, Rhea:RHEA-COMP:10636, Rhea:RHEA-COMP:10638,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:78442, ChEBI:CHEBI:78513,
CC ChEBI:CHEBI:78597, ChEBI:CHEBI:83562; EC=2.3.2.8;
CC Evidence={ECO:0000305};
CC -!- INTERACTION:
CC Q9ZT48; C0SUW7: ARID6; NbExp=3; IntAct=EBI-25522944, EBI-15192335;
CC Q9ZT48; Q1PF16: BHLH19; NbExp=3; IntAct=EBI-25522944, EBI-2367867;
CC Q9ZT48; O80450: GT-3B; NbExp=3; IntAct=EBI-25522944, EBI-1571089;
CC Q9ZT48; Q9C9L2: TCP15; NbExp=3; IntAct=EBI-25522944, EBI-4426144;
CC Q9ZT48; Q9MAH8: TCP3; NbExp=3; IntAct=EBI-25522944, EBI-25522447;
CC -!- DISRUPTION PHENOTYPE: Delayed leaf senescence phenotype
CC (PubMed:12366806). The double mutants ate1 and ate2 show reduced seed
CC germination potential and inhibition of seedling establishment by
CC sucrose (PubMed:19255443). The double mutants ate1 and ate2 exhibit
CC abnormal shoot and leaf development (PubMed:19620738).
CC {ECO:0000269|PubMed:12366806, ECO:0000269|PubMed:19255443,
CC ECO:0000269|PubMed:19620738}.
CC -!- SIMILARITY: Belongs to the R-transferase family. {ECO:0000305}.
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DR EMBL; AF079100; AAD12368.1; -; mRNA.
DR EMBL; AB005237; BAB09664.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90912.1; -; Genomic_DNA.
DR EMBL; AK175362; BAD43125.1; -; mRNA.
DR EMBL; AK176459; BAD44222.1; -; mRNA.
DR EMBL; AK220906; BAD94343.1; -; mRNA.
DR EMBL; BT046177; ACI49776.1; -; mRNA.
DR PIR; T51729; T51729.
DR RefSeq; NP_196189.1; NM_120652.4.
DR AlphaFoldDB; Q9ZT48; -.
DR BioGRID; 15733; 6.
DR IntAct; Q9ZT48; 5.
DR STRING; 3702.AT5G05700.1; -.
DR iPTMnet; Q9ZT48; -.
DR PaxDb; Q9ZT48; -.
DR PRIDE; Q9ZT48; -.
DR ProteomicsDB; 246540; -.
DR EnsemblPlants; AT5G05700.1; AT5G05700.1; AT5G05700.
DR GeneID; 830454; -.
DR Gramene; AT5G05700.1; AT5G05700.1; AT5G05700.
DR KEGG; ath:AT5G05700; -.
DR Araport; AT5G05700; -.
DR TAIR; locus:2166454; AT5G05700.
DR eggNOG; KOG1193; Eukaryota.
DR HOGENOM; CLU_020349_1_0_1; -.
DR InParanoid; Q9ZT48; -.
DR OMA; RYDCPYC; -.
DR OrthoDB; 1446907at2759; -.
DR PhylomeDB; Q9ZT48; -.
DR BRENDA; 2.3.2.8; 399.
DR PRO; PR:Q9ZT48; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9ZT48; baseline and differential.
DR Genevisible; Q9ZT48; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004057; F:arginyltransferase activity; IMP:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IGI:TAIR.
DR GO; GO:0010150; P:leaf senescence; IMP:TAIR.
DR GO; GO:0016598; P:protein arginylation; IBA:GO_Central.
DR GO; GO:0050994; P:regulation of lipid catabolic process; IGI:TAIR.
DR GO; GO:0010029; P:regulation of seed germination; IGI:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IGI:TAIR.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR017137; Arg-tRNA-P_Trfase_1_euk.
DR InterPro; IPR030700; N-end_Aminoacyl_Trfase.
DR InterPro; IPR007472; N-end_Aminoacyl_Trfase_C.
DR InterPro; IPR007471; N-end_Aminoacyl_Trfase_N.
DR PANTHER; PTHR21367; PTHR21367; 1.
DR Pfam; PF04377; ATE_C; 1.
DR Pfam; PF04376; ATE_N; 1.
DR PIRSF; PIRSF037207; ATE1_euk; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Plant defense; Reference proteome; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..632
FT /note="Arginyl-tRNA--protein transferase 1"
FT /id="PRO_0000195091"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..564
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 15
FT /note="S -> N (in Ref. 4; BAD44222)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="F -> S (in Ref. 4; BAD43125)"
FT /evidence="ECO:0000305"
FT CONFLICT 546..548
FT /note="Missing (in Ref. 1; AAD12368)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 632 AA; 71541 MW; F955FFD7C30182E9 CRC64;
MSLKNDASSS HDGGSNRESV IDDHGRRKST CGYCKSPARS SISHGLSAQT LTVYDYQALI
DRGWRRSGTY LYKHEMDKTC CPPYTIRLKA SDFVPTKEQQ RVSRRLERFL DGKLDVQPRE
QRGASSSGDV SDTRRKTLGA AKSEENKKVE AVMDDLSKNI DQAVQLCIRS GEFPSNMQIP
KASVKKVFCA RRKKLAEGTE QILYTSNIAF PIAAAIKRIQ TSEKEGINSA EGNRLSPETI
SEMLLSAMHK VGETPDVSIK VCKGHINFLS SAKDSFSDRD VVPNGNISRG ANSLDGSETL
HAKKDSENHQ ARKRKLEIHL KRSSFDPEEH ELYKRYQLKV HNDKPGHVVE SSYRRFLVDS
PLIDVQPSGD EKVPPCGFGS FHQQYRIDGR LIAVGVVDIL PKCLSSVYLF WDPDYAFLSL
GKYSAIQEIN WVIENQARCP SLQYYYLGYY IHSCSKMRYK AAYRPSELLC PLRFQWVPFE
VARPMLDKKP YVILSDIAIS HNQCSLLAGA SETLVEPAAS EHEDMEQGET NDNFMGCSDE
DEDEDEDDDD DDDDDEEMYE TESEDSHIES DPGSKDNDIN NILIGLYGSQ YRYKEMRQII
TPVGRKQLEP MLQSYRKVVG AELSERMVYE IN
