ATE2_ARATH
ID ATE2_ARATH Reviewed; 605 AA.
AC Q9C776;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Arginyl-tRNA--protein transferase 2 {ECO:0000305};
DE Short=Arginyltransferase 2 {ECO:0000305};
DE Short=R-transferase 2 {ECO:0000305};
DE EC=2.3.2.8 {ECO:0000305};
DE AltName: Full=Arginine-tRNA--protein transferase 2 {ECO:0000303|PubMed:19255443};
DE AltName: Full=AtATE2 {ECO:0000303|PubMed:19620738};
GN Name=ATE2 {ECO:0000303|PubMed:19255443};
GN OrderedLocusNames=At3g11240 {ECO:0000312|Araport:AT3G11240};
GN ORFNames=F11B9.16 {ECO:0000312|EMBL:AAG50969.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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].
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 FUNCTION, AND DISRUPTION PHENOTYPE.
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 [5]
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 [6]
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 [7]
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 ATE1 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). Involved in disease resistance (PubMed:27173012).
CC The end-rule pathway plays a role in regulating the timing and
CC amplitude of the immune response following infection with the bacterial
CC pathogen Pseudomonas syringae pv tomato (PubMed:27173012). Regulates
CC the biosynthesis of plant-defense metabolites such as glucosinolates,
CC and the biosynthesis and response to the phytohormone jasmonate (JA),
CC which plays a key role in plant immunity (PubMed:27173012).
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 -!- DISRUPTION PHENOTYPE: The double mutants ate1 and ate2 show reduced
CC seed 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:19255443, ECO:0000269|PubMed:19620738}.
CC -!- SIMILARITY: Belongs to the R-transferase family.
CC {ECO:0000255|PIRNR:PIRNR037207}.
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DR EMBL; AC073395; AAG50969.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75019.1; -; Genomic_DNA.
DR EMBL; AF370200; AAK44015.1; -; mRNA.
DR EMBL; AY056368; AAL07254.1; -; mRNA.
DR RefSeq; NP_187733.1; NM_111959.3.
DR AlphaFoldDB; Q9C776; -.
DR SMR; Q9C776; -.
DR STRING; 3702.AT3G11240.1; -.
DR PaxDb; Q9C776; -.
DR PRIDE; Q9C776; -.
DR ProteomicsDB; 246721; -.
DR EnsemblPlants; AT3G11240.1; AT3G11240.1; AT3G11240.
DR GeneID; 820295; -.
DR Gramene; AT3G11240.1; AT3G11240.1; AT3G11240.
DR KEGG; ath:AT3G11240; -.
DR Araport; AT3G11240; -.
DR TAIR; locus:2074718; AT3G11240.
DR eggNOG; KOG1193; Eukaryota.
DR HOGENOM; CLU_020349_1_0_1; -.
DR InParanoid; Q9C776; -.
DR OMA; SDRMVYS; -.
DR OrthoDB; 1446907at2759; -.
DR PhylomeDB; Q9C776; -.
DR PRO; PR:Q9C776; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9C776; baseline and differential.
DR Genevisible; Q9C776; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004057; F:arginyltransferase activity; IBA:GO_Central.
DR GO; GO:0050832; P:defense response to fungus; IGI: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 2: Evidence at transcript level;
KW Acyltransferase; Plant defense; Reference proteome; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..605
FT /note="Arginyl-tRNA--protein transferase 2"
FT /id="PRO_0000431719"
FT REGION 496..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..538
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 605 AA; 68599 MW; 362BE105ED73AABF CRC64;
MSSKKAKTKN EASSSRGGIG GESIVADCGR NKSTCGYCKS STRFSISHGL WTERLTVNDY
QALLDSGWRR SGCYLYKPEM EKTCCPSYTI RLKASDFVPS KEQQRVRRRI ERFLDGELDA
KPSEQTEDQD VSFSREVSVS VKKSLGAAKR EKNNELEPIM KDLSEQIDNA VQKCIQSGEF
PSNVQIPKAS VKKVFSAKRK KLAEGSEDLL YTSNIAFPIV AAMKHTQTLE KGKNVEENRL
SPEAVSEKLL SAMNKVGEFT GFSVKVSKGH INFLSATQVT SSDRNEGEES LCATTIKSSS
NKLHARKRKL EMHLKRSSFE PEEYELYKRY QMKVHNDKPE SISETSYKRF LVDTPLTEVP
SSGYDDEEKI PLCGFGSFHQ QYRVDDRLIA VGVIDILPKC LSSKYLFWDP DFASLSLGNY
SALQEIDWVK QNQAHCSTLE YYYLGYYIHS CNKMRYKAAY RPSELLCPLR YQWVPFEVAK
PLLDKKPYSV LSNISKVSSS SSSPQASETL LESTSEHEDM EQGDTNDDDD EMYNSDEDSD
SDSSSSRNRS DITNILISLN GPRLRYKDIP RFKNPVVQKQ LESMLVSYRK VVGAELSEIM
VYELR
