ATE1_DROME
ID ATE1_DROME Reviewed; 484 AA.
AC O96539; Q7KRL0; Q86PB1; Q8IH08; Q8N0R9; Q8T7L5; Q9V906; Q9V907;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 3.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Arginyl-tRNA--protein transferase 1;
DE Short=Arginyltransferase 1;
DE Short=R-transferase 1;
DE EC=2.3.2.8;
DE AltName: Full=Arginine-tRNA--protein transferase 1;
GN Name=Ate1; ORFNames=CG9204;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
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=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 163-484 (ISOFORM C).
RA Picaud F., Petit D., Maftah A.;
RT "Independent emergence of alternative splicing of arginyl-tRNA-protein
RT transferase in Drosophila melanogaster and mammals.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
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 Does not arginylate cysteine residues (By similarity). {ECO:0000250}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=B;
CC IsoId=O96539-1; Sequence=Displayed;
CC Name=A;
CC IsoId=O96539-2; Sequence=VSP_000339;
CC Name=C;
CC IsoId=O96539-4; Sequence=VSP_000339, VSP_011157;
CC Name=D;
CC IsoId=O96539-5; Sequence=VSP_011157;
CC -!- SIMILARITY: Belongs to the R-transferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO25000.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAO25000.1; Type=Miscellaneous discrepancy; Note=Deletion of many residues.; Evidence={ECO:0000305};
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DR EMBL; AF079101; AAD12369.1; -; mRNA.
DR EMBL; AE013599; AAF57496.3; -; Genomic_DNA.
DR EMBL; AE013599; AAF57497.3; -; Genomic_DNA.
DR EMBL; AE013599; AAF57498.2; -; Genomic_DNA.
DR EMBL; AY051688; AAK93112.1; -; mRNA.
DR EMBL; BT001498; AAN71253.1; -; mRNA.
DR EMBL; BT003243; AAO25000.1; ALT_SEQ; mRNA.
DR EMBL; AF354710; AAL83965.1; -; mRNA.
DR RefSeq; NP_477394.3; NM_058046.5. [O96539-2]
DR RefSeq; NP_725939.2; NM_166379.3. [O96539-1]
DR RefSeq; NP_725940.2; NM_166380.3. [O96539-4]
DR AlphaFoldDB; O96539; -.
DR SMR; O96539; -.
DR STRING; 7227.FBpp0085627; -.
DR PaxDb; O96539; -.
DR PRIDE; O96539; -.
DR DNASU; 37288; -.
DR EnsemblMetazoa; FBtr0086317; FBpp0085626; FBgn0025720. [O96539-2]
DR EnsemblMetazoa; FBtr0086318; FBpp0085627; FBgn0025720. [O96539-1]
DR EnsemblMetazoa; FBtr0086319; FBpp0089149; FBgn0025720. [O96539-4]
DR EnsemblMetazoa; FBtr0336634; FBpp0307617; FBgn0025720. [O96539-5]
DR GeneID; 37288; -.
DR KEGG; dme:Dmel_CG9204; -.
DR UCSC; CG9204-RA; d. melanogaster. [O96539-1]
DR CTD; 11101; -.
DR FlyBase; FBgn0025720; Ate1.
DR VEuPathDB; VectorBase:FBgn0025720; -.
DR eggNOG; KOG1193; Eukaryota.
DR GeneTree; ENSGT00500000044926; -.
DR InParanoid; O96539; -.
DR OMA; SDRMVYS; -.
DR PhylomeDB; O96539; -.
DR BioGRID-ORCS; 37288; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 37288; -.
DR PRO; PR:O96539; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0025720; Expressed in spermathecum and 25 other tissues.
DR ExpressionAtlas; O96539; baseline and differential.
DR Genevisible; O96539; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004057; F:arginyltransferase activity; IBA:GO_Central.
DR GO; GO:0016598; P:protein arginylation; IBA:GO_Central.
DR GO; GO:0071596; P:ubiquitin-dependent protein catabolic process via the N-end rule pathway; IMP:FlyBase.
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; Alternative splicing; Reference proteome; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..484
FT /note="Arginyl-tRNA--protein transferase 1"
FT /id="PRO_0000195090"
FT VAR_SEQ 175..181
FT /note="Missing (in isoform A and isoform C)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:9858543, ECO:0000303|Ref.6"
FT /id="VSP_000339"
FT VAR_SEQ 239..288
FT /note="LRLIHVYDDEFRRTLPQSFALYKKYQISIHNDPPKDQDAYKEHLQATPLQ
FT -> IVLVASSDTERTCADAVIALYRKYQITVHNDNPARLTLASMQRFLVKSPLK (in
FT isoform C and isoform D)"
FT /evidence="ECO:0000303|Ref.5, ECO:0000303|Ref.6"
FT /id="VSP_011157"
SQ SEQUENCE 484 AA; 55317 MW; 38677BF50672AC6D CRC64;
MSLSIVSYYG SQQSKCGYCA GANCSLSHGM HAYQLDCRDY QDLIDRGWRR CGYYCYKLRN
QETCCPCYTI KCNGLEFKLS KSNKRILRRI NRFLRDGKRE SKPEAGDGDG EADADYAIVA
PEVTASEPQP QLPDKSPPVI NVEQVASLAT AQRKPTKQAT AAAVEAPTLG SNKSSLLSSS
AAAPISNKPC KKAKQMRLDR RLAKLGDSAS YSTKSLTQEK TLRDFLNTDS ETNKHRLKLR
LIHVYDDEFR RTLPQSFALY KKYQISIHND PPKDQDAYKE HLQATPLQNE KPWDGPEMGY
GSFHQQYWLD DKLIAVGVID ILPGCVSSVY FFYDPDYSFL SLGTYGSLRE IELVQSLAEK
VPSLKYYYMG FYIHSCPKMR YKGKLSPSYL LCPETYEWLP LTDVIRAKLD EHKYQRLNED
PAARDVNEFL MEHLDEVKLL LGGRTRTDYK HFRQLRGTVS DDDIIIEYSK LVGKECARRM
LYVK
