ATE1_MOUSE
ID ATE1_MOUSE Reviewed; 516 AA.
AC Q9Z2A5; Q8CFP7; Q9Z2A4;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 138.
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;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ATE1-1 AND ATE1-2), FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Erythroleukemia;
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 MRNA] (ISOFORM ATE1-1).
RC STRAIN=C57BL/6J; TISSUE=Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ATE1-1).
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP INTERACTION WITH LIAT1.
RX PubMed=25369936; DOI=10.1073/pnas.1419587111;
RA Brower C.S., Rosen C.E., Jones R.H., Wadas B.C., Piatkov K.I.,
RA Varshavsky A.;
RT "Liat1, an arginyltransferase-binding protein whose evolution among
RT primates involved changes in the numbers of its 10-residue repeats.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:E4936-E4945(2014).
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. {ECO:0000269|PubMed:9858543}.
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 -!- SUBUNIT: Monomer. Interacts with LIAT1. {ECO:0000269|PubMed:25369936,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform ATE1-1]: Nucleus
CC {ECO:0000269|PubMed:9858543}. Cytoplasm {ECO:0000269|PubMed:9858543}.
CC -!- SUBCELLULAR LOCATION: [Isoform ATE1-2]: Cytoplasm
CC {ECO:0000269|PubMed:9858543}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=ATE1-1;
CC IsoId=Q9Z2A5-1; Sequence=Displayed;
CC Name=ATE1-2;
CC IsoId=Q9Z2A5-2; Sequence=VSP_000337;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9858543}.
CC -!- MISCELLANEOUS: [Isoform ATE1-1]: Shows significantly higher activity
CC than isoform ATE1-2.
CC -!- SIMILARITY: Belongs to the R-transferase family. {ECO:0000305}.
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DR EMBL; AF079096; AAD12364.1; -; mRNA.
DR EMBL; AF079097; AAD12365.1; -; mRNA.
DR EMBL; AK148442; BAE28555.1; -; mRNA.
DR EMBL; AK167591; BAE39649.1; -; mRNA.
DR EMBL; BC042601; AAH42601.1; -; mRNA.
DR CCDS; CCDS21902.1; -. [Q9Z2A5-1]
DR CCDS; CCDS52414.1; -. [Q9Z2A5-2]
DR RefSeq; NP_038827.2; NM_013799.3. [Q9Z2A5-1]
DR AlphaFoldDB; Q9Z2A5; -.
DR BioGRID; 198231; 2.
DR STRING; 10090.ENSMUSP00000033139; -.
DR iPTMnet; Q9Z2A5; -.
DR PhosphoSitePlus; Q9Z2A5; -.
DR EPD; Q9Z2A5; -.
DR MaxQB; Q9Z2A5; -.
DR PaxDb; Q9Z2A5; -.
DR PRIDE; Q9Z2A5; -.
DR ProteomicsDB; 277210; -. [Q9Z2A5-1]
DR ProteomicsDB; 277211; -. [Q9Z2A5-2]
DR Antibodypedia; 32214; 188 antibodies from 31 providers.
DR DNASU; 11907; -.
DR Ensembl; ENSMUST00000033139; ENSMUSP00000033139; ENSMUSG00000030850. [Q9Z2A5-1]
DR Ensembl; ENSMUST00000035458; ENSMUSP00000043365; ENSMUSG00000030850. [Q9Z2A5-2]
DR GeneID; 11907; -.
DR KEGG; mmu:11907; -.
DR UCSC; uc009kaa.2; mouse. [Q9Z2A5-1]
DR CTD; 11101; -.
DR MGI; MGI:1333870; Ate1.
DR VEuPathDB; HostDB:ENSMUSG00000030850; -.
DR eggNOG; KOG1193; Eukaryota.
DR GeneTree; ENSGT00500000044926; -.
DR InParanoid; Q9Z2A5; -.
DR OMA; SDRMVYS; -.
DR PhylomeDB; Q9Z2A5; -.
DR TreeFam; TF105976; -.
DR BRENDA; 2.3.2.8; 3474.
DR BioGRID-ORCS; 11907; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Ate1; mouse.
DR PRO; PR:Q9Z2A5; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9Z2A5; protein.
DR Bgee; ENSMUSG00000030850; Expressed in supraoptic nucleus and 238 other tissues.
DR ExpressionAtlas; Q9Z2A5; baseline and differential.
DR Genevisible; Q9Z2A5; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0004057; F:arginyltransferase activity; IDA:MGI.
DR GO; GO:0010498; P:proteasomal protein catabolic process; ISO:MGI.
DR GO; GO:0016598; P:protein arginylation; IDA:MGI.
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; Alternative splicing; Cytoplasm; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation pathway.
FT CHAIN 1..516
FT /note="Arginyl-tRNA--protein transferase 1"
FT /id="PRO_0000195089"
FT REGION 150..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 272..312
FT /note="VVRSSPPSPQFRATFQESYQVYKRYQMVVHKDPPDKPTVSQ -> LVPASFE
FT DPEFNSSFNQSFSLYTKYQVAIHQEAPEICEKSE (in isoform ATE1-2)"
FT /evidence="ECO:0000303|PubMed:9858543"
FT /id="VSP_000337"
FT CONFLICT 362
FT /note="S -> F (in Ref. 1; AAD12364/AAD12365)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 516 AA; 59146 MW; 40CCC7756C75858A CRC64;
MASWSAPSPS LVEYFEGQTS FQCGYCKNKL GSRSYGMWAH SMTVQDYQDL IDRGWRRSGK
YVYKPVMDQT CCPQYTIRCH PLQFQPSKSH KKVLKKMLKF LAKGEISKGN CEDEPMDSTV
EDAVDGDFAL INKLDIKCDL KTLSDLKGSI ESEEKEKEKS IKKEGSKEFI HPQSIEEKLG
SGEPSHPIKV HIGPKPGKGA DLSKPPCRKA REMRKERQRL KRMQQASAAA SEAQGQPVCL
LPKAKSNQPK SLEDLIFQSL PENASHKLEV RVVRSSPPSP QFRATFQESY QVYKRYQMVV
HKDPPDKPTV SQFTRFLCSS PLEAEHPADG PECGYGSFHQ QYWLDGKIIA VGVLDILPYC
VSSVYLYYDP DYSFLSLGVY SALREIAFTR QLHEKTSQLS YYYMGFYIHS CPKMRYKGQY
RPSDLLCPET YVWVPIEQCL PSLDNSKYCR FNQDPEAEDE GRSKELDRLR VFHRRSAMPY
GVYKNHQEDP SEEAGVLEYA NLVGQKCSER MLLFRH
