SYNC_MOUSE
ID SYNC_MOUSE Reviewed; 559 AA.
AC Q8BP47; Q3T9A7; Q7TPX0; Q9CRY5;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Asparagine--tRNA ligase, cytoplasmic;
DE EC=6.1.1.22 {ECO:0000250|UniProtKB:O43776};
DE AltName: Full=Asparaginyl-tRNA synthetase;
DE Short=AsnRS;
DE AltName: Full=Asparaginyl-tRNA synthetase 1;
GN Name=NARS1; Synonyms=Nars;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, and Spleen;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C3H/He; TISSUE=Osteoblast;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-493, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-501, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Catalyzes the attachment of asparagine to tRNA(Asn) in a two-
CC step reaction: asparagine is first activated by ATP to form Asn-AMP and
CC then transferred to the acceptor end of tRNA(Asn). In addition to its
CC essential role in protein synthesis, acts as a signaling molecule that
CC induced migration of CCR3-expressing cells. Has an essential role in
CC the development of the cerebral cortex, being required for proper
CC proliferation of radial glial cells. {ECO:0000250|UniProtKB:O43776}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + H(+) + L-
CC asparaginyl-tRNA(Asn); Xref=Rhea:RHEA:11180, Rhea:RHEA-COMP:9659,
CC Rhea:RHEA-COMP:9674, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58048, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78515, ChEBI:CHEBI:456215; EC=6.1.1.22;
CC Evidence={ECO:0000250|UniProtKB:O43776};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O43776}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O43776}.
CC -!- DOMAIN: The N-terminal domain (1-77) recruits and activates specific
CC immune cells by interacting with CCR3-expressing cells.
CC {ECO:0000250|UniProtKB:O43776}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH52849.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB29032.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK013880; BAB29032.1; ALT_INIT; mRNA.
DR EMBL; AK077699; BAC36965.1; -; mRNA.
DR EMBL; AK172657; BAE43117.1; -; mRNA.
DR EMBL; BC052849; AAH52849.1; ALT_INIT; mRNA.
DR RefSeq; NP_001136422.1; NM_001142950.1.
DR RefSeq; NP_081626.2; NM_027350.3.
DR AlphaFoldDB; Q8BP47; -.
DR SMR; Q8BP47; -.
DR BioGRID; 213922; 16.
DR IntAct; Q8BP47; 3.
DR MINT; Q8BP47; -.
DR STRING; 10090.ENSMUSP00000025483; -.
DR iPTMnet; Q8BP47; -.
DR PhosphoSitePlus; Q8BP47; -.
DR SwissPalm; Q8BP47; -.
DR EPD; Q8BP47; -.
DR jPOST; Q8BP47; -.
DR MaxQB; Q8BP47; -.
DR PaxDb; Q8BP47; -.
DR PeptideAtlas; Q8BP47; -.
DR PRIDE; Q8BP47; -.
DR ProteomicsDB; 263182; -.
DR Antibodypedia; 9706; 197 antibodies from 29 providers.
DR DNASU; 70223; -.
DR Ensembl; ENSMUST00000237400; ENSMUSP00000157402; ENSMUSG00000024587.
DR GeneID; 70223; -.
DR KEGG; mmu:70223; -.
DR UCSC; uc008fek.2; mouse.
DR CTD; 70223; -.
DR MGI; MGI:1917473; Nars.
DR VEuPathDB; HostDB:ENSMUSG00000024587; -.
DR eggNOG; KOG0555; Eukaryota.
DR GeneTree; ENSGT01030000234618; -.
DR HOGENOM; CLU_004553_2_10_1; -.
DR InParanoid; Q8BP47; -.
DR OMA; CKQHTVR; -.
DR OrthoDB; 1056670at2759; -.
DR PhylomeDB; Q8BP47; -.
DR TreeFam; TF105664; -.
DR BioGRID-ORCS; 70223; 28 hits in 74 CRISPR screens.
DR ChiTaRS; Nars; mouse.
DR PRO; PR:Q8BP47; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q8BP47; protein.
DR Bgee; ENSMUSG00000024587; Expressed in facial nucleus and 263 other tissues.
DR ExpressionAtlas; Q8BP47; baseline and differential.
DR Genevisible; Q8BP47; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0004816; F:asparagine-tRNA ligase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0031728; F:CCR3 chemokine receptor binding; ISS:UniProtKB.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB.
DR GO; GO:0006421; P:asparaginyl-tRNA aminoacylation; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0021987; P:cerebral cortex development; ISO:MGI.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR InterPro; IPR004364; Aa-tRNA-synt_II.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004522; Asn-tRNA-ligase.
DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR PRINTS; PR01042; TRNASYNTHASP.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00457; asnS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 1: Evidence at protein level;
KW Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..559
FT /note="Asparagine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000176497"
FT REGION 82..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43776"
FT MOD_RES 255
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O43776"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 501
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 15
FT /note="Missing (in Ref. 1; BAB29032)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="H -> R (in Ref. 1; BAB29032)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="Q -> E (in Ref. 1; BAB29032)"
FT /evidence="ECO:0000305"
FT CONFLICT 469
FT /note="L -> P (in Ref. 1; BAE43117)"
FT /evidence="ECO:0000305"
FT CONFLICT 526
FT /note="G -> E (in Ref. 2; AAH52849)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 559 AA; 64279 MW; D5F4025B57580DBD CRC64;
MSSEVIRGTA EMVLAELYVS DREGNDATGD GTKEKPFKTG LKALMTVGKE PFPTIYVDSQ
KENERWDVIS KSQMKNIKKM WHREQMKNDS REKKEAEDNL RREKNLEEAK KIIIKNDPSL
PEPACVKISA LEGYRGQRVK VFGWVHRLRR QGKNLMFLVL RDGTGYLQCV LSDDLCQCYN
GVVLSTESSV AVYGTLNLTP KGKQAPGGHE LSCDFWELVG LAPAGGADNL INEESDVDVQ
LNNRHMMIRG ENMSKILKAR SMITRCFRDH FFDRGYCEVT TPTLVQTQVE GGATLFKLDY
FGEEAFLTQS SQLYLETCLP ALGDVFCIAQ SYRAEQSRTR RHLAEFTHVE AECPFLTFED
LLNRLEDLVC DVVDRVLKSP VASIVYELNP NFKPPKRPFR RMNYSDAIEW LKEHDVKKED
GTFYEFGDDI PEAPERLMTD TINEPILLCR FPVEIKSFYM QRCPEDPRLT ESVDVLMPNV
GEIVGGSMRS WDSEEILEGY KREGIDPAPY YWYTDQRKYG TCPHGGYGLG LERFLSWILN
RYHIRDVCLY PRFLQRCRP
