SYNM_MOUSE
ID SYNM_MOUSE Reviewed; 477 AA.
AC Q8BGV0;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Probable asparagine--tRNA ligase, mitochondrial;
DE EC=6.1.1.22;
DE AltName: Full=Asparaginyl-tRNA synthetase;
DE Short=AsnRS;
DE Flags: Precursor;
GN Name=Nars2;
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;
RC TISSUE=Cerebellum, Hippocampus, Hypothalamus, and Medulla oblongata;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, and Kidney;
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 [3]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-353, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=25807530; DOI=10.1371/journal.pgen.1005097;
RA Simon M., Richard E.M., Wang X., Shahzad M., Huang V.H., Qaiser T.A.,
RA Potluri P., Mahl S.E., Davila A., Nazli S., Hancock S., Yu M., Gargus J.,
RA Chang R., Al-Sheqaih N., Newman W.G., Abdenur J., Starr A., Hegde R.,
RA Dorn T., Busch A., Park E., Wu J., Schwenzer H., Flierl A., Florentz C.,
RA Sissler M., Khan S.N., Li R., Guan M.X., Friedman T.B., Wu D.K.,
RA Procaccio V., Riazuddin S., Wallace D.C., Ahmed Z.M., Huang T.,
RA Riazuddin S.;
RT "Mutations of human NARS2, encoding the mitochondrial asparaginyl-tRNA
RT synthetase, cause nonsyndromic deafness and Leigh syndrome.";
RL PLoS Genet. 11:E1005097-E1005097(2015).
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 -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q96I59}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q96I59}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q96I59}.
CC -!- TISSUE SPECIFICITY: Expressed in brain and inner ear, including the
CC cochlear epithelium and organ of Corti. {ECO:0000269|PubMed:25807530}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AK046799; BAC32875.1; -; mRNA.
DR EMBL; AK047091; BAC32958.1; -; mRNA.
DR EMBL; AK050718; BAC34391.1; -; mRNA.
DR EMBL; AK138260; BAE23597.1; -; mRNA.
DR EMBL; AK164179; BAE37666.1; -; mRNA.
DR CCDS; CCDS21454.1; -.
DR RefSeq; NP_705819.3; NM_153591.4.
DR AlphaFoldDB; Q8BGV0; -.
DR SMR; Q8BGV0; -.
DR BioGRID; 232609; 9.
DR STRING; 10090.ENSMUSP00000044937; -.
DR iPTMnet; Q8BGV0; -.
DR PhosphoSitePlus; Q8BGV0; -.
DR EPD; Q8BGV0; -.
DR jPOST; Q8BGV0; -.
DR MaxQB; Q8BGV0; -.
DR PaxDb; Q8BGV0; -.
DR PeptideAtlas; Q8BGV0; -.
DR PRIDE; Q8BGV0; -.
DR ProteomicsDB; 254715; -.
DR Antibodypedia; 17519; 191 antibodies from 26 providers.
DR DNASU; 244141; -.
DR Ensembl; ENSMUST00000044466; ENSMUSP00000044937; ENSMUSG00000018995.
DR GeneID; 244141; -.
DR KEGG; mmu:244141; -.
DR UCSC; uc009iiw.2; mouse.
DR CTD; 79731; -.
DR MGI; MGI:2142075; Nars2.
DR VEuPathDB; HostDB:ENSMUSG00000018995; -.
DR eggNOG; KOG0554; Eukaryota.
DR GeneTree; ENSGT01030000234618; -.
DR HOGENOM; CLU_004553_2_0_1; -.
DR InParanoid; Q8BGV0; -.
DR OMA; DNMDLAE; -.
DR OrthoDB; 1056670at2759; -.
DR PhylomeDB; Q8BGV0; -.
DR TreeFam; TF315088; -.
DR BioGRID-ORCS; 244141; 31 hits in 77 CRISPR screens.
DR ChiTaRS; Nars2; mouse.
DR PRO; PR:Q8BGV0; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BGV0; protein.
DR Bgee; ENSMUSG00000018995; Expressed in right kidney and 228 other tissues.
DR ExpressionAtlas; Q8BGV0; baseline and differential.
DR Genevisible; Q8BGV0; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO: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:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006421; P:asparaginyl-tRNA aminoacylation; ISS:UniProtKB.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00534; Asn_tRNA_synth; 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; Ligase; Mitochondrion;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..14
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 15..477
FT /note="Probable asparagine--tRNA ligase, mitochondrial"
FT /id="PRO_0000250723"
FT MOD_RES 353
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
SQ SEQUENCE 477 AA; 53962 MW; 6CCBAC318E7830DD CRC64;
MLGARRLLGA LRLCSSVSCP RPRASAKMRV RDALRVQDAR GECVTVQGWI RSVRSQKEVL
FLHVNDGSSL ESLQIVADSS FDSRELTFGS SVQVQGQLVK SQSKRQNVEL KAEKIEVIGD
CEAKAFPIKY KERHPLEYLR QYPHLRCRTN ALGSILRVRS EATAAIHSYF KDNGFVHIHT
PVLTSNDCEG AGELFQVEPS SKIKGPKESF FDVPAFLTVS GQLHLEVMSG AFTQVFTFGP
TFRAENSQSR RHLAEFYMVE AEISFVESLQ DLMQVMEELF KATTEMVLSH CPEDVELCHQ
FIAAGQKGRL EHMLKNNFLI ISYTEAIEIL KQASQNFAFT PKWGVDLQTE HEKYLVRHCG
NIPVFVINYP SELKPFYMRE NEDGPQNTVA AVDLLVPGVG ELFGGSLREE RYHVLEQRLA
RSGLTKAYQW YLDLRKFGSV PHGGFGMGFE RYLQCILGVD NIKDVIPFPR FTHSCLL
