SYDM_MOUSE
ID SYDM_MOUSE Reviewed; 653 AA.
AC Q8BIP0; Q5FWV4;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Aspartate--tRNA ligase, mitochondrial;
DE EC=6.1.1.12 {ECO:0000250|UniProtKB:Q6PI48};
DE AltName: Full=Aspartyl-tRNA synthetase;
DE Short=AspRS;
DE Flags: Precursor;
GN Name=Dars2;
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; TISSUE=Thymus;
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=C57BL/6J; TISSUE=Brain;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, and Spleen;
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-
CC aspartyl-tRNA(Asp); Xref=Rhea:RHEA:19649, Rhea:RHEA-COMP:9660,
CC Rhea:RHEA-COMP:9678, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78516,
CC ChEBI:CHEBI:456215; EC=6.1.1.12;
CC Evidence={ECO:0000250|UniProtKB:Q6PI48};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q6PI48}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q6PI48}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type 1 subfamily. {ECO:0000305}.
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DR EMBL; AK037337; BAC29789.1; -; mRNA.
DR EMBL; AK138809; BAE23785.1; -; mRNA.
DR EMBL; BC076606; AAH76606.1; -; mRNA.
DR EMBL; BC089191; AAH89191.1; -; mRNA.
DR CCDS; CCDS15413.1; -.
DR RefSeq; NP_766232.1; NM_172644.4.
DR AlphaFoldDB; Q8BIP0; -.
DR SMR; Q8BIP0; -.
DR BioGRID; 230526; 7.
DR STRING; 10090.ENSMUSP00000041851; -.
DR iPTMnet; Q8BIP0; -.
DR PhosphoSitePlus; Q8BIP0; -.
DR EPD; Q8BIP0; -.
DR MaxQB; Q8BIP0; -.
DR PaxDb; Q8BIP0; -.
DR PeptideAtlas; Q8BIP0; -.
DR PRIDE; Q8BIP0; -.
DR ProteomicsDB; 257517; -.
DR Antibodypedia; 20564; 185 antibodies from 24 providers.
DR DNASU; 226539; -.
DR Ensembl; ENSMUST00000035430; ENSMUSP00000041851; ENSMUSG00000026709.
DR GeneID; 226539; -.
DR KEGG; mmu:226539; -.
DR UCSC; uc007dey.1; mouse.
DR CTD; 55157; -.
DR MGI; MGI:2442510; Dars2.
DR VEuPathDB; HostDB:ENSMUSG00000026709; -.
DR eggNOG; KOG2411; Eukaryota.
DR GeneTree; ENSGT01030000234618; -.
DR HOGENOM; CLU_014330_3_1_1; -.
DR InParanoid; Q8BIP0; -.
DR OMA; YQLDVEM; -.
DR OrthoDB; 697974at2759; -.
DR PhylomeDB; Q8BIP0; -.
DR TreeFam; TF314827; -.
DR BioGRID-ORCS; 226539; 25 hits in 77 CRISPR screens.
DR ChiTaRS; Dars2; mouse.
DR PRO; PR:Q8BIP0; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8BIP0; protein.
DR Bgee; ENSMUSG00000026709; Expressed in epiblast (generic) and 234 other tissues.
DR Genevisible; Q8BIP0; MM.
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:0004815; F:aspartate-tRNA ligase activity; ISS:UniProtKB.
DR GO; GO:0050560; F:aspartate-tRNA(Asn) ligase activity; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IBA:GO_Central.
DR GO; GO:0070145; P:mitochondrial asparaginyl-tRNA aminoacylation; ISS:UniProtKB.
DR GO; GO:0043039; P:tRNA aminoacylation; ISO:MGI.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.1360.30; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00044; Asp_tRNA_synth_type1; 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; IPR004524; Asp-tRNA-ligase_1.
DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR InterPro; IPR004115; GAD-like_sf.
DR InterPro; IPR029351; GAD_dom.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR PANTHER; PTHR22594:SF5; PTHR22594:SF5; 1.
DR Pfam; PF02938; GAD; 1.
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; SSF55261; SSF55261; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00459; aspS_bact; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Mitochondrion;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..46
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 47..653
FT /note="Aspartate--tRNA ligase, mitochondrial"
FT /id="PRO_0000250737"
FT REGION 243..246
FT /note="Aspartate"
FT /evidence="ECO:0000250"
FT BINDING 265..267
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 534
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 541
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 583..586
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 218
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q3KRD0"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PI48"
FT CONFLICT 71
FT /note="I -> V (in Ref. 2; AAH89191)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="R -> G (in Ref. 2; AAH89191)"
FT /evidence="ECO:0000305"
FT CONFLICT 540
FT /note="V -> A (in Ref. 2; AAH89191)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 653 AA; 74102 MW; 8A02D2E62E914E99 CRC64;
MYLGFWLSRL CRGLSRPIGK TMRPIWGSLS RNLALSSQRI PEFSSFVART NTCGELRSSH
LGQEVTLCGW IQYRRQNTFL VLRDCHGLVQ ILIPQDESAA SVRRILCEAP VESVVRVSGT
VISRPPGQEN PKMPTGEIEI KVKTAELLNA CKKLPFEIKD FVKKTEALRL QYRYLDLRSF
QMQYNLRLRS QMVMKMREYL CNLHGFVDIE TPTLFKRTPG GAKEFLVPSR EPGKFYSLPQ
SPQQFKQLLM VGGLDRYFQV ARCYRDEGSR PDRQPEFTQI DIEMSFVEQT GIQRLVEGLL
QYSWPGDKDP LVTPFPSMTF AEALATYGTD KPDTRFGMKI VDVSDVFRNT ELRFLQDALA
KPQGTVKAIC VHDGAKYLRK EDIEFIRKFA VHHFSQEVLP IFLNAKKNWS SPFAKFIMEE
ERLELARSME IQEEDIVLLT AGEHEKACSL LGKLRLECAD LLEMRGAVLR DPAVFSFLWV
VDFPLFLAKE ESPTELESAH HPFTAPNSSD IHLLYTEPEK VRGQHYDLVL NGNEIGGGSV
RIHDAQLQRY ILETLLKEDV KLLSHLLQAL DYGAPPHGGI ALGLDRLVCL VTGAPSIRDV
IAFPKSYRGQ DLMSNAPDSV SPEELKPYHI HVLWPADSEE ESASATPSKH LSS
