SYIM_MOUSE
ID SYIM_MOUSE Reviewed; 1012 AA.
AC Q8BIJ6; Q3TKT8; Q8BIJ0; Q8BIP3;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Isoleucine--tRNA ligase, mitochondrial;
DE EC=6.1.1.5;
DE AltName: Full=Isoleucyl-tRNA synthetase;
DE Short=IleRS;
DE Flags: Precursor;
GN Name=Iars2;
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=Cerebellum, Head, and Liver;
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;
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, 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 SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-56; LYS-74; LYS-194; LYS-241;
RP LYS-479; LYS-500; LYS-775 AND LYS-781, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast, and Liver;
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).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-74; LYS-725 AND LYS-775, AND
RP IDENTIFICATION BY MASS 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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-
CC isoleucyl-tRNA(Ile); Xref=Rhea:RHEA:11060, Rhea:RHEA-COMP:9666,
CC Rhea:RHEA-COMP:9695, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58045, ChEBI:CHEBI:78442, ChEBI:CHEBI:78528,
CC ChEBI:CHEBI:456215; EC=6.1.1.5;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AK166832; BAE39055.1; -; mRNA.
DR EMBL; AK036182; BAC29337.1; -; mRNA.
DR EMBL; AK048653; BAC33410.1; -; mRNA.
DR EMBL; AK050358; BAC34208.1; -; mRNA.
DR EMBL; BC052403; AAH52403.1; -; mRNA.
DR CCDS; CCDS15596.1; -.
DR RefSeq; NP_941055.1; NM_198653.2.
DR AlphaFoldDB; Q8BIJ6; -.
DR SMR; Q8BIJ6; -.
DR BioGRID; 237874; 11.
DR STRING; 10090.ENSMUSP00000027921; -.
DR iPTMnet; Q8BIJ6; -.
DR PhosphoSitePlus; Q8BIJ6; -.
DR SwissPalm; Q8BIJ6; -.
DR EPD; Q8BIJ6; -.
DR jPOST; Q8BIJ6; -.
DR MaxQB; Q8BIJ6; -.
DR PaxDb; Q8BIJ6; -.
DR PeptideAtlas; Q8BIJ6; -.
DR PRIDE; Q8BIJ6; -.
DR ProteomicsDB; 253437; -.
DR Antibodypedia; 20735; 155 antibodies from 29 providers.
DR DNASU; 381314; -.
DR Ensembl; ENSMUST00000027921; ENSMUSP00000027921; ENSMUSG00000026618.
DR GeneID; 381314; -.
DR KEGG; mmu:381314; -.
DR UCSC; uc007dyz.1; mouse.
DR CTD; 55699; -.
DR MGI; MGI:1919586; Iars2.
DR VEuPathDB; HostDB:ENSMUSG00000026618; -.
DR eggNOG; KOG0433; Eukaryota.
DR GeneTree; ENSGT00550000074910; -.
DR HOGENOM; CLU_001493_7_2_1; -.
DR InParanoid; Q8BIJ6; -.
DR OMA; HLGTAWN; -.
DR OrthoDB; 59501at2759; -.
DR PhylomeDB; Q8BIJ6; -.
DR TreeFam; TF300518; -.
DR BioGRID-ORCS; 381314; 31 hits in 75 CRISPR screens.
DR ChiTaRS; Iars2; mouse.
DR PRO; PR:Q8BIJ6; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8BIJ6; protein.
DR Bgee; ENSMUSG00000026618; Expressed in migratory enteric neural crest cell and 267 other tissues.
DR ExpressionAtlas; Q8BIJ6; baseline and differential.
DR Genevisible; Q8BIJ6; MM.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004822; F:isoleucine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IBA:GO_Central.
DR GO; GO:0032543; P:mitochondrial translation; IBA:GO_Central.
DR CDD; cd07960; Anticodon_Ia_Ile_BEm; 1.
DR Gene3D; 3.40.50.620; -; 2.
DR Gene3D; 3.90.740.10; -; 1.
DR HAMAP; MF_02002; Ile_tRNA_synth_type1; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR033708; Anticodon_Ile_BEm.
DR InterPro; IPR002301; Ile-tRNA-ligase.
DR InterPro; IPR023585; Ile-tRNA-ligase_type1.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR PRINTS; PR00984; TRNASYNTHILE.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00392; ileS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 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..48
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 49..1012
FT /note="Isoleucine--tRNA ligase, mitochondrial"
FT /id="PRO_0000233337"
FT MOTIF 116..126
FT /note="'HIGH' region"
FT /evidence="ECO:0000250"
FT MOTIF 664..668
FT /note="'KMSKS' region"
FT /evidence="ECO:0000250"
FT BINDING 667
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 56
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 74
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 74
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 194
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 233
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9NSE4"
FT MOD_RES 241
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9NSE4"
FT MOD_RES 241
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 479
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 500
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 725
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 775
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 775
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 781
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9NSE4"
FT MOD_RES 781
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 68
FT /note="Q -> K (in Ref. 1; BAC29337)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="E -> G (in Ref. 1; BAE39055)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="N -> K (in Ref. 1; BAC29337)"
FT /evidence="ECO:0000305"
FT CONFLICT 709
FT /note="V -> M (in Ref. 1; BAC34208)"
FT /evidence="ECO:0000305"
FT CONFLICT 819
FT /note="C -> Y (in Ref. 1; BAE39055)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1012 AA; 112804 MW; A4663D3A1BC3D678 CRC64;
MHWGLCPRGP GAAAVAAAGS FWGPARLPSR LGCLGMTRRL VVRSVAGADS PQSSSKGGRY
RDTVLLPQTS FPMKLLGRQQ SDMELEIQQK CGFSELYSWQ RERKVKTEFC LHDGPPYANG
DPHVGHALNK ILKDIANRFH MMRGSKVHFV PGWDCHGLPI ETKVLSELGV DAQSLSAMEI
REKARSFAQA AIEKQKSAFV RWGVMADWNN CYYTFDPKYE AKQLRVFYQM YEKGLVYRSY
KPVYWSPSSR TALAEAELEY NPEHVSRSIY VRFPLLRPPP KLESLTDASS PVSVLVWTTQ
PWTIPANQAI CYMPEAKYAV VKCSASGHLY ILAEDKIAPV ASALETTFDV VAAFSGVDLE
GGTCSHPLTP DKVSPLLPAT HVTMAKGTGL VHTAPAHGME DYSVASQHSL PMDCLVDEGG
MFTDAAGPEL QNKAVLKEGT DVVIKMLQAT KNVLKEENIV HSYPCDWRTK TPVLIRASKQ
WFVNITDIKA AAKESLKTVK FIPGAALNSM TDMLDRRPYW CISRQRVWGV PIPVFHHKTK
DEYLINSQTT EHIIKLVEQH GSDVWWTLPA EQLLPAEVLA QAGGPGALEY APGQDILDIW
FDSGTSWSCV LQDTQQRADL YLEGKDQLGG WFQSSLLTSV ATRSKAPFRT VMVHGFTLGE
KGEKMSKSLG NVINPDTIIS GGKDHSKEPP YGADILRWWI AESNVFTEVT IGPSVLSAAR
DDISKLRNTL RFLLGNLTGF NPETDSVPVK NMYVIDQYML HLIQDFATKI TDSYKQYDFG
KVVRLLKAFY TRELSSFYFS IVKDRLYCEN EKDPKRRSCQ TALAEILDVL VRAFAPILPH
LAEEVFQHIP YVTEPKSVFR TGWINTSSIW KKPGLEEAVE SACAMRDSFL GSIPGKNAAE
YEVIIVIEPG LLFEIMEMLQ AEETSSTSQL NELMMASQTT LLAQEPRERT AGDIELTGTF
VINLEGGDIR EESSYKVIVV PTAREKCPRC WKHTSETADA LCPRCAEVIG AK
