SYIC_MOUSE
ID SYIC_MOUSE Reviewed; 1262 AA.
AC Q8BU30; Q6NXK4;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Isoleucine--tRNA ligase, cytoplasmic;
DE EC=6.1.1.5 {ECO:0000269|PubMed:12060739};
DE AltName: Full=Isoleucyl-tRNA synthetase;
DE Short=IRS;
DE Short=IleRS;
GN Name=Iars1; Synonyms=Iars;
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 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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP SUBUNIT, CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=12060739; DOI=10.1073/pnas.122110199;
RA Kim J.Y., Kang Y.-S., Lee J.-W., Kim H.J., Ahn Y.H., Park H., Ko Y.-G.,
RA Kim S.;
RT "p38 is essential for the assembly and stability of macromolecular tRNA
RT synthetase complex: implications for its physiological significance.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:7912-7916(2002).
RN [5]
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).
CC -!- FUNCTION: Catalyzes the specific attachment of an amino acid to its
CC cognate tRNA in a 2 step reaction: the amino acid (AA) is first
CC activated by ATP to form AA-AMP and then transferred to the acceptor
CC end of the tRNA. {ECO:0000269|PubMed:12060739}.
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 Evidence={ECO:0000269|PubMed:12060739};
CC -!- SUBUNIT: Part of a multisubunit complex that groups tRNA ligases for
CC Arg (RARS1), Asp (DARS1), Gln (QARS1), Ile (IARS1), Leu (LARS1), Lys
CC (KARS1), Met (MARS1) the bifunctional ligase for Glu and Pro (EPRS1)
CC and the auxiliary subunits AIMP1/p43, AIMP2/p38 and EEF1E1/p18.
CC {ECO:0000269|PubMed:12060739}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P41252}.
CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:P41252}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AK087992; BAC40081.1; -; mRNA.
DR EMBL; AK133856; BAE21890.1; -; mRNA.
DR EMBL; CH466546; EDL41088.1; -; Genomic_DNA.
DR EMBL; BC067029; AAH67029.1; -; mRNA.
DR CCDS; CCDS36659.1; -.
DR RefSeq; NP_742012.2; NM_172015.3.
DR RefSeq; XP_006516889.1; XM_006516826.2.
DR AlphaFoldDB; Q8BU30; -.
DR SMR; Q8BU30; -.
DR BioGRID; 222774; 9.
DR IntAct; Q8BU30; 2.
DR MINT; Q8BU30; -.
DR STRING; 10090.ENSMUSP00000132082; -.
DR iPTMnet; Q8BU30; -.
DR PhosphoSitePlus; Q8BU30; -.
DR SwissPalm; Q8BU30; -.
DR EPD; Q8BU30; -.
DR jPOST; Q8BU30; -.
DR MaxQB; Q8BU30; -.
DR PaxDb; Q8BU30; -.
DR PeptideAtlas; Q8BU30; -.
DR PRIDE; Q8BU30; -.
DR ProteomicsDB; 253436; -.
DR Antibodypedia; 28131; 137 antibodies from 21 providers.
DR DNASU; 105148; -.
DR Ensembl; ENSMUST00000047363; ENSMUSP00000048096; ENSMUSG00000037851.
DR Ensembl; ENSMUST00000164260; ENSMUSP00000126806; ENSMUSG00000037851.
DR Ensembl; ENSMUST00000165316; ENSMUSP00000132082; ENSMUSG00000037851.
DR GeneID; 105148; -.
DR KEGG; mmu:105148; -.
DR UCSC; uc007qjv.2; mouse.
DR CTD; 105148; -.
DR MGI; MGI:2145219; Iars.
DR VEuPathDB; HostDB:ENSMUSG00000037851; -.
DR eggNOG; KOG0434; Eukaryota.
DR GeneTree; ENSGT00550000074921; -.
DR HOGENOM; CLU_001493_1_1_1; -.
DR InParanoid; Q8BU30; -.
DR OMA; KMMAPFT; -.
DR OrthoDB; 59501at2759; -.
DR PhylomeDB; Q8BU30; -.
DR BioGRID-ORCS; 105148; 26 hits in 75 CRISPR screens.
DR ChiTaRS; Iars; mouse.
DR PRO; PR:Q8BU30; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8BU30; protein.
DR Bgee; ENSMUSG00000037851; Expressed in primary oocyte and 281 other tissues.
DR ExpressionAtlas; Q8BU30; baseline and differential.
DR Genevisible; Q8BU30; MM.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IDA:CAFA.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO: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:0051020; F:GTPase binding; ISO:MGI.
DR GO; GO:0004822; F:isoleucine-tRNA ligase activity; IMP:CAFA.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IDA:CAFA.
DR CDD; cd07961; Anticodon_Ia_Ile_ABEc; 1.
DR Gene3D; 3.40.50.620; -; 2.
DR HAMAP; MF_02003; Ile_tRNA_synth_type2; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR033709; Anticodon_Ile_ABEc.
DR InterPro; IPR002301; Ile-tRNA-ligase.
DR InterPro; IPR023586; Ile-tRNA-ligase_type2.
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 PANTHER; PTHR42780; PTHR42780; 1.
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; Cytoplasm; Ligase;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..1262
FT /note="Isoleucine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000098598"
FT MOTIF 48..58
FT /note="'HIGH' region"
FT MOTIF 600..604
FT /note="'KMSKS' region"
FT BINDING 603
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P41252"
FT MOD_RES 1049
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41252"
FT MOD_RES 1058
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P41252"
FT CONFLICT 1033
FT /note="I -> V (in Ref. 1; BAC40081)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1262 AA; 144271 MW; 2039614F557E1312 CRC64;
MVQQVPENIS FPAEEEKILE FWSKHNCFQE CLKQSKLRPK FTFYDGPPFA TGLPHYGHIL
AGTIKDIVTR YAHQSGFHVD RRFGWDCHGL PVEYEIDKTL GIKGPEDVAK MGIAEYNKQC
RAIVMRYSAE WKSTVTRLGR WIDFDNDYKT LYPQFMESVW WVFKQLYDKG LVYRGVKVMP
FSTACGTPLS NFESNQNYKD VQDPSVFVTF PLEEDENTSL VAWTTTPWTL PSNLALCVNP
EIQYVKIKDV ARGKLFILTE ARLSALYKQE SDYEILERFP GASLKGKKYK PLFDYFIKCK
ENGAFTVLVD HYVKDEEGTG VVHQAPYFGA DDHRVCMDFN IIQKDSVPVC PVDASGCFTE
EVTHFVGQYV KDADKNIIRM LKEQGRLLAA GTFTHSYPFC WRSDTPLIYK SVPSWFVRVE
PMVDQLLKNN DLCYWVPEFV REKRFGNWLK EARDWAISRN RYWGTPIPLW VSEDLEEVVC
IGSVAELEEL SGTKISDLHR ESIDHLTIPS RCGKAPLRRV SEVFDCWFES GSMPYAQVHY
PFESKREFED AFPADFIAEG IDQTRGWFYT LLVLATALFG QPPFKNVIVN GLILASDGQK
MSKRKKNYPD PVSIIDKYGA DALRLYLINS PVVRAENLRF KEEGVRDVLK DVLLPWYNAY
RFFIQNVFRL HKEEEVKFLY NEHTVRESPN ITDRWVLSFM QSLLGFFETE MAAYRLYTVV
PRLVKFVDIL TNWYVRMNRR RLKGESGVED CVMALETLFS VLLSLCRLMA PYTPFLTELM
YQNLKLLIDP ASLRDKDTLS IHYLMLPRVR EELIDKKTEN AVSRMQSVIE LGRVIRDRKT
IPIKYPLKEI VVIHQDPEAL EDIRSLEKYI IEELNVRKVT LSTDKNKYGI RLRAEPDHMV
LGKRLKGAFK AVMMAIKRLS NEELERFQKS GSIVVEGHEL HEEDIRLMYT FDQATGGTAQ
FEAHSDAQAL VLLDVTPDQS MVDEGMAREV INRIQKLRKK CNLVPTDEIT VYYNAKSEGR
YLNNVIESHT DFIFATIKAP LKPYPVPTSD NILIQEQTQL KGSELEITLT KGSCVPGPAC
AYVNLNICAN GTEQGGVLLL ENPKGDNQLN LVKLKTVVTS VFGVKNAKLS VFHGETEIQN
QTDLLSLSGR TLCVTAGASP SPISSPSTLL CQYLNLQLLN AEPQECLTGT VGTLLLENPL
GQNGLTHQGL VHEAAKVFGL RSRRLRLFLN ETQTQEITED IPMKTLNMKT VYVSVLPTTA
DG
