SYHM_MOUSE
ID SYHM_MOUSE Reviewed; 505 AA.
AC Q99KK9;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Histidine--tRNA ligase, mitochondrial;
DE EC=6.1.1.21 {ECO:0000250|UniProtKB:P49590};
DE AltName: Full=Histidine--tRNA ligase-like;
DE AltName: Full=Histidyl-tRNA synthetase;
DE Short=HisRS;
DE Flags: Precursor;
GN Name=Hars2; Synonyms=Harsl;
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=FVB/N; TISSUE=Mammary tumor;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, 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: Mitochondrial aminoacyl-tRNA synthetase that catalyzes the
CC ATP-dependent ligation of histidine to the 3'-end of its cognate tRNA,
CC via the formation of an aminoacyl-adenylate intermediate (His-AMP).
CC {ECO:0000250|UniProtKB:P49590}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-
CC histidyl-tRNA(His); Xref=Rhea:RHEA:17313, Rhea:RHEA-COMP:9665,
CC Rhea:RHEA-COMP:9689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57595, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78527, ChEBI:CHEBI:456215; EC=6.1.1.21;
CC Evidence={ECO:0000250|UniProtKB:P49590};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P49590}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P49590}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; BC004596; AAH04596.1; -; mRNA.
DR CCDS; CCDS29165.1; -.
DR RefSeq; NP_542367.1; NM_080636.2.
DR AlphaFoldDB; Q99KK9; -.
DR SMR; Q99KK9; -.
DR BioGRID; 214256; 11.
DR STRING; 10090.ENSMUSP00000117231; -.
DR iPTMnet; Q99KK9; -.
DR PhosphoSitePlus; Q99KK9; -.
DR EPD; Q99KK9; -.
DR jPOST; Q99KK9; -.
DR MaxQB; Q99KK9; -.
DR PaxDb; Q99KK9; -.
DR PeptideAtlas; Q99KK9; -.
DR PRIDE; Q99KK9; -.
DR ProteomicsDB; 254734; -.
DR Antibodypedia; 27080; 218 antibodies from 23 providers.
DR DNASU; 70791; -.
DR Ensembl; ENSMUST00000152954; ENSMUSP00000117231; ENSMUSG00000019143.
DR GeneID; 70791; -.
DR KEGG; mmu:70791; -.
DR UCSC; uc008eor.2; mouse.
DR CTD; 23438; -.
DR MGI; MGI:1918041; Hars2.
DR VEuPathDB; HostDB:ENSMUSG00000019143; -.
DR eggNOG; KOG1936; Eukaryota.
DR GeneTree; ENSGT00390000005922; -.
DR HOGENOM; CLU_025113_4_2_1; -.
DR InParanoid; Q99KK9; -.
DR OMA; YQIQKVW; -.
DR OrthoDB; 1065556at2759; -.
DR PhylomeDB; Q99KK9; -.
DR TreeFam; TF300652; -.
DR BioGRID-ORCS; 70791; 21 hits in 59 CRISPR screens.
DR ChiTaRS; Hars2; mouse.
DR PRO; PR:Q99KK9; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q99KK9; protein.
DR Bgee; ENSMUSG00000019143; Expressed in retinal neural layer and 258 other tissues.
DR ExpressionAtlas; Q99KK9; baseline and differential.
DR Genevisible; Q99KK9; MM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004821; F:histidine-tRNA ligase activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0006427; P:histidyl-tRNA aminoacylation; ISO:MGI.
DR CDD; cd00773; HisRS-like_core; 1.
DR CDD; cd00859; HisRS_anticodon; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 1.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004154; Anticodon-bd.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR015807; His-tRNA-ligase.
DR InterPro; IPR041715; HisRS-like_core.
DR InterPro; IPR004516; HisRS/HisZ.
DR InterPro; IPR033656; HisRS_anticodon.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF13393; tRNA-synt_His; 1.
DR PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00442; hisS; 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; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..31
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 32..505
FT /note="Histidine--tRNA ligase, mitochondrial"
FT /id="PRO_0000254584"
FT BINDING 130..132
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000250|UniProtKB:P12081"
FT BINDING 157
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000250|UniProtKB:P12081"
FT BINDING 173
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000250|UniProtKB:P12081"
FT BINDING 177
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000250|UniProtKB:P12081"
FT BINDING 326
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000250|UniProtKB:P12081"
FT BINDING 330..331
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000250|UniProtKB:P12081"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 443
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P49590"
SQ SEQUENCE 505 AA; 56985 MW; 1865426DF408DA1E CRC64;
MPHLGPLRRR AWAALLGQLL RPPSTVCTRG CHSQVAKAVL TSEQLKSHQE KPNFVIKVPK
GTRDLSPQQM VVREKILDKI ISCFKRHGAK GLDTPAFELK EMLTEKYEDN FGLMYDLKDQ
GGELLSLRYD LTVPFARYLA MNKLKKMKRY QVGKVWRRES PAIAQGRYRE FCQCDFDIAG
EFDPMIPDAE CLRIMCEILS GLQLGDFLIK VNDRRVVDGI FAVCGVPESK LRTICSSMDK
LDKMSWEGVR HEMVAKKGLA PEVADRIGDF VQYHGGISLV EDLFKDPRLS QSQLALQGLG
DLKLLFEYLR LFGIADKISL DLSLARGLDY YTGVIYEAVL LESPAQAGKE TLSVGSVAAG
GRYDNLVAQF DPKGHHVPCV GLSIGVERIF YLVEQKMKMS GEKVRTTETQ VFVATPQKNF
LQERLKIIAE LWDAGIKAEM LYKNNPKLLT QLHYCEKADI PLMVIIGEQE RNEGVIKLRS
VASREEVTIN RESLVAEIQK RLSES
