SYAM_MOUSE
ID SYAM_MOUSE Reviewed; 980 AA.
AC Q14CH7; Q68FH3; Q69ZM9;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Alanine--tRNA ligase, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03133};
DE EC=6.1.1.7 {ECO:0000255|HAMAP-Rule:MF_03133};
DE AltName: Full=Alanyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_03133};
DE Short=AlaRS {ECO:0000255|HAMAP-Rule:MF_03133};
DE Flags: Precursor;
GN Name=Aars2; Synonyms=Aarsl, Gm89, Kiaa1270;
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=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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 242-980.
RC TISSUE=Embryonic intestine;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Spleen, and
RC 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 attachment of alanine to tRNA(Ala) in a two-
CC step reaction: alanine is first activated by ATP to form Ala-AMP and
CC then transferred to the acceptor end of tRNA(Ala). Also edits
CC incorrectly charged tRNA(Ala) via its editing domain.
CC {ECO:0000255|HAMAP-Rule:MF_03133}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-
CC tRNA(Ala); Xref=Rhea:RHEA:12540, Rhea:RHEA-COMP:9657, Rhea:RHEA-
CC COMP:9923, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57972,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78497, ChEBI:CHEBI:456215; EC=6.1.1.7;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03133};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03133};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03133};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03133}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- DOMAIN: Consists of three domains; the N-terminal catalytic domain, the
CC editing domain and the C-terminal C-Ala domain. The editing domain
CC removes incorrectly charged amino acids, while the C-Ala domain, along
CC with tRNA(Ala), serves as a bridge to cooperatively bring together the
CC editing and aminoacylation centers thus stimulating deacylation of
CC misacylated tRNAs. {ECO:0000255|HAMAP-Rule:MF_03133}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_03133}.
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DR EMBL; BC079844; AAH79844.1; -; mRNA.
DR EMBL; BC113172; AAI13173.1; -; mRNA.
DR EMBL; BC113779; AAI13780.1; -; mRNA.
DR EMBL; AK173139; BAD32417.1; -; Transcribed_RNA.
DR CCDS; CCDS28809.1; -.
DR RefSeq; NP_941010.2; NM_198608.2.
DR AlphaFoldDB; Q14CH7; -.
DR SMR; Q14CH7; -.
DR BioGRID; 230321; 8.
DR IntAct; Q14CH7; 1.
DR MINT; Q14CH7; -.
DR STRING; 10090.ENSMUSP00000024733; -.
DR iPTMnet; Q14CH7; -.
DR PhosphoSitePlus; Q14CH7; -.
DR EPD; Q14CH7; -.
DR MaxQB; Q14CH7; -.
DR PaxDb; Q14CH7; -.
DR PeptideAtlas; Q14CH7; -.
DR PRIDE; Q14CH7; -.
DR ProteomicsDB; 254615; -.
DR Antibodypedia; 46060; 137 antibodies from 28 providers.
DR DNASU; 224805; -.
DR Ensembl; ENSMUST00000024733; ENSMUSP00000024733; ENSMUSG00000023938.
DR GeneID; 224805; -.
DR KEGG; mmu:224805; -.
DR UCSC; uc008cqr.1; mouse.
DR CTD; 57505; -.
DR MGI; MGI:2681839; Aars2.
DR VEuPathDB; HostDB:ENSMUSG00000023938; -.
DR eggNOG; KOG0188; Eukaryota.
DR GeneTree; ENSGT00940000158246; -.
DR HOGENOM; CLU_004485_5_0_1; -.
DR InParanoid; Q14CH7; -.
DR OMA; DTEACCG; -.
DR OrthoDB; 129373at2759; -.
DR PhylomeDB; Q14CH7; -.
DR TreeFam; TF300737; -.
DR BioGRID-ORCS; 224805; 25 hits in 74 CRISPR screens.
DR ChiTaRS; Aars2; mouse.
DR PRO; PR:Q14CH7; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q14CH7; protein.
DR Bgee; ENSMUSG00000023938; Expressed in otolith organ and 198 other tissues.
DR Genevisible; Q14CH7; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0004813; F:alanine-tRNA ligase activity; ISO:MGI.
DR GO; GO:0016597; F:amino acid binding; IBA:GO_Central.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006419; P:alanyl-tRNA aminoacylation; IBA:GO_Central.
DR GO; GO:0070143; P:mitochondrial alanyl-tRNA aminoacylation; ISO:MGI.
DR GO; GO:0006400; P:tRNA modification; IBA:GO_Central.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00036_B; Ala_tRNA_synth_B; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR002318; Ala-tRNA-lgiase_IIc.
DR InterPro; IPR018162; Ala-tRNA-ligase_IIc_anticod-bd.
DR InterPro; IPR018165; Ala-tRNA-synth_IIc_core.
DR InterPro; IPR018164; Ala-tRNA-synth_IIc_N.
DR InterPro; IPR023033; Ala_tRNA_ligase_euk/bac.
DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR012947; tRNA_SAD.
DR Pfam; PF01411; tRNA-synt_2c; 1.
DR Pfam; PF07973; tRNA_SAD; 1.
DR PRINTS; PR00980; TRNASYNTHALA.
DR SMART; SM00863; tRNA_SAD; 1.
DR SUPFAM; SSF101353; SSF101353; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF55186; SSF55186; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00344; alaS; 1.
DR PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Metal-binding;
KW Mitochondrion; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome; RNA-binding; Transit peptide; tRNA-binding; Zinc.
FT TRANSIT 1..23
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT CHAIN 24..980
FT /note="Alanine--tRNA ligase, mitochondrial"
FT /id="PRO_0000250726"
FT BINDING 105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT BINDING 123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT BINDING 205
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT BINDING 235..237
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT BINDING 237
FT /ligand="L-alanine"
FT /ligand_id="ChEBI:CHEBI:57972"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT BINDING 260
FT /ligand="L-alanine"
FT /ligand_id="ChEBI:CHEBI:57972"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT BINDING 264
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT BINDING 627
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT BINDING 631
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT BINDING 744
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT BINDING 748
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT CONFLICT 618..625
FT /note="AWRMGCMV -> RSRPG (in Ref. 2; BAD32417)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 980 AA; 106783 MW; 7734BC58CDB5463D CRC64;
MAVALAAAAG KLRRAIGRSC PWQPFSTEPG PPHGAAVRDA FLSFFRDRHG HRLVPSATVR
PRGDPSLLFV NAGMNQFKPI FLGTVDPRSE MAGFRRVVNS QKCVRAGGRH NDLEDVGRDL
SHHTFFEMLG NWAFGGEYFK EEACSMAWEL LTQVYGIPED RLWVSYFSGD SQTGLDPDLE
TRDIWLSLGV PASRVLSFGP QENFWEMGDT GPCGPCTEIH YDLAGGVGSP QLVELWNLVF
MQHYREADGS LQLLPQRHVD TGMGLERLVA VLQGKRSTYD TDLFSPLLDA IHQSCGAPPY
SGRVGAADEG RIDTAYRVVA DHIRTLSVCI ADGVSPGMSG APLVLRRILR RAVRYSTEVL
QAPPGFLGSL VPVVVETLGS AYPELEKNSV KIASLVSEDE AAFLASLQRG RRIIDRTVKR
LGPSDLFPAE VAWSLSLSGN LGIPLDLVEL MLEEKGVKLD TAGLEQLAQK EAQHRAQQAE
ADQEDRLCLD VHALEELHRQ GIPTTDDSPK YNYTLHPNGD YEFGLCEARV LQLYSETGTA
VASVGAGQRC GLLLDRTNFY AEQGGQASDR GYLVRTGQQD MLFPVAGAQL CGGFILHEAM
APERLQVGDQ VQLYVDKAWR MGCMVKHTAT HLLSWALRQT LGPTTEQRGS HLNPERLRFD
VATQTLLTTE QLRTVESYVQ EVVGQDKPVF MEEVPLAHTA RIPGLRSLDE VYPDPVRVVS
VGVPVAHALG PASQAAMHTS VELCCGTHLL STGAVGDLVI IGERQLVKGI TRLLAITGEQ
AQQAREVGQS LSQEVEAASE RLSQGSRDLP EAHRLSKDIG RLTEVAESAV IPQWQRQELQ
TTLKMLQRRA NTAIRKLEKG QATEKSQELL KRHSEGPLIV DTVSAESLSV LVKVVRQLCK
QAPSISVLLL SPQPTGSVLC ACQVAQDATP TFTAEAWALA VCSHMGGKAW GSRVVAQGTG
HTADLEAALG TARAYALSQL
