SYFM_MOUSE
ID SYFM_MOUSE Reviewed; 451 AA.
AC Q99M01; Q3TBZ7; Q9CYY0;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Phenylalanine--tRNA ligase, mitochondrial;
DE EC=6.1.1.20 {ECO:0000250|UniProtKB:O95363};
DE AltName: Full=Phenylalanyl-tRNA synthetase;
DE Short=PheRS;
DE Flags: Precursor;
GN Name=Fars2; Synonyms=Fars1;
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;
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=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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, and Lung;
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: Is responsible for the charging of tRNA(Phe) with
CC phenylalanine in mitochondrial translation. To a lesser extent, also
CC catalyzes direct attachment of m-Tyr (an oxidized version of Phe) to
CC tRNA(Phe), thereby opening the way for delivery of the misacylated tRNA
CC to the ribosome and incorporation of ROS-damaged amino acid into
CC proteins (By similarity). {ECO:0000250|UniProtKB:O95363}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) +
CC L-phenylalanyl-tRNA(Phe); Xref=Rhea:RHEA:19413, Rhea:RHEA-COMP:9668,
CC Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58095, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78531, ChEBI:CHEBI:456215; EC=6.1.1.20;
CC Evidence={ECO:0000250|UniProtKB:O95363};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000305}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q6AYQ3}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AK013211; BAB28715.1; -; mRNA.
DR EMBL; AK170986; BAE42160.1; -; mRNA.
DR EMBL; BC002147; AAH02147.1; -; mRNA.
DR CCDS; CCDS26453.1; -.
DR RefSeq; NP_077236.1; NM_024274.3.
DR RefSeq; XP_006516832.1; XM_006516769.3.
DR RefSeq; XP_011242647.1; XM_011244345.2.
DR AlphaFoldDB; Q99M01; -.
DR SMR; Q99M01; -.
DR BioGRID; 213774; 3.
DR STRING; 10090.ENSMUSP00000021857; -.
DR PhosphoSitePlus; Q99M01; -.
DR EPD; Q99M01; -.
DR jPOST; Q99M01; -.
DR MaxQB; Q99M01; -.
DR PaxDb; Q99M01; -.
DR PeptideAtlas; Q99M01; -.
DR PRIDE; Q99M01; -.
DR ProteomicsDB; 254705; -.
DR Antibodypedia; 2800; 126 antibodies from 24 providers.
DR DNASU; 69955; -.
DR Ensembl; ENSMUST00000021857; ENSMUSP00000021857; ENSMUSG00000021420.
DR Ensembl; ENSMUST00000224241; ENSMUSP00000153628; ENSMUSG00000021420.
DR Ensembl; ENSMUST00000224611; ENSMUSP00000153658; ENSMUSG00000021420.
DR GeneID; 69955; -.
DR KEGG; mmu:69955; -.
DR UCSC; uc007qck.2; mouse.
DR CTD; 10667; -.
DR MGI; MGI:1917205; Fars2.
DR VEuPathDB; HostDB:ENSMUSG00000021420; -.
DR eggNOG; KOG2783; Eukaryota.
DR GeneTree; ENSGT00940000158071; -.
DR HOGENOM; CLU_022696_1_0_1; -.
DR InParanoid; Q99M01; -.
DR OMA; SKSDTYY; -.
DR OrthoDB; 1115196at2759; -.
DR PhylomeDB; Q99M01; -.
DR TreeFam; TF105798; -.
DR BioGRID-ORCS; 69955; 29 hits in 73 CRISPR screens.
DR ChiTaRS; Fars2; mouse.
DR PRO; PR:Q99M01; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q99M01; protein.
DR Bgee; ENSMUSG00000021420; Expressed in dentate gyrus of hippocampal formation granule cell and 270 other tissues.
DR ExpressionAtlas; Q99M01; baseline and differential.
DR Genevisible; Q99M01; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; ISS:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; ISS:UniProtKB.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; ISS:UniProtKB.
DR GO; GO:0008033; P:tRNA processing; ISS:UniProtKB.
DR Gene3D; 3.30.70.380; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR005121; Fdx_antiC-bd.
DR InterPro; IPR036690; Fdx_antiC-bd_sf.
DR InterPro; IPR004530; Phe-tRNA-synth_IIc_mito.
DR InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR PANTHER; PTHR11538:SF41; PTHR11538:SF41; 1.
DR Pfam; PF03147; FDX-ACB; 1.
DR Pfam; PF01409; tRNA-synt_2d; 2.
DR SMART; SM00896; FDX-ACB; 1.
DR SUPFAM; SSF54991; SSF54991; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00469; pheS_mito; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS51447; FDX_ACB; 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..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..451
FT /note="Phenylalanine--tRNA ligase, mitochondrial"
FT /id="PRO_0000035814"
FT DOMAIN 358..450
FT /note="FDX-ACB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00778"
FT BINDING 157..160
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 186..188
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 193..195
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 287
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 312
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 202
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O95363"
FT CONFLICT 253
FT /note="H -> N (in Ref. 1; BAB28715)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="E -> G (in Ref. 1; BAB28715)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="E -> K (in Ref. 1; BAB28715)"
FT /evidence="ECO:0000305"
FT CONFLICT 413
FT /note="C -> L (in Ref. 1; BAB28715)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 451 AA; 52337 MW; 79F3C58E77BC4AF5 CRC64;
MVCLALVRAA YEHIYLVRKV SHACRCHQHR AWSSKPAASQ SAVQGAPGSV LEILGKSYPQ
DDHTNLTQKV LSKVGRNLHN QKFHPLWLIK ERVKEHFYQQ YMVRSRTPLF SVYDQLPPVV
TTWQNFDSLL IPADHPSRKK GDNYYLNRAH MLRAHTSAHQ WDLLHAGLNA FLVVGDVYRR
DQIDCQHYPV FHQLEGVRLF SKHELFAGVK DGESLQLFEE GSRSAHKQET HTMEAVKLVE
FDLKQVLTRL VTHLFGDGLE VRWVDCYFPF THPSFEMEIN FRGEWLEVLG CGVMEQQLVN
SAGAQDRIGW AFGLGLERLA MVLYDIPDIR LFWSEDERFL KQFLLSDINQ SVKFQPLSKY
PAVFNDISFW LPSENYTEND FYDIVRTVGG DLVEKVDLID KFEHPKTHRT SHCYRITYRH
MERTLSQREV GNVHQAVQEA AVQLLGVEGR F
