ID   SYFA_MOUSE              Reviewed;         508 AA.
AC   Q8C0C7; Q3U3Q9; Q91WR4; Q922S1;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   24-JAN-2024, entry version 153.
DE   RecName: Full=Phenylalanine--tRNA ligase alpha subunit;
DE            EC=6.1.1.20 {ECO:0000250|UniProtKB:Q9Y285};
DE   AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit;
DE            Short=PheRS;
GN   Name=Farsa; Synonyms=Farsla;
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=Testis;
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=Kidney, and 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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, 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   -!- 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:Q9Y285};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:A5K9S0};
CC   -!- SUBUNIT: Heterotetramer; dimer of two heterodimers formed by FARSA and
CC       FARSB. {ECO:0000250|UniProtKB:Q9Y285}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q505J8}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Phe-tRNA synthetase alpha subunit type 2 subfamily. {ECO:0000305}.
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DR   EMBL; AK031697; BAC27519.1; -; mRNA.
DR   EMBL; AK154629; BAE32726.1; -; mRNA.
DR   EMBL; BC006862; AAH06862.1; -; mRNA.
DR   EMBL; BC013533; AAH13533.1; -; mRNA.
DR   CCDS; CCDS22480.2; -.
DR   RefSeq; NP_079924.2; NM_025648.3.
DR   AlphaFoldDB; Q8C0C7; -.
DR   SMR; Q8C0C7; -.
DR   BioGRID; 211576; 11.
DR   IntAct; Q8C0C7; 4.
DR   STRING; 10090.ENSMUSP00000003906; -.
DR   GlyGen; Q8C0C7; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8C0C7; -.
DR   PhosphoSitePlus; Q8C0C7; -.
DR   SwissPalm; Q8C0C7; -.
DR   EPD; Q8C0C7; -.
DR   jPOST; Q8C0C7; -.
DR   MaxQB; Q8C0C7; -.
DR   PaxDb; 10090-ENSMUSP00000003906; -.
DR   PeptideAtlas; Q8C0C7; -.
DR   ProteomicsDB; 258789; -.
DR   Pumba; Q8C0C7; -.
DR   Antibodypedia; 1072; 158 antibodies from 25 providers.
DR   DNASU; 66590; -.
DR   Ensembl; ENSMUST00000003906.13; ENSMUSP00000003906.7; ENSMUSG00000003808.19.
DR   GeneID; 66590; -.
DR   KEGG; mmu:66590; -.
DR   UCSC; uc009mnt.2; mouse.
DR   AGR; MGI:1913840; -.
DR   CTD; 2193; -.
DR   MGI; MGI:1913840; Farsa.
DR   VEuPathDB; HostDB:ENSMUSG00000003808; -.
DR   eggNOG; KOG2784; Eukaryota.
DR   GeneTree; ENSGT00390000006387; -.
DR   InParanoid; Q8C0C7; -.
DR   OMA; QIEGWVM; -.
DR   OrthoDB; 4619at2759; -.
DR   PhylomeDB; Q8C0C7; -.
DR   TreeFam; TF300647; -.
DR   BioGRID-ORCS; 66590; 23 hits in 79 CRISPR screens.
DR   ChiTaRS; Farsa; mouse.
DR   PRO; PR:Q8C0C7; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q8C0C7; Protein.
DR   Bgee; ENSMUSG00000003808; Expressed in spermatocyte and 218 other cell types or tissues.
DR   ExpressionAtlas; Q8C0C7; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0009328; C:phenylalanine-tRNA ligase complex; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0004826; F:phenylalanine-tRNA ligase activity; ISS:UniProtKB.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; ISS:UniProtKB.
DR   GO; GO:0051290; P:protein heterotetramerization; ISS:UniProtKB.
DR   CDD; cd00496; PheRS_alpha_core; 1.
DR   Gene3D; 1.10.10.2320; -; 1.
DR   Gene3D; 1.10.10.2330; -; 1.
DR   Gene3D; 3.30.1370.240; -; 1.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004529; Phe-tRNA-synth_IIc_asu.
DR   InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR   InterPro; IPR040724; PheRS_DBD1.
DR   InterPro; IPR040586; PheRS_DBD2.
DR   InterPro; IPR040725; PheRS_DBD3.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   NCBIfam; TIGR00468; pheS; 1.
DR   PANTHER; PTHR11538:SF40; PHENYLALANINE--TRNA LIGASE ALPHA SUBUNIT; 1.
DR   PANTHER; PTHR11538; PHENYLALANYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF18552; PheRS_DBD1; 1.
DR   Pfam; PF18554; PheRS_DBD2; 1.
DR   Pfam; PF18553; PheRS_DBD3; 1.
DR   Pfam; PF01409; tRNA-synt_2d; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR   Genevisible; Q8C0C7; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Protein biosynthesis; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y285"
FT   CHAIN           2..508
FT                   /note="Phenylalanine--tRNA ligase alpha subunit"
FT                   /id="PRO_0000280447"
FT   BINDING         329
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y285"
FT   BINDING         372..374
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y285"
FT   BINDING         412
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y285"
FT   BINDING         414
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with beta subunit"
FT                   /evidence="ECO:0000250|UniProtKB:A5K9S0"
FT   BINDING         438
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y285"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y285"
FT   MOD_RES         193
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y285"
FT   MOD_RES         301
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         311
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y285"
FT   CONFLICT        291
FT                   /note="G -> D (in Ref. 2; AAH06862/AAH13533)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        343
FT                   /note="Missing (in Ref. 2; AAH13533)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        455
FT                   /note="I -> T (in Ref. 2; AAH06862)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        455
FT                   /note="I -> V (in Ref. 1; BAE32726)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   508 AA;  57599 MW;  9C125BC4D4A26DAA CRC64;
     MADNPVLELL LRRLEVADGG LDSAELATQL GVEHQAVVGA VKSLQALGEV IEAELRSTKC
     WELTTEGEEI AREGSHEARV FRSIPLEGLV QSELMHLPSG KVGFSKAMSN KWIRVDKSAA
     DGPRVFRVVD SIEDEVQKRL QLVQAGQAEK LAEKERNELR KRKLLTEVIL KTYWVSKGKA
     FSTSVSKQEA ELSPEMISSG SWRDRPFKPY NFSARGVLPD SGHLHPLLKV RSQFRQIFLE
     MGFTEMPTDN FIESSFWNFD ALFQPQQHPA RDQHDTFFLR DPAEALQLPM GYVQRVKRTH
     SQGGYGSQGY KYTWKLEEAR KNLLRTHTTA ASARALYQLA QKKPFTPAKY FSIDRVFRNE
     TLDATHLAEF HQIEGVIADH GLTLGHLMGV LREFFTKLGI TQLRFKPAYN PYTEPSMEVF
     SYHQGLKKWV EVGNSGVFRP EMLLPMGLPE NVSVIAWGLS LERPTMIKYG INNIRELVGH
     KVNLQMVYDS PVCRLDIEPR SSKTQEAA
//