SYFA_MOUSE
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 03-AUG-2022, entry version 145.
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, 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 -!- 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; 10.
DR IntAct; Q8C0C7; 4.
DR STRING; 10090.ENSMUSP00000003906; -.
DR iPTMnet; Q8C0C7; -.
DR PhosphoSitePlus; Q8C0C7; -.
DR SwissPalm; Q8C0C7; -.
DR EPD; Q8C0C7; -.
DR jPOST; Q8C0C7; -.
DR MaxQB; Q8C0C7; -.
DR PaxDb; Q8C0C7; -.
DR PeptideAtlas; Q8C0C7; -.
DR PRIDE; Q8C0C7; -.
DR ProteomicsDB; 258789; -.
DR Antibodypedia; 1072; 142 antibodies from 24 providers.
DR DNASU; 66590; -.
DR Ensembl; ENSMUST00000003906; ENSMUSP00000003906; ENSMUSG00000003808.
DR GeneID; 66590; -.
DR KEGG; mmu:66590; -.
DR UCSC; uc009mnt.2; mouse.
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; 733355at2759; -.
DR PhylomeDB; Q8C0C7; -.
DR TreeFam; TF300647; -.
DR BioGRID-ORCS; 66590; 23 hits in 76 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 215 other tissues.
DR ExpressionAtlas; Q8C0C7; baseline and differential.
DR Genevisible; Q8C0C7; MM.
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: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 Gene3D; 3.30.930.10; -; 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 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; SSF46785; SSF46785; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00468; pheS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
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
