LOCUS       NP_084011               1512 aa            linear   ROD 24-DEC-2024
DEFINITION  bifunctional glutamate/proline--tRNA ligase isoform 1 [Mus
            musculus].
ACCESSION   NP_084011 XP_129647 XP_904720 XP_904723 XP_904728 XP_904733
            XP_904735 XP_904740 XP_904744 XP_904748 XP_904752 XP_904758
            XP_921738
VERSION     NP_084011.1
DBSOURCE    REFSEQ: accession NM_029735.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1512)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 1512)
  AUTHORS   Wu,J., Hollinger,J., Bonanno,E., Jiang,F. and Yao,P.
  TITLE     Cardiomyocyte-Specific Loss of Glutamyl-prolyl-tRNA Synthetase
            Leads to Disturbed Protein Homeostasis and Dilated Cardiomyopathy
  JOURNAL   Cells 13 (1), 35 (2023)
   PUBMED   38201239
  REMARK    GeneRIF: Cardiomyocyte-Specific Loss of Glutamyl-prolyl-tRNA
            Synthetase Leads to Disturbed Protein Homeostasis and Dilated
            Cardiomyopathy.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1512)
  AUTHORS   Lee,E.Y., Kim,S.M., Hwang,J.H., Jang,S.Y., Park,S., Choi,S.,
            Lee,G.S., Hwang,J., Moon,J.H., Fox,P.L., Kim,S., Lee,C.H. and
            Kim,M.H.
  TITLE     Glutamyl-prolyl-tRNA synthetase 1 coordinates early endosomal
            anti-inflammatory AKT signaling
  JOURNAL   Nat Commun 13 (1), 6455 (2022)
   PUBMED   36309524
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1512)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1512)
  AUTHORS   Vasu,K., Ramachandiran,I., Terenzi,F., Khan,D., China,A., Khan,K.,
            Chechi,A., Baleanu-Gogonea,C., Gogonea,V. and Fox,P.L.
  TITLE     The zinc-binding domain of mammalian prolyl-tRNA synthetase is
            indispensable for catalytic activity and organism viability
  JOURNAL   iScience 24 (3), 102215 (2021)
   PUBMED   33748704
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1512)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   7  (residues 1 to 1512)
  AUTHORS   Kim,J.Y., Kang,Y.S., Lee,J.W., Kim,H.J., Ahn,Y.H., Park,H., Ko,Y.G.
            and Kim,S.
  TITLE     p38 is essential for the assembly and stability of macromolecular
            tRNA synthetase complex: implications for its physiological
            significance
  JOURNAL   Proc Natl Acad Sci U S A 99 (12), 7912-7916 (2002)
   PUBMED   12060739
REFERENCE   8  (residues 1 to 1512)
  AUTHORS   Piao,Y., Ko,N.T., Lim,M.K. and Ko,M.S.
  TITLE     Construction of long-transcript enriched cDNA libraries from
            submicrogram amounts of total RNAs by a universal PCR amplification
            method
  JOURNAL   Genome Res 11 (9), 1553-1558 (2001)
   PUBMED   11544199
REFERENCE   9  (residues 1 to 1512)
  AUTHORS   Kaiser,E., Hu,B., Becher,S., Eberhard,D., Schray,B., Baack,M.,
            Hameister,H. and Knippers,R.
  TITLE     The human EPRS locus (formerly the QARS locus): a gene encoding a
            class I and a class II aminoacyl-tRNA synthetase
  JOURNAL   Genomics 19 (2), 280-290 (1994)
   PUBMED   8188258
REFERENCE   10 (residues 1 to 1512)
  AUTHORS   Fett,R. and Knippers,R.
  TITLE     The primary structure of human glutaminyl-tRNA synthetase. A highly
            conserved core, amino acid repeat regions, and homologies with
            translation elongation factors
  JOURNAL   J Biol Chem 266 (3), 1448-1455 (1991)
   PUBMED   1988429
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK141072.1, CF537682.1, CB520692.1, BC094679.1, BC058337.1,
            CK635189.1 and AI845980.1.
            
            On or before Dec 7, 2005 this sequence version replaced
            XP_129647.3, XP_904720.1, XP_904723.1, XP_904728.1, XP_904733.1,
            XP_904735.1, XP_904740.1, XP_904744.1, XP_904748.1, XP_904752.1,
            XP_904758.1, XP_921738.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660817.46524.1, BC141049.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849375, SAMN00849380
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1512
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="1"
                     /map="1 89.5 cM"
     Protein         1..1512
                     /product="bifunctional glutamate/proline--tRNA ligase
                     isoform 1"
                     /EC_number="6.1.1.15"
                     /EC_number="6.1.1.17"
                     /note="bifunctional aminoacyl-tRNA synthetase;
                     glutamine-proline-tRNA synthetase; bifunctional
                     glutamate/proline--tRNA ligase"
                     /calculated_mol_wt=169949
     Region          6..711
                     /region_name="PLN02907"
                     /note="glutamate-tRNA ligase"
                     /db_xref="CDD:215492"
     Region          164..759
                     /region_name="Glutamate--tRNA ligase.
                     /evidence=ECO:0000250|UniProtKB:P28668"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CGC7.4)"
     Region          204..214
                     /region_name="'HIGH' region.
                     /evidence=ECO:0000250|UniProtKB:P28668"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CGC7.4)"
     Region          294..315
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CGC7.4)"
     Site            300
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (Q8CGC7.4)"
     Site            355
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P07814; propagated from
                     UniProtKB/Swiss-Prot (Q8CGC7.4)"
     Site            417
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P07814; propagated from
                     UniProtKB/Swiss-Prot (Q8CGC7.4)"
     Region          432..436
                     /region_name="'KMSKS' region.
                     /evidence=ECO:0000250|UniProtKB:P28668"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CGC7.4)"
     Site            434
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P07814; propagated from
                     UniProtKB/Swiss-Prot (Q8CGC7.4)"
     Site            498
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P07814; propagated from
                     UniProtKB/Swiss-Prot (Q8CGC7.4)"
     Site            535
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P07814; propagated from
                     UniProtKB/Swiss-Prot (Q8CGC7.4)"
     Site            542
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P07814; propagated from
                     UniProtKB/Swiss-Prot (Q8CGC7.4)"
     Site            637
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P07814; propagated from
                     UniProtKB/Swiss-Prot (Q8CGC7.4)"
     Region          709..742
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CGC7.4)"
     Region          753..802
                     /region_name="WEPRS_RNA"
                     /note="WEPRS_RNA binding domain. This short RNA-binding
                     domain is found in several higher eukaryote aminoacyl-tRNA
                     synthetases (aaRSs). It is found in multiple copies in
                     eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases
                     (EPRS) in a region that separates...; cd00936"
                     /db_xref="CDD:238473"
     Region          760..956
                     /region_name="3 X 57 AA approximate repeats.
                     /evidence=ECO:0000250|UniProtKB:P07814"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CGC7.4)"
     Site            order(760,762,765,770,775,779,787,795)
                     /site_type="other"
                     /note="tRNA binding site [nucleotide binding]"
                     /db_xref="CDD:238473"
     Site            788
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (Q8CGC7.4)"
     Region          795..819
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CGC7.4)"
     Region          826..875
                     /region_name="WEPRS_RNA"
                     /note="WEPRS_RNA binding domain. This short RNA-binding
                     domain is found in several higher eukaryote aminoacyl-tRNA
                     synthetases (aaRSs). It is found in multiple copies in
                     eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases
                     (EPRS) in a region that separates...; cd00936"
                     /db_xref="CDD:238473"
     Site            order(833,835,838,843,848,852,860,868)
                     /site_type="other"
                     /note="tRNA binding site [nucleotide binding]"
                     /db_xref="CDD:238473"
     Site            861
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (Q8CGC7.4)"
     Region          869..898
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CGC7.4)"
     Site            872
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P07814; propagated from
                     UniProtKB/Swiss-Prot (Q8CGC7.4)"
     Site            885
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P07814; propagated from
                     UniProtKB/Swiss-Prot (Q8CGC7.4)"
     Region          904..956
                     /region_name="WHEP-TRS"
                     /note="WHEP-TRS domain; pfam00458"
                     /db_xref="CDD:459819"
     Region          956..1011
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CGC7.4)"
     Site            998
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P07814; propagated from
                     UniProtKB/Swiss-Prot (Q8CGC7.4)"
     Site            999
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by RPS6KB1.
                     /evidence=ECO:0000269|PubMed:23071094; propagated from
                     UniProtKB/Swiss-Prot (Q8CGC7.4)"
     Region          1007..1512
                     /region_name="Proline--tRNA ligase.
                     /evidence=ECO:0000250|UniProtKB:P28668"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CGC7.4)"
     Region          1018..1512
                     /region_name="proS_fam_I"
                     /note="prolyl-tRNA synthetase, family I; TIGR00408"
                     /db_xref="CDD:273062"
     Site            1152
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P07814; propagated from
                     UniProtKB/Swiss-Prot (Q8CGC7.4)"
     Site            1350
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P07814; propagated from
                     UniProtKB/Swiss-Prot (Q8CGC7.4)"
     Site            1503
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P07814; propagated from
                     UniProtKB/Swiss-Prot (Q8CGC7.4)"
     CDS             1..1512
                     /gene="Eprs1"
                     /gene_synonym="2410081F06Rik; 3010002K18Rik; Eprs; Qprs"
                     /coded_by="NM_029735.2:155..4693"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS35818.1"
                     /db_xref="GeneID:107508"
                     /db_xref="MGI:MGI:97838"
ORIGIN      
        1 maalcltvna gnpplealla vehvkgdvsi sveegkenll rvsetvaftd vnsilrylar
       61 iattsglygt nlmehteidh wlefsatkls scdrltsain elnhclslrt ylvgnsltla
      121 dlcvwatlkg saawqehlkq nktlvhvkrw fgfleaqqaf rsvgtkwdvs gnratvapdk
      181 kqdvgkfvel pgaemgkvtv rfppeasgyl highakaall nqhyqvnfkg klimrfddtn
      241 pekekedfek viledvamlh ikpdqftyts dhfetimkya ekliqegkay vddtpaeqmk
      301 aereqrtesk hrknsveknl qmweemkkgs qfgqscclra kidmssnngc mrdptlyrck
      361 iqphprtgnk ynvyptydfa cpivdsiegv thalrtteyh drdeqfywii ealgirkpyi
      421 weysrlnlnn tvlskrkltw fvneglvdgw ddprfptvrg vlrrgmtveg lkqfiaaqgs
      481 srsvvnmewd kiwafnkkvi dpvapryval lkkevvpvnv ldaqeemkev arhpknpdvg
      541 lkpvwyspkv fiegadaetf segemvtfin wgninitkih knadgkitsl daklnlenkd
      601 ykkttkitwl aesthalsip avcvtyehli tkpvlgkded fkqyinkdsk heelmlgdpc
      661 lkdlkkgdii qlqrrgffic dqpyepvspy screapcili yipdghtkem ptsgskektk
      721 veiskketss apkerpapav sstcataeds svlysrvavq gdvvrelkak kapkedidaa
      781 vkqlltlkae ykektgqeyk pgnpsaaavq tvstksssnt vestslynkv aaqgevvrkl
      841 kaekapkakv teavecllsl kaeykektgk dyvpgqppas qnshsnpvsn aqpagaekpe
      901 akvlfdrvac qgevvrklka ekaskdqvds avqellqlka qyksltgiey kpvsatgaed
      961 kdkkkkeken ksekqnkpqk qndgqgkdss ksqgsglssg gagegqgpkk qtrlgleakk
     1021 eenlaewysq vitksemiey ydvsgcyilr pwsysiwesi kdffdaeikk lgvencyfpi
     1081 fvsqaaleke knhiedfape vawvtrsgkt elaepiairp tsetvmypay akwvqshrdl
     1141 pvrlnqwcnv vrwefkhpqp flrtreflwq eghsafatfe eaadevlqil elyarvyeel
     1201 laipvvrgrk tekekfaggd ytttieafis asgraiqgat shhlgqnfsk mceivfedpk
     1261 tpgekqfayq cswglttrti gvmvmvhgdn mglvlpprva svqvvvipcg itnalseedr
     1321 ealmakcney rrrllganir vrvdlrdnys pgwkfnhwel kgvpvrlevg prdmkscqfv
     1381 avrrdtgekl tiaekeaeak lekvlediql nlftrasedl kthmvvsntl edfqkvldag
     1441 kvaqipfcge idcedwikkm tardqdvepg apsmgakslc ipfnplcelq pgamcvcgkn
     1501 pakfytlfgr sy
//
