LOCUS       NP_001007607             512 aa            linear   ROD 02-JUN-2024
DEFINITION  serine--tRNA ligase, cytoplasmic [Rattus norvegicus].
ACCESSION   NP_001007607 XP_342320
VERSION     NP_001007607.1
DBSOURCE    REFSEQ: accession NM_001007606.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Musante,L., Puttmann,L., Kahrizi,K., Garshasbi,M., Hu,H., Stehr,H.,
            Lipkowitz,B., Otto,S., Jensen,L.R., Tzschach,A., Jamali,P.,
            Wienker,T., Najmabadi,H., Ropers,H.H. and Kuss,A.W.
  TITLE     Mutations of the aminoacyl-tRNA-synthetases SARS and WARS2 are
            implicated in the etiology of autosomal recessive intellectual
            disability
  JOURNAL   Hum Mutat 38 (6), 621-636 (2017)
   PUBMED   28236339
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Wang,C., Guo,Y., Tian,Q., Jia,Q., Gao,Y., Zhang,Q., Zhou,C. and
            Xie,W.
  TITLE     SerRS-tRNASec complex structures reveal mechanism of the first step
            in selenocysteine biosynthesis
  JOURNAL   Nucleic Acids Res 43 (21), 10534-10545 (2015)
   PUBMED   26433229
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Shi,Y., Xu,X., Zhang,Q., Fu,G., Mo,Z., Wang,G.S., Kishi,S. and
            Yang,X.L.
  TITLE     tRNA synthetase counteracts c-Myc to develop functional vasculature
  JOURNAL   Elife 3, e02349 (2014)
   PUBMED   24940000
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 512)
  AUTHORS   Ikromov,O., Alkamal,I., Magheli,A., Ratert,N., Sendeski,M.,
            Miller,K., Krause,H. and Kempkensteffen,C.
  TITLE     Functional Epigenetic Analysis of Prostate Carcinoma: A Role for
            Seryl-tRNA Synthetase?
  JOURNAL   J Biomark 2014, 362164 (2014)
   PUBMED   26317032
REFERENCE   5  (residues 1 to 512)
  AUTHORS   Xu,X., Shi,Y. and Yang,X.L.
  TITLE     Crystal structure of human Seryl-tRNA synthetase and Ser-SA complex
            reveals a molecular lever specific to higher eukaryotes
  JOURNAL   Structure 21 (11), 2078-2086 (2013)
   PUBMED   24095058
REFERENCE   6  (residues 1 to 512)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   7  (residues 1 to 512)
  AUTHORS   Miseta,A., Woodley,C.L., Greenberg,J.R. and Slobin,L.I.
  TITLE     Mammalian seryl-tRNA synthetase associates with mRNA in vivo and
            has homology to elongation factor 1 alpha
  JOURNAL   J Biol Chem 266 (29), 19158-19161 (1991)
   PUBMED   1918033
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC061765.1.
            
            On Nov 29, 2004 this sequence version replaced XP_342320.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC061765.1, SRR8487227.99464.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760434
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..512
                     /product="serine--tRNA ligase, cytoplasmic"
                     /EC_number="6.1.1.11"
                     /note="seryl-tRNA synthetase, cytoplasmic; serRS;
                     seryl-tRNA(Ser/Sec) synthetase; seryl-aminoacyl-tRNA
                     synthetase 1"
                     /calculated_mol_wt=58457
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P49591; propagated from
                     UniProtKB/Swiss-Prot (Q6P799.3)"
     Region          3..486
                     /region_name="PLN02678"
                     /note="seryl-tRNA synthetase"
                     /db_xref="CDD:215364"
     Region          9..61
                     /region_name="Interaction with tRNA.
                     /evidence=ECO:0000250|UniProtKB:P49591"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P799.3)"
     Site            241
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49591; propagated from
                     UniProtKB/Swiss-Prot (Q6P799.3)"
     Site            323
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P49591; propagated from
                     UniProtKB/Swiss-Prot (Q6P799.3)"
     Site            429
                     /site_type="other"
                     /note="Important for serine binding.
                     /evidence=ECO:0000250|UniProtKB:P49591; propagated from
                     UniProtKB/Swiss-Prot (Q6P799.3)"
     Region          472..512
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P799.3)"
     Region          482..494
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250|UniProtKB:P49591"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P799.3)"
     CDS             1..512
                     /gene="Sars1"
                     /gene_synonym="Sars"
                     /coded_by="NM_001007606.1:59..1597"
                     /db_xref="GeneID:266975"
                     /db_xref="RGD:628813"
ORIGIN      
        1 mvldldlfrv dkggdpalir etqekrfkdp glvdqlvkad sewrrcrfra dnlnklknlc
       61 sktigekmkk kepvgedesi pedvlnfddl tadtlaalkv sqikkvrllv deaiqkcdge
      121 rvkleaerfe nlreignllh psvpisnded adnkveriwg dctvrkkysh vdlvvmvdgf
      181 egekgavvag srgyflkgvl vfleqaliqy alrtlgsrgy tpiytpffmr kevmqevaql
      241 sqfdeelykv igkgseksdd ssydekylia tseqpiaalh rdewlrpedl pikyagfstc
      301 frqevgshgr dtrgifrvhq fekieqfvys sphdnkswem fdemittaee fyqslgipyh
      361 ivnivsgsln haaskkldle awfpgsgafr elvscsnctd yqarrlriry gqtkkmmdkv
      421 efvhmlnatm cattrticai lenyqtekgi vvpeklrefm ppglqelipf vkpapidqep
      481 skkqkkqheg skkkakevtl enqlqnmevt ea
//
