LOCUS       NP_001019925             693 aa            linear   ROD 24-JUN-2024
DEFINITION  GMP synthase [glutamine-hydrolyzing] [Rattus norvegicus].
ACCESSION   NP_001019925 XP_215574
VERSION     NP_001019925.1
DBSOURCE    REFSEQ: accession NM_001024754.1
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 693)
  AUTHORS   Camici,M., Micheli,V., Ipata,P.L. and Tozzi,M.G.
  TITLE     Pediatric neurological syndromes and inborn errors of purine
            metabolism
  JOURNAL   Neurochem Int 56 (3), 367-378 (2010)
   PUBMED   20005278
  REMARK    Review article
REFERENCE   2  (residues 1 to 693)
  AUTHORS   Pegram,L.D., Megonigal,M.D., Lange,B.J., Nowell,P.C., Rowley,J.D.,
            Rappaport,E.F. and Felix,C.A.
  TITLE     t(3;11) translocation in treatment-related acute myeloid leukemia
            fuses MLL with the GMPS (GUANOSINE 5' MONOPHOSPHATE SYNTHETASE)
            gene
  JOURNAL   Blood 96 (13), 4360-4362 (2000)
   PUBMED   11110714
REFERENCE   3  (residues 1 to 693)
  AUTHORS   Nakamura,J. and Lou,L.
  TITLE     Biochemical characterization of human GMP synthetase
  JOURNAL   J Biol Chem 270 (13), 7347-7353 (1995)
   PUBMED   7706277
REFERENCE   4  (residues 1 to 693)
  AUTHORS   Hirst,M., Haliday,E., Nakamura,J. and Lou,L.
  TITLE     Human GMP synthetase. Protein purification, cloning, and functional
            expression of cDNA
  JOURNAL   J Biol Chem 269 (38), 23830-23837 (1994)
   PUBMED   8089153
REFERENCE   5  (residues 1 to 693)
  AUTHORS   Harendza,S.G., Thaiss,F. and Stahl,R.A.
  TITLE     Enhanced in vitro growth of glomerular cells derived from rats with
            immune-mediated mesangial injury
  JOURNAL   Exp Nephrol 1 (1), 55-61 (1993)
   PUBMED   8081953
REFERENCE   6  (residues 1 to 693)
  AUTHORS   Jayaram,H.N., Lui,M.S., Plowman,J., Pillwein,K., Reardon,M.A.,
            Elliott,W.L. and Weber,G.
  TITLE     Oncolytic activity and mechanism of action of a novel L-cysteine
            derivative, L-cysteine, ethyl ester, S-(N-methylcarbamate)
            monohydrochloride
  JOURNAL   Cancer Chemother Pharmacol 26 (2), 88-92 (1990)
   PUBMED   2347042
REFERENCE   7  (residues 1 to 693)
  AUTHORS   Prajda,N., Natsumeda,Y., Ikegami,T., Reardon,M.A., Szondy,S.,
            Hashimoto,Y., Emrani,J. and Weber,G.
  TITLE     Enzymic programs of rat bone marrow and the impact of acivicin and
            tiazofurin
  JOURNAL   Biochem Pharmacol 37 (5), 875-880 (1988)
   PUBMED   3345200
REFERENCE   8  (residues 1 to 693)
  AUTHORS   Pillwein,K., Reardon,M.A., Jayaram,H.N., Natsumeda,Y.,
            Elliott,W.L., Faderan,M.A., Prajda,N., Sperl,W. and Weber,G.
  TITLE     Insulin regulatory effects on purine- and pyrimidine metabolism in
            alloxan diabetic rat liver
  JOURNAL   Padiatr Padol 23 (2), 135-144 (1988)
   PUBMED   3043317
REFERENCE   9  (residues 1 to 693)
  AUTHORS   Hirai,K., Matsuda,Y. and Nakagawa,H.
  TITLE     Purification and characterization of GMP synthetase from Yoshida
            sarcoma ascites cells
  JOURNAL   J Biochem 102 (4), 893-902 (1987)
   PUBMED   3436958
REFERENCE   10 (residues 1 to 693)
  AUTHORS   Zoref-Shani,E., Shainberg,A. and Sperling,O.
  TITLE     Characterization of purine nucleotide metabolism in primary rat
            muscle cultures
  JOURNAL   Biochim Biophys Acta 716 (3), 324-330 (1982)
   PUBMED   6180773
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC098016.1.
            
            On Jun 10, 2005 this sequence version replaced XP_215574.3.
            
            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 :: BC098016.1, SRR8487226.17623.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132262, SAMD00132264
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..693
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q31"
     Protein         1..693
                     /product="GMP synthase [glutamine-hydrolyzing]"
                     /EC_number="6.3.5.2"
                     /note="GMP synthase; GMP synthetase; glutamine
                     amidotransferase; guanine monophosphate synthetase"
                     /calculated_mol_wt=76627
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P49915; propagated from
                     UniProtKB/Swiss-Prot (Q4V7C6.1)"
     Site            8
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49915; propagated from
                     UniProtKB/Swiss-Prot (Q4V7C6.1)"
     Site            9
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P49915; propagated from
                     UniProtKB/Swiss-Prot (Q4V7C6.1)"
     Region          28..693
                     /region_name="guaA"
                     /note="GMP synthase; Reviewed; PRK00074"
                     /db_xref="CDD:234614"
     Site            318
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P49915; propagated from
                     UniProtKB/Swiss-Prot (Q4V7C6.1)"
     Site            332
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4V7C6.1)"
     CDS             1..693
                     /gene="Gmps"
                     /coded_by="NM_001024754.1:63..2144"
                     /db_xref="GeneID:295088"
                     /db_xref="RGD:1310063"
ORIGIN      
        1 malcngdskp enaggdlkdg chhyegavvi ldagaqygkv idrrvrelfv qseifpletp
       61 afaikeqgfr aiiisggpns vyaedapwfd paiftigkpv lgicygmqmm nkvfggtvhk
      121 ksvredgvfn ismdntcslf rglqkeeivl lthgdsvdkv adgfkvvars gnivagiane
      181 skklygvqfh pevgltengk vilknflydi agcsgnftvq nrelecirei kekvgtskvl
      241 vllsggvdst vctallnral nqdqviavhi dngfmrkres qsveealkkl giqvkvinaa
      301 hsfyngtttl pisdedrtpr krisktlnmt tspeekrkii gdtfvkiane vigemslkpe
      361 evflaqgtlr pdliesaslv asgkaelikt hhndtelirk lreegkviep lkdfhkdevr
      421 ilgreldlpe elvsrhpfpg pglairvica eepyickdfp etnnilkiva dfsasvkkph
      481 tllqrvkact teedqeklme itsqhslnaf llpiktvgvq gdcrsysyvc gisskdepdw
      541 esliflarli prmchninrv vyifgppvke pptdvtptfl ttgvlstlrq adfeahnilr
      601 esgyagkisq mpviltplhf drdplqkqps cqrsvvirtf itsdfmtgvp atpgneipve
      661 vvlkmvteik kipgisrimy dltskppgtt ewe
//
