LOCUS       NP_001034092             506 aa            linear   ROD 24-JUN-2024
DEFINITION  methionine synthase reductase [Rattus norvegicus].
ACCESSION   NP_001034092 XP_225078
VERSION     NP_001034092.1
DBSOURCE    REFSEQ: accession NM_001039003.1
KEYWORDS    RefSeq.
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 506)
  AUTHORS   Cheng,H., Li,H., Bu,Z., Zhang,Q., Bai,B., Zhao,H., Li,R.K.,
            Zhang,T. and Xie,J.
  TITLE     Functional variant in methionine synthase reductase intron-1 is
            associated with pleiotropic congenital malformations
  JOURNAL   Mol Cell Biochem 407 (1-2), 51-56 (2015)
   PUBMED   26045171
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Gherasim,C., Yadav,P.K., Kabil,O., Niu,W.N. and Banerjee,R.
  TITLE     Nitrite reductase activity and inhibition of HS biogenesis by human
            cystathionine ss-synthase
  JOURNAL   PLoS One 9 (1), e85544 (2014)
   PUBMED   24416422
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 506)
  AUTHORS   Padmanabhan,N., Jia,D., Geary-Joo,C., Wu,X., Ferguson-Smith,A.C.,
            Fung,E., Bieda,M.C., Snyder,F.F., Gravel,R.A., Cross,J.C. and
            Watson,E.D.
  TITLE     Mutation in folate metabolism causes epigenetic instability and
            transgenerational effects on development
  JOURNAL   Cell 155 (1), 81-93 (2013)
   PUBMED   24074862
REFERENCE   4  (residues 1 to 506)
  AUTHORS   Lautner-Csorba,O., Gezsi,A., Erdelyi,D.J., Hullam,G., Antal,P.,
            Semsei,A.F., Kutszegi,N., Kovacs,G., Falus,A. and Szalai,C.
  TITLE     Roles of genetic polymorphisms in the folate pathway in childhood
            acute lymphoblastic leukemia evaluated by Bayesian relevance and
            effect size analysis
  JOURNAL   PLoS One 8 (8), e69843 (2013)
   PUBMED   23940529
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 506)
  AUTHORS   Zhao,J.Y., Yang,X.Y., Gong,X.H., Gu,Z.Y., Duan,W.Y., Wang,J.,
            Ye,Z.Z., Shen,H.B., Shi,K.H., Hou,J., Huang,G.Y., Jin,L., Qiao,B.
            and Wang,H.Y.
  TITLE     Functional variant in methionine synthase reductase intron-1
            significantly increases the risk of congenital heart disease in the
            Han Chinese population
  JOURNAL   Circulation 125 (3), 482-490 (2012)
   PUBMED   22179537
REFERENCE   6  (residues 1 to 506)
  AUTHORS   Gemmati,D., Ongaro,A., Scapoli,G.L., Della Porta,M., Tognazzo,S.,
            Serino,M.L., Di Bona,E., Rodeghiero,F., Gilli,G., Reverberi,R.,
            Caruso,A., Pasello,M., Pellati,A. and De Mattei,M.
  TITLE     Common gene polymorphisms in the metabolic folate and methylation
            pathway and the risk of acute lymphoblastic leukemia and
            non-Hodgkin's lymphoma in adults
  JOURNAL   Cancer Epidemiol Biomarkers Prev 13 (5), 787-794 (2004)
   PUBMED   15159311
REFERENCE   7  (residues 1 to 506)
  AUTHORS   Gueant-Rodriguez,R.M., Rendeli,C., Namour,B., Venuti,L., Romano,A.,
            Anello,G., Bosco,P., Debard,R., Gerard,P., Viola,M., Salvaggio,E.
            and Gueant,J.L.
  TITLE     Transcobalamin and methionine synthase reductase mutated
            polymorphisms aggravate the risk of neural tube defects in humans
  JOURNAL   Neurosci Lett 344 (3), 189-192 (2003)
   PUBMED   12812837
REFERENCE   8  (residues 1 to 506)
  AUTHORS   Pietrzyk,J.J., Bik-Multanowski,M., Sanak,M. and Twardowska,M.
  TITLE     Polymorphisms of the 5,10-methylenetetrahydrofolate and the
            methionine synthase reductase genes as independent risk factors for
            spina bifida
  JOURNAL   J Appl Genet 44 (1), 111-113 (2003)
   PUBMED   12590188
REFERENCE   9  (residues 1 to 506)
  AUTHORS   Doolin,M.T., Barbaux,S., McDonnell,M., Hoess,K., Whitehead,A.S. and
            Mitchell,L.E.
  TITLE     Maternal genetic effects, exerted by genes involved in homocysteine
            remethylation, influence the risk of spina bifida
  JOURNAL   Am J Hum Genet 71 (5), 1222-1226 (2002)
   PUBMED   12375236
REFERENCE   10 (residues 1 to 506)
  AUTHORS   Olteanu,H. and Banerjee,R.
  TITLE     Human methionine synthase reductase, a soluble P-450 reductase-like
            dual flavoprotein, is sufficient for NADPH-dependent methionine
            synthase activation
  JOURNAL   J Biol Chem 276 (38), 35558-35563 (2001)
   PUBMED   11466310
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC100107.1.
            
            On Jan 12, 2006 this sequence version replaced XP_225078.3.
            
            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 :: BC100107.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00155337, SAMN06621351
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p11"
     Protein         1..506
                     /product="methionine synthase reductase"
                     /EC_number="1.16.1.8"
                     /note="aqCbl reductase; aquacobalamin reductase"
                     /calculated_mol_wt=56400
     Region          6..>50
                     /region_name="Flavodoxin_1"
                     /note="pfam00258"
                     /db_xref="CDD:425562"
     Region          84..505
                     /region_name="methionine_synthase_red"
                     /note="Human methionine synthase reductase (MSR) restores
                     methionine sythase which is responsible for the
                     regeneration of methionine from homocysteine, as well as
                     the coversion of methyltetrahydrofolate to
                     tetrahydrofolate. In MSR, electrons are transferred...;
                     cd06203"
                     /db_xref="CDD:99800"
     Site            order(258..261,276..277,294..297,332,505)
                     /site_type="other"
                     /note="FAD binding pocket [chemical binding]"
                     /db_xref="CDD:99800"
     Site            order(258,260..261)
                     /site_type="other"
                     /note="FAD binding motif [chemical binding]"
                     /db_xref="CDD:99800"
     Site            order(261,458,503,505)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:99800"
     Site            order(278..281,352,354,387..388,417..418,432,434,464)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99800"
     Site            order(294,297,300)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99800"
     Site            order(349,353..356,358)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99800"
     CDS             1..506
                     /gene="Mtrr"
                     /gene_synonym="MSR"
                     /coded_by="NM_001039003.1:77..1597"
                     /db_xref="GeneID:290947"
                     /db_xref="RGD:1308671"
ORIGIN      
        1 mrrflllyat qrgqakaiae eiseqalshg fsadlhcvse seksslsipa vspeylevyl
       61 qeslgqdenq asvppsvdpi fqvpiskave lttndaiktt llleldiskv efshqpgdsf
      121 nvicpnsgse vedllqrlql adkqahrvil kikmdtkkkg aslpqhvpeg sslqfiftwc
      181 leiravpkka flralsdyts datekrrlqe lcskqgaady nrfirdasvc lldllltfps
      241 cqpplnllle hlpklqprpy scasssllhp dklhfvfniv elpsnttaas lrkgvctgwl
      301 atlvapflqp ntevltadhs dalapeilis pratnsfhlp ddlsapiimv gpgtgvapfv
      361 gflqhreklq eqhpdgnfga mwlffgcrhk drdylfreel rhflktgvlt hlkvsfsrda
      421 apeeeeeapa kyvqdnlqhh sqqvartllq engyiyvcgd aknmakdvhd alveiiskea
      481 gvdkleamkt latlkqekry lqdiws
//
