LOCUS       NP_062243                875 aa            linear   ROD 28-JUL-2024
DEFINITION  ectonucleotide pyrophosphatase/phosphodiesterase family member 3
            [Rattus norvegicus].
ACCESSION   NP_062243 XP_346529
VERSION     NP_062243.2
DBSOURCE    REFSEQ: accession NM_019370.2
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 875)
  AUTHORS   Dohler,C., Zebisch,M., Krinke,D., Robitzki,A. and Strater,N.
  TITLE     Crystallization of ectonucleotide
            phosphodiesterase/pyrophosphatase-3 and orientation of the SMB
            domains in the full-length ectodomain
  JOURNAL   Acta Crystallogr F Struct Biol Commun 74 (Pt 11), 696-703 (2018)
   PUBMED   30387774
  REMARK    GeneRIF: NPP3 crystall structure at 2.77 A resolution reveals that
            the active-site zinc ions are missing and a large part of the
            active site and the surrounding residues are flexible.
REFERENCE   2  (residues 1 to 875)
  AUTHORS   Gorelik,A., Randriamihaja,A., Illes,K. and Nagar,B.
  TITLE     Structural basis for nucleotide recognition by the ectoenzyme
            CD203c
  JOURNAL   FEBS J 285 (13), 2481-2494 (2018)
   PUBMED   29717535
REFERENCE   3  (residues 1 to 875)
  AUTHORS   Tsai,S.H., Kinoshita,M., Kusu,T., Kayama,H., Okumura,R., Ikeda,K.,
            Shimada,Y., Takeda,A., Yoshikawa,S., Obata-Ninomiya,K.,
            Kurashima,Y., Sato,S., Umemoto,E., Kiyono,H., Karasuyama,H. and
            Takeda,K.
  TITLE     The ectoenzyme E-NPP3 negatively regulates ATP-dependent chronic
            allergic responses by basophils and mast cells
  JOURNAL   Immunity 42 (2), 279-293 (2015)
   PUBMED   25692702
REFERENCE   4  (residues 1 to 875)
  AUTHORS   Jankowski,M., Piwkowska,A., Rogacka,D., Audzeyenka,I.,
            Janaszak-Jasiecka,A. and Angielski,S.
  TITLE     Expression of membrane-bound NPP-type ecto-phosphodiesterases in
            rat podocytes cultured at normal and high glucose concentrations
  JOURNAL   Biochem Biophys Res Commun 416 (1-2), 64-69 (2011)
   PUBMED   22086174
  REMARK    GeneRIF: ecto-nucleotide pyrophosphatase/phosphodiesterase 1 and 3
            are expressed on podocytes, but changes in expression of these
            enzymes are most likely not involved in etiology of insulin
            resistance in podocytes.
REFERENCE   5  (residues 1 to 875)
  AUTHORS   Gonzalez-Begne,M., Lu,B., Han,X., Hagen,F.K., Hand,A.R.,
            Melvin,J.E. and Yates,J.R.
  TITLE     Proteomic analysis of human parotid gland exosomes by
            multidimensional protein identification technology (MudPIT)
  JOURNAL   J Proteome Res 8 (3), 1304-1314 (2009)
   PUBMED   19199708
REFERENCE   6  (residues 1 to 875)
  AUTHORS   Meerson,N.R., Bello,V., Delaunay,J.L., Slimane,T.A., Delautier,D.,
            Lenoir,C., Trugnan,G. and Maurice,M.
  TITLE     Intracellular traffic of the ecto-nucleotide
            pyrophosphatase/phosphodiesterase NPP3 to the apical plasma
            membrane of MDCK and Caco-2 cells: apical targeting occurs in the
            absence of N-glycosylation
  JOURNAL   J Cell Sci 113 Pt 23, 4193-4202 (2000)
   PUBMED   11069764
REFERENCE   7  (residues 1 to 875)
  AUTHORS   Johnson,K., Vaingankar,S., Chen,Y., Moffa,A., Goldring,M.B.,
            Sano,K., Jin-Hua,P., Sali,A., Goding,J. and Terkeltaub,R.
  TITLE     Differential mechanisms of inorganic pyrophosphate production by
            plasma cell membrane glycoprotein-1 and B10 in chondrocytes
  JOURNAL   Arthritis Rheum 42 (9), 1986-1997 (1999)
   PUBMED   10513816
REFERENCE   8  (residues 1 to 875)
  AUTHORS   Kettenhofen,R., Meyer zu Brickwedde,M.K., KO,Y., Vetter,H. and
            Sachinidis,A.
  TITLE     Identification of a phosphodiesterase I/nucleotide
            pyrophosphatase-related gene mRNA in rat vascular smooth muscle
            cells by the differential display approach
  JOURNAL   J Mol Biol 279 (2), 323-329 (1998)
   PUBMED   9642040
REFERENCE   9  (residues 1 to 875)
  AUTHORS   Scott,L.J., Delautier,D., Meerson,N.R., Trugnan,G., Goding,J.W. and
            Maurice,M.
  TITLE     Biochemical and molecular identification of distinct forms of
            alkaline phosphodiesterase I expressed on the apical and
            basolateral plasma membrane surfaces of rat hepatocytes
  JOURNAL   Hepatology 25 (4), 995-1002 (1997)
   PUBMED   9096610
REFERENCE   10 (residues 1 to 875)
  AUTHORS   Deissler,H., Lottspeich,F. and Rajewsky,M.F.
  TITLE     Affinity purification and cDNA cloning of rat neural
            differentiation and tumor cell surface antigen gp130RB13-6 reveals
            relationship to human and murine PC-1
  JOURNAL   J Biol Chem 270 (17), 9849-9855 (1995)
   PUBMED   7730366
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC097326.1.
            
            On Dec 11, 2007 this sequence version replaced NP_062243.1.
            
            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 :: BC097326.1, U78787.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760384, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..875
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p12"
     Protein         1..875
                     /product="ectonucleotide pyrophosphatase/phosphodiesterase
                     family member 3"
                     /EC_number="3.1.4.1"
                     /EC_number="3.6.1.9"
                     /note="RB13-6 antigen; NPPase; phosphodiesterase I beta;
                     phosphodiesterase I/nucleotide pyrophosphatase 3; alkaline
                     phosphodiesterase; ectonucleotide
                     pyrophosphatase/phosphodiesterase family member 3-like;
                     nucleotide diphosphatase; alkaline phosphodiesterase I;
                     dinucleoside polyphosphatase"
                     /calculated_mol_wt=98941
     Site            12..30
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P97675.2)"
     Region          51..94
                     /region_name="SO"
                     /note="Somatomedin B -like domains; smart00201"
                     /db_xref="CDD:197571"
     Region          79..81
                     /region_name="Cell attachment site. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P97675.2)"
     Region          95..138
                     /region_name="SO"
                     /note="Somatomedin B -like domains; smart00201"
                     /db_xref="CDD:197571"
     Region          161..545
                     /region_name="Phosphodiesterase.
                     /evidence=ECO:0000250|UniProtKB:O14638"
                     /note="propagated from UniProtKB/Swiss-Prot (P97675.2)"
     Region          162..486
                     /region_name="Phosphodiest"
                     /note="Type I phosphodiesterase / nucleotide
                     pyrophosphatase; pfam01663"
                     /db_xref="CDD:396300"
     Site            order(168,205..206,227,326,330,373..374,483)
                     /site_type="active"
                     /db_xref="CDD:293742"
     Site            order(168,205..206,227,326,330,374,483)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:293742"
     Site            237
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97675.2)"
     Site            280
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97675.2)"
     Site            289
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97675.2)"
     Site            508..510
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:293742"
     Site            533
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97675.2)"
     Site            574
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97675.2)"
     Region          582..875
                     /region_name="Nuclease.
                     /evidence=ECO:0000250|UniProtKB:O14638"
                     /note="propagated from UniProtKB/Swiss-Prot (P97675.2)"
     Site            594
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97675.2)"
     Region          608..867
                     /region_name="NUC"
                     /note="DNA/RNA non-specific endonuclease; prokaryotic and
                     eukaryotic double- and single-stranded DNA and RNA
                     endonucleases also present in phosphodiesterases. They
                     exists as monomers and homodimers; cd00091"
                     /db_xref="CDD:238043"
     Site            order(689..690,692,729,733)
                     /site_type="active"
                     /db_xref="CDD:238043"
     Site            order(689..690,733)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238043"
     Site            702
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97675.2)"
     Site            789
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97675.2)"
     CDS             1..875
                     /gene="Enpp3"
                     /gene_synonym="B10; E-NPP 3; Npp3; PD-Ibeta; RB13-6"
                     /coded_by="NM_019370.2:57..2684"
                     /db_xref="GeneID:54410"
                     /db_xref="RGD:708511"
ORIGIN      
        1 mdsrlalate epikkdslkr ykilcavlla llvivslglg lglglrkpee higscrkkcf
       61 dsshrglegc rcdsgctdrg dccwdfedtc vkstqiwtcn sfrcgetrle aalcscaddc
      121 lqrkdcctdy kavcqgevpw vteacassqe pqcpegfdqp pvilfsmdgf raeylqtwst
      181 llpninklkt cglhskymra myptktfpnh ytivtglype shgiidnnmy dvylnknfsl
      241 ssveksnpaw wsgqpiwlta myqglkaasy ywpgsdvavn gsfpniyrny snsvpyesri
      301 atllqwldlp kaerpsfyti yveepdsagh ksgpvsagvi kalqlvddaf gmlmeglkqr
      361 nlhncvniiv ladhgmdqts cdrveymtdy fpeinfymyq gpaprirtrn ipqdfftfns
      421 eeivrdlscr ksdqhfkpyl tpdlpkrlhy aknvridkvh lmvdrqwlay rnkgssnceg
      481 gthgynnefk smeaiflahg psfkektvie pfenievynl lcdllhiqpa pnngshgsln
      541 hllkapfyqp shaeelsksa gcgfttplpk dslncsclal qtsgqeeqvn qrlnlsggev
      601 satektnlpf grprviqknk dhcllyhrey vsgfgkamkm pmwssytvpk pgdtsslppt
      661 vpdclradvr vdpsesqkcs fyladqnidh gflyppaikg nnesqydali tsnlvpmyke
      721 fkkmwdyfhk vllikyaier ngvnvvsgpi fdynydghfd apdeitnyva gtdvpvpthy
      781 fvvltscknk thtpdscpgw ldvlpfvvph rptnvescpe nkaedlwvee rfkahiarvr
      841 dvelltgldf yqektqpvse ilqlktylpt fetii
//
