LOCUS       NP_598766                874 aa            linear   ROD 28-JUL-2024
DEFINITION  ectonucleotide pyrophosphatase/phosphodiesterase family member 3
            [Mus musculus].
ACCESSION   NP_598766 XP_125594
VERSION     NP_598766.2
DBSOURCE    REFSEQ: accession NM_134005.2
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 874)
  AUTHORS   Mardjuki,R., Wang,S., Carozza,J., Zirak,B., Subramanyam,V.,
            Abhiraman,G., Lyu,X., Goodarzi,H. and Li,L.
  TITLE     Identification of the extracellular membrane protein ENPP3 as a
            major cGAMP hydrolase and innate immune checkpoint
  JOURNAL   Cell Rep 43 (5), 114209 (2024)
   PUBMED   38749434
  REMARK    GeneRIF: Identification of the extracellular membrane protein ENPP3
            as a major cGAMP hydrolase and innate immune checkpoint.
REFERENCE   2  (residues 1 to 874)
  AUTHORS   Furuta,Y., Tsai,S.H., Kinoshita,M., Fujimoto,K., Okumura,R.,
            Umemoto,E., Kurashima,Y., Kiyono,H., Kayama,H. and Takeda,K.
  TITLE     E-NPP3 controls plasmacytoid dendritic cell numbers in the small
            intestine
  JOURNAL   PLoS One 12 (2), e0172509 (2017)
   PUBMED   28225814
  REMARK    GeneRIF: In Enpp3-/- mice, ATP concentrations were increased in the
            intestinal lumen. Plasmacytoid dendritic cell (pDC) numbers were
            remarkably decreased in the small intestinal lamina propria and
            Peyer's patches. Intestinal pDCs of Enpp3-/- mice showed enhanced
            cell death.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 874)
  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
  REMARK    GeneRIF: E-NPP3 decreases ATP concentration and suppresses basophil
            and mast cell activity.
REFERENCE   4  (residues 1 to 874)
  AUTHORS   Lieben,L., Stockmans,I., Moermans,K. and Carmeliet,G.
  TITLE     Maternal hypervitaminosis D reduces fetal bone mass and mineral
            acquisition and leads to neonatal lethality
  JOURNAL   Bone 57 (1), 123-131 (2013)
   PUBMED   23895994
REFERENCE   5  (residues 1 to 874)
  AUTHORS   Korekane,H., Park,J.Y., Matsumoto,A., Nakajima,K., Takamatsu,S.,
            Ohtsubo,K., Miyamoto,Y., Hanashima,S., Kanekiyo,K., Kitazume,S.,
            Yamaguchi,Y., Matsuo,I. and Taniguchi,N.
  TITLE     Identification of ectonucleotide pyrophosphatase/phosphodiesterase
            3 (ENPP3) as a regulator of N-acetylglucosaminyltransferase GnT-IX
            (GnT-Vb)
  JOURNAL   J Biol Chem 288 (39), 27912-27926 (2013)
   PUBMED   23960081
REFERENCE   6  (residues 1 to 874)
  AUTHORS   Villa-Bellosta,R., Wang,X., Millan,J.L., Dubyak,G.R. and
            O'Neill,W.C.
  TITLE     Extracellular pyrophosphate metabolism and calcification in
            vascular smooth muscle
  JOURNAL   Am J Physiol Heart Circ Physiol 301 (1), H61-H68 (2011)
   PUBMED   21490328
REFERENCE   7  (residues 1 to 874)
  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
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK132256.1 and BB400671.1.
            
            On Jul 31, 2007 this sequence version replaced NP_598766.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK132256.1, AY630402.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164134 [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..874
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="10"
                     /map="10 12.26 cM"
     Protein         1..874
                     /product="ectonucleotide pyrophosphatase/phosphodiesterase
                     family member 3"
                     /EC_number="3.1.4.1"
                     /EC_number="3.6.1.9"
                     /note="E-NPP 3; PD-Ibeta; phosphodiesterase I beta;
                     phosphodiesterase I/nucleotide pyrophosphatase 3; NPPase;
                     nucleotide diphosphatase; alkaline phosphodiesterase I;
                     dinucleoside polyphosphatase"
                     /calculated_mol_wt=98532
     Site            12..30
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6DYE8.2)"
     Region          50..93
                     /region_name="SO"
                     /note="Somatomedin B -like domains; smart00201"
                     /db_xref="CDD:197571"
     Region          78..80
                     /region_name="Cell attachment site. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6DYE8.2)"
     Region          94..137
                     /region_name="SO"
                     /note="Somatomedin B -like domains; smart00201"
                     /db_xref="CDD:197571"
     Region          160..544
                     /region_name="Phosphodiesterase.
                     /evidence=ECO:0000250|UniProtKB:O14638"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6DYE8.2)"
     Region          161..485
                     /region_name="Phosphodiest"
                     /note="Type I phosphodiesterase / nucleotide
                     pyrophosphatase; pfam01663"
                     /db_xref="CDD:396300"
     Site            order(167,204..205,226,325,329,372..373,482)
                     /site_type="active"
                     /db_xref="CDD:293742"
     Site            order(167,204..205,226,325,329,373,482)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:293742"
     Site            236
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6DYE8.2)"
     Site            279
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6DYE8.2)"
     Site            288
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6DYE8.2)"
     Site            425
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6DYE8.2)"
     Site            507..509
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:293742"
     Site            532
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6DYE8.2)"
     Region          581..874
                     /region_name="Nuclease.
                     /evidence=ECO:0000250|UniProtKB:O14638"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6DYE8.2)"
     Site            594
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (Q6DYE8.2)"
     Region          627..856
                     /region_name="NUC"
                     /note="DNA/RNA non-specific endonuclease; smart00477"
                     /db_xref="CDD:214683"
     Site            687
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6DYE8.2)"
     Site            order(689..690,692,728,732)
                     /site_type="active"
                     /db_xref="CDD:238043"
     Site            order(689..690,732)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238043"
     Site            701
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6DYE8.2)"
     Site            820
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6DYE8.2)"
     CDS             1..874
                     /gene="Enpp3"
                     /gene_synonym="CD203c"
                     /coded_by="NM_134005.2:103..2727"
                     /db_xref="CCDS:CCDS23752.1"
                     /db_xref="GeneID:209558"
                     /db_xref="MGI:MGI:2143702"
ORIGIN      
        1 mdsrlalate epikkdslkk ykilcvvlla llvivslglg lglglrkpee qgscrkkcfd
       61 sshrglegcr cdsgctgrgd ccwdfedtcv kstqiwtcnl frcgenrlet alcscaddcl
      121 qrkdccadyk tvcqgespwv teacassqep qcppgfdlpp vilfsmdgfr aeylqtwstl
      181 lpninklktc gihskymram yptktfpnhy tivtglypes hgiidnnmyd vhlnknfsls
      241 sveksnpaww sgqpiwltam yqglkaacyy wpgsdvavng sfptiyrnys nsvpyerrit
      301 tllqwldlpk adrpsfytiy veepdsaghs sgpvsagvik alqsvdnafg mlmeglkqrn
      361 lhncvniivl adhgmdqtsc drveymtdyf pkinfymyqg paprirtrni pqdfftfnse
      421 eivrnlscrk pdqhfkpylt pdlpkrlhya knvridkahl mvdrqwlafr skgssncggg
      481 thgynnefks meaiflahgp sfiektviep fenievynll cdllhiepap nngthgslnh
      541 llktpfykps hagelstpad cgfttplptd pldcscpalq ntpgleeqan qrlnlsegev
      601 aatvkanlpf grprvmqkng dhcllyhrdy isgygkamkm pmwssytvlk pgdtsslppt
      661 vpdclradvr vapsesqkcs fyladknith gflypaikgt nesrydalit snlvpmykef
      721 kkmwdyfhev llikyaiern glnvvsgpif dynydghfda pdeitqyvag tdvpipthyf
      781 vvltsckdqt htpdscpgwl dvlpfivphr ptniescsen ktedlwveer fqahaarvrd
      841 velltgldfy qekaqpvsqi lqlktylptf etii
//
