LOCUS       NP_005012                875 aa            linear   PRI 11-SEP-2024
DEFINITION  ectonucleotide pyrophosphatase/phosphodiesterase family member 3
            [Homo sapiens].
ACCESSION   NP_005012
VERSION     NP_005012.2
DBSOURCE    REFSEQ: accession NM_005021.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 875)
  AUTHORS   Qin,Y., Li,Y., Hao,Y., Li,Y. and Kang,S.
  TITLE     Hypomethylation of the ENPP3 promoter region contributes to the
            occurrence and development of ovarian endometriosis via the
            AKT/mTOR/4EBP1 signaling pathway
  JOURNAL   Biomol Biomed 24 (4), 848-856 (2023)
   PUBMED   38149831
  REMARK    GeneRIF: Hypomethylation of the ENPP3 promoter region contributes
            to the occurrence and development of ovarian endometriosis via the
            AKT/mTOR/4EBP1 signaling pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 875)
  AUTHORS   Sadovnik,I., Ivanov,D., Smiljkovic,D., Stefanzl,G.,
            Degenfeld-Schonburg,L., Herndlhofer,S., Eisenwort,G.,
            Hauswirth,A.W., Sliwa,T., Keil,F., Sperr,W.R. and Valent,P.
  TITLE     Identification of CD203c as a New Basophil-Specific Flow-Marker in
            Ph+ Chronic Myeloid Leukemia
  JOURNAL   Cells 12 (1), 3 (2022)
   PUBMED   36611797
  REMARK    GeneRIF: Identification of CD203c as a New Basophil-Specific
            Flow-Marker in Ph[+] Chronic Myeloid Leukemia.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 875)
  AUTHORS   Qi,Z., Xue,Q., Wang,H., Cao,B., Su,Y., Xing,Q. and Yang,J.J.
  TITLE     Serum CD203c+ Extracellular Vesicle Serves as a Novel Diagnostic
            and Prognostic Biomarker for Succinylated Gelatin Induced
            Perioperative Hypersensitive Reaction
  JOURNAL   Front Immunol 12, 732209 (2021)
   PUBMED   34650557
  REMARK    GeneRIF: Serum CD203c+ Extracellular Vesicle Serves as a Novel
            Diagnostic and Prognostic Biomarker for Succinylated Gelatin
            Induced Perioperative Hypersensitive Reaction.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 875)
  AUTHORS   Imamura,S., Washio,K., Mizuno,M., Oda,Y., Fukunaga,A. and
            Nishigori,C.
  TITLE     Activated steady status and distinctive FcepsilonRI-mediated
            responsiveness in basophils of atopic dermatitis
  JOURNAL   Allergol Int 70 (3), 327-334 (2021)
   PUBMED   33674191
  REMARK    GeneRIF: Activated steady status and distinctive
            FcepsilonRI-mediated responsiveness in basophils of atopic
            dermatitis.
REFERENCE   5  (residues 1 to 875)
  AUTHORS   Heneberg,P., Riegerova,K., Rihova,A., Simcikova,D. and Kucera,P.
  TITLE     Updates on the surface antigens of basophils: CD16 on basophils of
            patients with respiratory or insect venom allergy and the rejection
            of CD203c and CD63 externalization decoupling by
            bisindolylmaleimides
  JOURNAL   Clin Exp Allergy 49 (1), 54-67 (2019)
   PUBMED   30288810
  REMARK    GeneRIF: Updates on the surface antigens of basophils: CD16 on
            basophils of patients with respiratory or insect venom allergy and
            the rejection of CD203c and CD63 externalization decoupling by
            bisindolylmaleimides.
REFERENCE   6  (residues 1 to 875)
  AUTHORS   Vollmayer,P., Clair,T., Goding,J.W., Sano,K., Servos,J. and
            Zimmermann,H.
  TITLE     Hydrolysis of diadenosine polyphosphates by nucleotide
            pyrophosphatases/phosphodiesterases
  JOURNAL   Eur J Biochem 270 (14), 2971-2978 (2003)
   PUBMED   12846830
REFERENCE   7  (residues 1 to 875)
  AUTHORS   Buhring,H.J., Seiffert,M., Giesert,C., Marxer,A., Kanz,L.,
            Valent,P. and Sano,K.
  TITLE     The basophil activation marker defined by antibody 97A6 is
            identical to the ectonucleotide pyrophosphatase/phosphodiesterase 3
  JOURNAL   Blood 97 (10), 3303-3305 (2001)
   PUBMED   11342463
REFERENCE   8  (residues 1 to 875)
  AUTHORS   Andoh,K., Piao,J.H., Terashima,K., Nakamura,H. and Sano,K.
  TITLE     Genomic structure and promoter analysis of the
            ecto-phosphodiesterase I gene (PDNP3) expressed in glial cells
  JOURNAL   Biochim Biophys Acta 1446 (3), 213-224 (1999)
   PUBMED   10524196
REFERENCE   9  (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   10 (residues 1 to 875)
  AUTHORS   Jin-Hua,P., Goding,J.W., Nakamura,H. and Sano,K.
  TITLE     Molecular cloning and chromosomal localization of PD-Ibeta (PDNP3),
            a new member of the human phosphodiesterase I genes
  JOURNAL   Genomics 45 (2), 412-415 (1997)
   PUBMED   9344668
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY106781.1, AL121575.24,
            EF560735.1 and AK024899.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 4, 2006 this sequence version replaced NP_005012.1.
            
            Summary: The protein encoded by this gene belongs to a series of
            ectoenzymes that are involved in hydrolysis of extracellular
            nucleotides. These ectoenzymes possess ATPase and ATP
            pyrophosphatase activities and are type II transmembrane proteins.
            Expression of the related rat mRNA has been found in a subset of
            immature glial cells and in the alimentary tract. The corresponding
            rat protein has been detected in the pancreas, small intestine,
            colon, and liver. The human mRNA is expressed in glioma cells,
            prostate, and uterus. Expression of the human protein has been
            detected in uterus, basophils, and mast cells. Two transcript
            variants, one protein coding and the other non-protein coding, have
            been found for this gene. [provided by RefSeq, Oct 2015].
            
            Transcript Variant: This variant (1) represents the longer,
            protein-coding transcript.
            
            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 :: AK024899.1, AK292903.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000357639.8/ ENSP00000350265.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..875
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q23.2"
     Protein         1..875
                     /product="ectonucleotide pyrophosphatase/phosphodiesterase
                     family member 3"
                     /EC_number="3.1.4.1"
                     /EC_number="3.6.1.9"
                     /note="phosphodiesterase-I beta; gp130RB13-6;
                     phosphodiesterase I/nucleotide pyrophosphatase 3;
                     dJ914N13.3 (phosphodiesterase I/nucleotide pyrophosphatase
                     3); NPPase; dJ1005H11.3 (phosphodiesterase I/nucleotide
                     pyrophosphatase 3); nucleotide diphosphatase; alkaline
                     phosphodiesterase I; dinucleoside polyphosphatase"
                     /calculated_mol_wt=99994
     Site            12..30
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O14638.2)"
     Region          51..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 (O14638.2)"
     Region          94..137
                     /region_name="SO"
                     /note="Somatomedin B -like domains; smart00201"
                     /db_xref="CDD:197571"
     Region          159..525
                     /region_name="Enpp"
                     /note="Ectonucleotide pyrophosphatase/phosphodiesterase,
                     also called autotaxin; cd16018"
                     /db_xref="CDD:293742"
     Region          160..545
                     /region_name="Phosphodiesterase.
                     /evidence=ECO:0000305|PubMed:29717535"
                     /note="propagated from UniProtKB/Swiss-Prot (O14638.2)"
     Site            order(167,204..205,226,325,329,372..373,483)
                     /site_type="active"
                     /db_xref="CDD:293742"
     Site            order(167,204..205,226,325,329,373,483)
                     /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:0000269|PubMed:29717535,
                     ECO:0007744|PDB:6C02; propagated from UniProtKB/Swiss-Prot
                     (O14638.2)"
     Site            279
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:29717535,
                     ECO:0007744|PDB:6C02; propagated from UniProtKB/Swiss-Prot
                     (O14638.2)"
     Site            290
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:29717535,
                     ECO:0007744|PDB:6C02; propagated from UniProtKB/Swiss-Prot
                     (O14638.2)"
     Site            426
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:29717535,
                     ECO:0007744|PDB:6C02; propagated from UniProtKB/Swiss-Prot
                     (O14638.2)"
     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:0000269|PubMed:29717535,
                     ECO:0007744|PDB:6C02; propagated from UniProtKB/Swiss-Prot
                     (O14638.2)"
     Region          582..875
                     /region_name="Nuclease.
                     /evidence=ECO:0000305|PubMed:29717535"
                     /note="propagated from UniProtKB/Swiss-Prot (O14638.2)"
     Site            582
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:29717535,
                     ECO:0007744|PDB:6C01; propagated from UniProtKB/Swiss-Prot
                     (O14638.2)"
     Site            594
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:29717535,
                     ECO:0007744|PDB:6C01; propagated from UniProtKB/Swiss-Prot
                     (O14638.2)"
     Region          627..857
                     /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:0000305|PubMed:29717535; propagated from
                     UniProtKB/Swiss-Prot (O14638.2)"
     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            699
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:29717535,
                     ECO:0007744|PDB:6C02; propagated from UniProtKB/Swiss-Prot
                     (O14638.2)"
     Site            789
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:29717535,
                     ECO:0007744|PDB:6C02; propagated from UniProtKB/Swiss-Prot
                     (O14638.2)"
     CDS             1..875
                     /gene="ENPP3"
                     /gene_synonym="B10; CD203c; NPP3; PD-IBETA; PDNP3"
                     /coded_by="NM_005021.5:84..2711"
                     /db_xref="CCDS:CCDS5148.1"
                     /db_xref="GeneID:5169"
                     /db_xref="HGNC:HGNC:3358"
                     /db_xref="MIM:602182"
ORIGIN      
        1 mestltlate qpvkkntlkk ykiacivlla llvimslglg lglglrklek qgscrkkcfd
       61 asfrglencr cdvackdrgd ccwdfedtcv estriwmcnk frcgetrlea slcscsddcl
      121 qrkdccadyk svcqgetswl eencdtaqqs qcpegfdlpp vilfsmdgfr aeylytwdtl
      181 mpninklktc gihskymram yptktfpnhy tivtglypes hgiidnnmyd vnlnknfsls
      241 skeqnnpaww hgqpmwltam yqglkaatyf wpgsevaing sfpsiympyn gsvpfeeris
      301 tllkwldlpk aerprfytmy feepdssgha ggpvsarvik alqvvdhafg mlmeglkqrn
      361 lhncvniill adhgmdqtyc nkmeymtdyf prinffymye gpaprirahn iphdffsfns
      421 eeivrnlscr kpdqhfkpyl tpdlpkrlhy aknvridkvh lfvdqqwlav rsksntncgg
      481 gnhgynnefr smeaiflahg psfkekteve pfenievynl mcdllriqpa pnngthgsln
      541 hllkvpfyep shaeevskfs vcgfanplpt esldcfcphl qnstqleqvn qmlnltqeei
      601 tatvkvnlpf grprvlqknv dhcllyhrey vsgfgkamrm pmwssytvpq lgdtsplppt
      661 vpdclradvr vppsesqkcs fyladknith gflyppasnr tsdsqydali tsnlvpmyee
      721 frkmwdyfhs vllikhater ngvnvvsgpi fdynydghfd apdeitkhla ntdvpipthy
      781 fvvltscknk shtpencpgw ldvlpfiiph rptnvescpe gkpealwvee rftahiarvr
      841 dvelltgldf yqdkvqpvse ilqlktylpt fetti
//
