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Ectonucleotide pyrophosphatase/phosphodiesterase family member 3 (E-NPP 3) (Phosphodiesterase I beta) (PD-Ibeta) (Phosphodiesterase I/nucleotide pyrophosphatase 3) (CD antigen CD203c) [Includes: Alkaline phosphodiesterase I (EC 3.1.4.1); Nucleotide pyrophosphatase (NPPase) (EC 3.6.1.9) (Nucleotide diphosphatase)]

 ENPP3_HUMAN             Reviewed;         875 AA.
O14638; Q5JTL3;
19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
23-SEP-2008, sequence version 2.
22-NOV-2017, entry version 157.
RecName: Full=Ectonucleotide pyrophosphatase/phosphodiesterase family member 3;
Short=E-NPP 3;
AltName: Full=Phosphodiesterase I beta;
Short=PD-Ibeta;
AltName: Full=Phosphodiesterase I/nucleotide pyrophosphatase 3;
AltName: CD_antigen=CD203c;
Includes:
RecName: Full=Alkaline phosphodiesterase I;
EC=3.1.4.1 {ECO:0000250|UniProtKB:P06802};
Includes:
RecName: Full=Nucleotide pyrophosphatase;
Short=NPPase;
EC=3.6.1.9 {ECO:0000250|UniProtKB:P06802};
AltName: Full=Nucleotide diphosphatase {ECO:0000305};
Name=ENPP3; Synonyms=PDNP3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Prostate;
PubMed=9344668; DOI=10.1006/geno.1997.4949;
Piao J.-H., Goding J.W., Nakamura H., Sano K.;
"Molecular cloning and chromosomal localization of PD-Ibeta (PDNP3), a
new member of the human phosphodiesterase I genes.";
Genomics 45:412-415(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Endometrium;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
PROTEIN SEQUENCE OF 393-405, IDENTIFICATION AS CD203C, AND SUBCELLULAR
LOCATION.
PubMed=11342463; DOI=10.1182/blood.V97.10.3303;
Buehring H.J., Seiffert M., Giesert C., Marxer A., Kanz L., Valent P.,
Sano K.;
"The basophil activation marker defined by antibody 97A6 is identical
to the ectonucleotide pyrophosphatase/phosphodiesterase 3.";
Blood 97:3303-3305(2001).
[6]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=15072822; DOI=10.1016/j.canlet.2003.11.002;
Yano Y., Hayashi Y., Sano K., Nagano H., Nakaji M., Seo Y.,
Ninomiya T., Yoon S., Yokozaki H., Kasuga M.;
"Expression and localization of ecto-nucleotide
pyrophosphatase/phosphodiesterase I-1 (E-NPP1/PC-1) and -3 (E-
NPP3/CD203c/PD-Ibeta/B10/gp130(RB13-6)) in inflammatory and neoplastic
bile duct diseases.";
Cancer Lett. 207:139-147(2004).
[7]
INDUCTION, AND POSSIBLE APPLICATION IN ALLERGY DIAGNOSIS.
PubMed=15031605; DOI=10.1159/000077351;
Buehring H.J., Streble A., Valent P.;
"The basophil-specific ectoenzyme E-NPP3 (CD203c) as a marker for cell
activation and allergy diagnosis.";
Int. Arch. Allergy Immunol. 133:317-329(2004).
-!- FUNCTION: Cleaves a variety of phosphodiester and phosphosulfate
bonds including deoxynucleotides, nucleotide sugars, and NAD.
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: Hydrolytically removes 5'-nucleotides
successively from the 3'-hydroxy termini of 3'-hydroxy-terminated
oligonucleotides. {ECO:0000250|UniProtKB:P06802}.
-!- CATALYTIC ACTIVITY: A nucleoside triphosphate + H(2)O = a
nucleotide + diphosphate. {ECO:0000250|UniProtKB:P06802}.
-!- COFACTOR:
Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
Evidence={ECO:0000305};
Note=Binds 2 divalent metal cations per subunit. {ECO:0000305};
-!- ENZYME REGULATION: At low concentrations of ATP, a phosphorylated
active site intermediate is formed which inhibits further ATP
hydrolysis.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
membrane protein {ECO:0000305}. Secreted
{ECO:0000269|PubMed:11342463, ECO:0000269|PubMed:15072822}.
Note=Located to the apical surface in intestinal and kidney
epithelial cells. Located to the cell surface of basophils, and to
the apical plasma membrane of bile duct cells. Secreted in serum,
and in lumen of epithelial cells.
-!- TISSUE SPECIFICITY: Expressed in bile ducts, prostate, uterus and
colon. Exclusively expressed on basophils, mast cells and their
progenitors. {ECO:0000269|PubMed:15072822,
ECO:0000269|PubMed:9344668}.
-!- INDUCTION: Up-regulated by stimulation by allergen or by cross-
linking with IgE. The IgE-mediated activation is enhanced by
tetradecanoyl phorbol acetate (TPA), a stimulator of the PKC
pathway, and inhibited by the P13 kinase inhibitors, LY294002 and
wortmannin. Up-regulated in invasive bile duct cancers.
{ECO:0000269|PubMed:15031605}.
-!- PTM: N-glycosylation is necessary for correct trafficking to the
apical surface, but is not the apical targeting signal.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the nucleotide
pyrophosphatase/phosphodiesterase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD05192.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF005632; AAC51813.1; -; mRNA.
EMBL; EF560735; ABQ59045.1; -; mRNA.
EMBL; AC005587; AAD05192.1; ALT_SEQ; Genomic_DNA.
EMBL; AL121575; CAI23322.1; -; Genomic_DNA.
EMBL; AC005587; CAI23322.1; JOINED; Genomic_DNA.
EMBL; AL355150; CAI23322.1; JOINED; Genomic_DNA.
EMBL; AL355150; CAI40481.1; -; Genomic_DNA.
EMBL; AC005587; CAI40481.1; JOINED; Genomic_DNA.
EMBL; AL121575; CAI40481.1; JOINED; Genomic_DNA.
EMBL; CH471051; EAW48045.1; -; Genomic_DNA.
CCDS; CCDS5148.1; -.
RefSeq; NP_005012.2; NM_005021.4.
UniGene; Hs.486489; -.
ProteinModelPortal; O14638; -.
SMR; O14638; -.
BioGrid; 111195; 1.
IntAct; O14638; 1.
MINT; MINT-6610326; -.
STRING; 9606.ENSP00000350265; -.
BindingDB; O14638; -.
ChEMBL; CHEMBL5580; -.
iPTMnet; O14638; -.
PhosphoSitePlus; O14638; -.
BioMuta; ENPP3; -.
MaxQB; O14638; -.
PaxDb; O14638; -.
PeptideAtlas; O14638; -.
PRIDE; O14638; -.
DNASU; 5169; -.
Ensembl; ENST00000357639; ENSP00000350265; ENSG00000154269.
Ensembl; ENST00000414305; ENSP00000406261; ENSG00000154269.
GeneID; 5169; -.
KEGG; hsa:5169; -.
UCSC; uc003qcu.5; human.
CTD; 5169; -.
DisGeNET; 5169; -.
EuPathDB; HostDB:ENSG00000154269.14; -.
GeneCards; ENPP3; -.
HGNC; HGNC:3358; ENPP3.
HPA; HPA043772; -.
MIM; 602182; gene.
neXtProt; NX_O14638; -.
OpenTargets; ENSG00000154269; -.
PharmGKB; PA27793; -.
eggNOG; KOG2645; Eukaryota.
eggNOG; COG1524; LUCA.
GeneTree; ENSGT00760000119157; -.
HOGENOM; HOG000037439; -.
HOVERGEN; HBG051484; -.
InParanoid; O14638; -.
KO; K01513; -.
OMA; WDYFHSV; -.
OrthoDB; EOG091G017X; -.
PhylomeDB; O14638; -.
TreeFam; TF330032; -.
BRENDA; 3.6.1.9; 2681.
Reactome; R-HSA-199220; Vitamin B5 (pantothenate) metabolism.
ChiTaRS; ENPP3; human.
GeneWiki; ENPP3; -.
GenomeRNAi; 5169; -.
PRO; PR:O14638; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000154269; -.
CleanEx; HS_ENPP3; -.
ExpressionAtlas; O14638; baseline and differential.
Genevisible; O14638; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0035529; F:NADH pyrophosphatase activity; IEA:UniProtKB-EC.
GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IDA:BHF-UCL.
GO; GO:0004551; F:nucleotide diphosphatase activity; TAS:ProtInc.
GO; GO:0004528; F:phosphodiesterase I activity; TAS:ProtInc.
GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
GO; GO:0006955; P:immune response; IEA:InterPro.
GO; GO:0009143; P:nucleoside triphosphate catabolic process; IDA:BHF-UCL.
GO; GO:0006796; P:phosphate-containing compound metabolic process; IDA:BHF-UCL.
Gene3D; 3.40.720.10; -; 1.
InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
InterPro; IPR017850; Alkaline_phosphatase_core_sf.
InterPro; IPR001604; DNA/RNA_non-sp_Endonuclease.
InterPro; IPR020821; Extracellular_endonuc_su_A.
InterPro; IPR002591; Phosphodiest/P_Trfase.
InterPro; IPR036024; Somatomedin_B-like_dom_sf.
InterPro; IPR001212; Somatomedin_B_dom.
Pfam; PF01223; Endonuclease_NS; 1.
Pfam; PF01663; Phosphodiest; 1.
Pfam; PF01033; Somatomedin_B; 2.
SMART; SM00892; Endonuclease_NS; 1.
SMART; SM00477; NUC; 1.
SMART; SM00201; SO; 2.
SUPFAM; SSF53649; SSF53649; 1.
SUPFAM; SSF90188; SSF90188; 2.
PROSITE; PS00524; SMB_1; 2.
PROSITE; PS50958; SMB_2; 2.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Hydrolase; Membrane; Metal-binding; Polymorphism;
Reference proteome; Repeat; Secreted; Signal-anchor; Transmembrane;
Transmembrane helix; Zinc.
CHAIN 1 875 Ectonucleotide
pyrophosphatase/phosphodiesterase family
member 3.
/FTId=PRO_0000188570.
TOPO_DOM 1 11 Cytoplasmic. {ECO:0000255}.
TRANSMEM 12 30 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 31 875 Extracellular. {ECO:0000255}.
DOMAIN 50 93 SMB 1. {ECO:0000255|PROSITE-
ProRule:PRU00350}.
DOMAIN 94 138 SMB 2. {ECO:0000255|PROSITE-
ProRule:PRU00350}.
REGION 140 510 Phosphodiesterase.
REGION 605 875 Nuclease.
MOTIF 78 80 Cell attachment site. {ECO:0000255}.
ACT_SITE 205 205 AMP-threonine intermediate.
{ECO:0000250}.
METAL 167 167 Zinc 1; catalytic. {ECO:0000250}.
METAL 205 205 Zinc 1; catalytic. {ECO:0000250}.
METAL 325 325 Zinc 2; catalytic. {ECO:0000250}.
METAL 329 329 Zinc 2; via tele nitrogen; catalytic.
{ECO:0000250}.
METAL 372 372 Zinc 1; catalytic. {ECO:0000250}.
METAL 373 373 Zinc 1; via tele nitrogen; catalytic.
{ECO:0000250}.
METAL 483 483 Zinc 2; via tele nitrogen; catalytic.
{ECO:0000250}.
BINDING 226 226 Substrate. {ECO:0000250}.
BINDING 320 320 Substrate. {ECO:0000250}.
CARBOHYD 236 236 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 279 279 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 290 290 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 426 426 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 533 533 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 582 582 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 594 594 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 687 687 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 699 699 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 789 789 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 54 71 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 58 89 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 69 82 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 75 81 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 98 115 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 103 133 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 113 126 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 119 125 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 144 190 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 152 364 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 380 478 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 429 818 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 575 679 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 577 664 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 787 797 {ECO:0000255|PROSITE-ProRule:PRU00350}.
VARIANT 620 620 V -> M (in dbSNP:rs9321309).
/FTId=VAR_018516.
VARIANT 744 744 N -> H (in dbSNP:rs36094194).
/FTId=VAR_046538.
VARIANT 786 786 S -> N (in dbSNP:rs17601580).
/FTId=VAR_031253.
CONFLICT 122 122 R -> K (in Ref. 1; AAC51813).
{ECO:0000305}.
SEQUENCE 875 AA; 100124 MW; 629D2E33B4C45196 CRC64;
MESTLTLATE QPVKKNTLKK YKIACIVLLA LLVIMSLGLG LGLGLRKLEK QGSCRKKCFD
ASFRGLENCR CDVACKDRGD CCWDFEDTCV ESTRIWMCNK FRCGETRLEA SLCSCSDDCL
QRKDCCADYK SVCQGETSWL EENCDTAQQS QCPEGFDLPP VILFSMDGFR AEYLYTWDTL
MPNINKLKTC GIHSKYMRAM YPTKTFPNHY TIVTGLYPES HGIIDNNMYD VNLNKNFSLS
SKEQNNPAWW HGQPMWLTAM YQGLKAATYF WPGSEVAING SFPSIYMPYN GSVPFEERIS
TLLKWLDLPK AERPRFYTMY FEEPDSSGHA GGPVSARVIK ALQVVDHAFG MLMEGLKQRN
LHNCVNIILL ADHGMDQTYC NKMEYMTDYF PRINFFYMYE GPAPRIRAHN IPHDFFSFNS
EEIVRNLSCR KPDQHFKPYL TPDLPKRLHY AKNVRIDKVH LFVDQQWLAV RSKSNTNCGG
GNHGYNNEFR SMEAIFLAHG PSFKEKTEVE PFENIEVYNL MCDLLRIQPA PNNGTHGSLN
HLLKVPFYEP SHAEEVSKFS VCGFANPLPT ESLDCFCPHL QNSTQLEQVN QMLNLTQEEI
TATVKVNLPF GRPRVLQKNV DHCLLYHREY VSGFGKAMRM PMWSSYTVPQ LGDTSPLPPT
VPDCLRADVR VPPSESQKCS FYLADKNITH GFLYPPASNR TSDSQYDALI TSNLVPMYEE
FRKMWDYFHS VLLIKHATER NGVNVVSGPI FDYNYDGHFD APDEITKHLA NTDVPIPTHY
FVVLTSCKNK SHTPENCPGW LDVLPFIIPH RPTNVESCPE GKPEALWVEE RFTAHIARVR
DVELLTGLDF YQDKVQPVSE ILQLKTYLPT FETTI


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