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Protein

Ectonucleotide pyrophosphatase/phosphodiesterase family member 1

Gene

Enpp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Appears to modulate insulin sensitivity (By similarity). By generating PPi, plays a role in regulating pyrophosphate levels, and functions in bone mineralization and soft tissue calcification. PPi inhibits mineralization by binding to nascent hydroxyapatite (HA) crystals, thereby preventing further growth of these crystals. Preferentially hydrolyzes ATP, but can also hydrolyze other nucleoside 5' triphosphates such as GTP, CTP, TTP and UTP to their corresponding monophosphates with release of pyrophosphate and diadenosine polyphosphates, and also 3',5'-cAMP to AMP. May also be involved in the regulation of the availability of nucleotide sugars in the endoplasmic reticulum and Golgi, and the regulation of purinergic signaling.By similarity2 Publications

Catalytic activityi

Hydrolytically removes 5'-nucleotides successively from the 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides.
A dinucleotide + H2O = 2 mononucleotides.

Cofactori

Zn2+2 PublicationsNote: Binds 2 Zn2+ ions per subunit.2 Publications

Enzyme regulationi

At low concentrations of ATP, a phosphorylated intermediate is formed which inhibits further hydrolysis.

Kineticsi

  1. KM=46 µM for ATP1 Publication
  2. KM=4.3 mM for UTP1 Publication
  3. KM=4.2 mM for GTP1 Publication
  4. KM=1.2 mM for CTP1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei84 – 852Cleavage
Metal bindingi200 – 2001Zinc 1; catalytic1 Publication
Active sitei238 – 2381AMP-threonine intermediate1 Publication
Metal bindingi238 – 2381Zinc 1; catalytic1 Publication
Binding sitei259 – 2591Substrate
Binding sitei277 – 2771Substrate
Binding sitei322 – 3221Substrate
Metal bindingi358 – 3581Zinc 2; catalytic1 Publication
Metal bindingi362 – 3621Zinc 2; via tele nitrogen; catalytic1 Publication
Metal bindingi405 – 4051Zinc 1; catalytic1 Publication
Metal bindingi406 – 4061Zinc 1; via tele nitrogen; catalytic1 Publication
Metal bindingi517 – 5171Zinc 2; via tele nitrogen; catalytic1 Publication
Metal bindingi781 – 7811Calcium1 Publication
Metal bindingi783 – 7831Calcium1 Publication
Metal bindingi785 – 7851Calcium1 Publication
Metal bindingi787 – 7871Calcium; via carbonyl oxygen1 Publication
Metal bindingi789 – 7891Calcium1 Publication
Sitei896 – 8961Essential for catalytic activityBy similarity

GO - Molecular functioni

  1. ATP binding Source: MGI
  2. calcium ion binding Source: UniProtKB
  3. insulin receptor binding Source: MGI
  4. NADH pyrophosphatase activity Source: UniProtKB-EC
  5. nucleic acid binding Source: InterPro
  6. nucleoside-triphosphate diphosphatase activity Source: MGI
  7. nucleotide diphosphatase activity Source: UniProtKB
  8. phosphodiesterase I activity Source: UniProtKB
  9. polysaccharide binding Source: InterPro
  10. protein homodimerization activity Source: MGI
  11. scavenger receptor activity Source: InterPro
  12. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. 3'-phosphoadenosine 5'-phosphosulfate metabolic process Source: MGI
  2. biomineral tissue development Source: UniProtKB-KW
  3. bone remodeling Source: MGI
  4. cellular phosphate ion homeostasis Source: MGI
  5. cellular response to insulin stimulus Source: MGI
  6. generation of precursor metabolites and energy Source: MGI
  7. immune response Source: InterPro
  8. inorganic diphosphate transport Source: MGI
  9. negative regulation of cell growth Source: MGI
  10. negative regulation of fat cell differentiation Source: BHF-UCL
  11. negative regulation of glucose import Source: MGI
  12. negative regulation of glycogen biosynthetic process Source: MGI
  13. negative regulation of insulin receptor signaling pathway Source: MGI
  14. negative regulation of ossification Source: MGI
  15. negative regulation of protein autophosphorylation Source: MGI
  16. nucleic acid phosphodiester bond hydrolysis Source: GOC
  17. nucleoside triphosphate catabolic process Source: MGI
  18. phosphate-containing compound metabolic process Source: MGI
  19. sequestering of triglyceride Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Biomineralization

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.1.4.1. 3474.
3.6.1.9. 3474.
ReactomeiREACT_324263. Vitamin B2 (riboflavin) metabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
Short name:
E-NPP 1
Alternative name(s):
Lymphocyte antigen 41
Short name:
Ly-41
Phosphodiesterase I/nucleotide pyrophosphatase 1
Plasma-cell membrane glycoprotein PC-1
Including the following 2 domains:
Alkaline phosphodiesterase I (EC:3.1.4.1)
Nucleotide pyrophosphatase (EC:3.6.1.9)
Short name:
NPPase
Gene namesi
Name:Enpp1
Synonyms:Npps, Pc1, Pdnp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:97370. Enpp1.

Subcellular locationi

  1. Cell membrane; Single-pass type II membrane protein
  2. Basolateral cell membrane; Single-pass type II membrane protein
  3. Secreted

  4. Note: Targeted to the basolateral membrane in polarized epithelial cells and in hepatocytes, and to matrix vesicles in osteoblasts. In bile duct cells and cancer cells, located to the apical cytoplasmic side (By similarity). The proteolytically processed form is secreted.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5858CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei59 – 7921Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini80 – 906827ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. basolateral plasma membrane Source: UniProtKB-SubCell
  2. cell surface Source: BHF-UCL
  3. extracellular space Source: BHF-UCL
  4. integral component of membrane Source: UniProtKB
  5. integral component of plasma membrane Source: UniProtKB
  6. lysosomal membrane Source: MGI
  7. plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Involvement in diseasei

Defects in Enpp1 are the cause of the tiptoe walking (ttw) phenotype. Ttw mice exhibit ossification of the spinal ligaments.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi28 – 281A → G: No effect on basolateral sorting in epithelial cells. 1 Publication
Mutagenesisi30 – 301S → A or D: Little change in baolateral sorting in epithelial cells. 1 Publication
Mutagenesisi31 – 311L → A: 60% of ENPP1 redirected to apical surface in epithelial cells. 75% of ENPP1 redirected to apical surface in epithelial cells; abrogation of increased NPP activity in oestoblastic matrix vesicles; when associated with A-32. 2 Publications
Mutagenesisi32 – 321L → A: 70% of ENPP1 redirected to apical surface in epithelial cells; abrogation of increased NPP activity in oestoblastic matrix vesicles. 75% of ENPP1 redirected to apical surface in epithelial cells; abrogation of increased NPP activity in oestoblastic matrix vesicles; when associated with A-31. 2 Publications
Mutagenesisi42 – 421L → A: No change in increased NPP activity in oestoblastic matrix vesicles. 1 Publication
Mutagenesisi57 – 571Y → G: No change in increased NPP activity in oestoblastic matrix vesicles. 1 Publication
Mutagenesisi200 – 2001D → N: Decreases phosphodiesterase activity by 95%. Abolishes formation of nucleotidylated intermediate. 1 Publication
Mutagenesisi237 – 2371K → A: Decreases phosphodiesterase activity by 40%. Decreased formation of nucleotidylated intermediate. 1 Publication
Mutagenesisi238 – 2381T → A: Abolishes all phosphodiesterase activity. Abolishes formation of nucleotidylated intermediate. 1 Publication
Mutagenesisi238 – 2381T → S: Decreases phosphodiesterase activity by 95%. Accumulates nucleotidylated intermediate. 1 Publication
Mutagenesisi239 – 2391F → A: Decreases phosphodiesterase activity by 50%. Decreased formation of nucleotidylated intermediate. 2 Publications
Mutagenesisi242 – 2421H → L: Strongly decreased phosphodiesterase activity. 1 Publication
Mutagenesisi304 – 32320Missing : Nearly abolishes activity with nucleotide phosphates. Confers very low activity with lysophospholipids. 1 PublicationAdd
BLAST
Mutagenesisi308 – 3081D → A: Decreased phosphodiesterase activity. 1 Publication
Mutagenesisi322 – 3221Y → A: Strongly decreased phosphodiesterase activity. 1 Publication
Mutagenesisi358 – 3581D → Q: Decreases phosphodiesterase activity by 90%. Accumulates nucleotidylated intermediate. 1 Publication
Mutagenesisi362 – 3621H → Q: Decreases phosphodiesterase activity by 95%. 65% activity can be restored by addition of Zn(2+) ions. Accumulates nucleotidylated intermediate. 1 Publication
Mutagenesisi405 – 4051D → N: Abolishes all phosphodiesterase activity. 10% activity can be restored by addition of Zn(2+) ions. Abolishes formation of nucleotidylated intermediate. 1 Publication
Mutagenesisi406 – 4061H → Q: Abolishes all phosphodiesterase activity. 15% activity can be restored by addition of Zn(2+) ions. Abolishes formation of nucleotidylated intermediate. 1 Publication
Mutagenesisi517 – 5171H → Q: Abolishes all phosphodiesterase activity. 60% activity can be restored by addition of Zn(2+) ions. Abolishes formation of nucleotidylated intermediate. 1 Publication

Keywords - Diseasei

Disease mutation

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 906906Ectonucleotide pyrophosphatase/phosphodiesterase family member 1PRO_0000188565Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi90 ↔ 104PROSITE-ProRule annotation
Disulfide bondi94 ↔ 122PROSITE-ProRule annotation
Disulfide bondi102 ↔ 115PROSITE-ProRule annotation
Disulfide bondi108 ↔ 114PROSITE-ProRule annotation
Disulfide bondi131 ↔ 148PROSITE-ProRule annotation
Disulfide bondi136 ↔ 166PROSITE-ProRule annotation
Disulfide bondi146 ↔ 159PROSITE-ProRule annotation
Disulfide bondi152 ↔ 158PROSITE-ProRule annotation
Glycosylationi161 – 1611N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi177 ↔ 223
Disulfide bondi185 ↔ 397
Glycosylationi267 – 2671N-linked (GlcNAc...)2 Publications
Glycosylationi323 – 3231N-linked (GlcNAc...)3 Publications
Disulfide bondi413 ↔ 512
Glycosylationi459 – 4591N-linked (GlcNAc...)1 Publication
Disulfide bondi462 ↔ 849
Glycosylationi567 – 5671N-linked (GlcNAc...)2 Publications
Disulfide bondi596 ↔ 653
Disulfide bondi607 ↔ 707
Disulfide bondi609 ↔ 692
Glycosylationi624 – 6241N-linked (GlcNAc...)2 Publications
Disulfide bondi819 ↔ 829

Post-translational modificationi

The N-terminal is blocked.
N-glycosylated.5 Publications
A secreted form is produced through cleavage at Lys-85 by intracellular processing.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP06802.
PaxDbiP06802.
PRIDEiP06802.

PTM databases

PhosphoSiteiP06802.

Expressioni

Tissue specificityi

Selectively expressed on the surface of antibody-secreting cells.

Gene expression databases

BgeeiP06802.
ExpressionAtlasiP06802. baseline and differential.
GenevestigatoriP06802.

Interactioni

Subunit structurei

Homodimer. The secreted form is monomeric. Interacts with INSR (By similarity).By similarity

Protein-protein interaction databases

DIPiDIP-59981N.

Structurei

Secondary structure

1
906
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni94 – 963Combined sources
Beta strandi100 – 1034Combined sources
Helixi108 – 1114Combined sources
Helixi118 – 1225Combined sources
Helixi124 – 1263Combined sources
Turni133 – 1375Combined sources
Beta strandi145 – 1473Combined sources
Helixi152 – 1554Combined sources
Helixi162 – 1676Combined sources
Turni172 – 1743Combined sources
Beta strandi194 – 1996Combined sources
Helixi204 – 2107Combined sources
Helixi211 – 2133Combined sources
Helixi215 – 2228Combined sources
Beta strandi224 – 2285Combined sources
Helixi238 – 24710Combined sources
Helixi251 – 2544Combined sources
Beta strandi259 – 2635Combined sources
Turni264 – 2674Combined sources
Beta strandi268 – 2703Combined sources
Beta strandi272 – 2743Combined sources
Helixi275 – 2784Combined sources
Turni280 – 2823Combined sources
Helixi288 – 2947Combined sources
Beta strandi299 – 3035Combined sources
Beta strandi307 – 3093Combined sources
Beta strandi311 – 3133Combined sources
Beta strandi317 – 3193Combined sources
Helixi328 – 33811Combined sources
Turni343 – 3453Combined sources
Beta strandi348 – 3547Combined sources
Helixi358 – 3647Combined sources
Beta strandi366 – 3683Combined sources
Helixi369 – 39123Combined sources
Beta strandi399 – 4035Combined sources
Beta strandi413 – 4186Combined sources
Helixi420 – 4234Combined sources
Beta strandi428 – 4325Combined sources
Beta strandi434 – 4363Combined sources
Beta strandi438 – 4436Combined sources
Turni444 – 4463Combined sources
Beta strandi449 – 4513Combined sources
Helixi453 – 4608Combined sources
Beta strandi468 – 4736Combined sources
Helixi474 – 4763Combined sources
Helixi479 – 4813Combined sources
Beta strandi487 – 4893Combined sources
Beta strandi491 – 4966Combined sources
Beta strandi501 – 5055Combined sources
Turni506 – 5083Combined sources
Beta strandi514 – 5163Combined sources
Helixi524 – 5263Combined sources
Beta strandi528 – 53710Combined sources
Beta strandi539 – 5435Combined sources
Helixi548 – 5503Combined sources
Helixi551 – 5599Combined sources
Turni570 – 5734Combined sources
Helixi574 – 5763Combined sources
Beta strandi577 – 5793Combined sources
Beta strandi591 – 5944Combined sources
Beta strandi611 – 6133Combined sources
Helixi617 – 6248Combined sources
Turni630 – 6323Combined sources
Helixi633 – 6375Combined sources
Beta strandi652 – 6565Combined sources
Beta strandi658 – 6658Combined sources
Turni666 – 6694Combined sources
Beta strandi670 – 6789Combined sources
Turni703 – 7053Combined sources
Helixi707 – 7093Combined sources
Beta strandi717 – 7226Combined sources
Turni728 – 7314Combined sources
Helixi736 – 7383Combined sources
Helixi740 – 7423Combined sources
Beta strandi743 – 7464Combined sources
Helixi748 – 75912Combined sources
Helixi761 – 7688Combined sources
Beta strandi771 – 7799Combined sources
Beta strandi785 – 7873Combined sources
Helixi791 – 7966Combined sources
Beta strandi799 – 8013Combined sources
Beta strandi804 – 8063Combined sources
Beta strandi810 – 82112Combined sources
Helixi826 – 8283Combined sources
Beta strandi830 – 84011Combined sources
Turni846 – 8494Combined sources
Helixi855 – 86511Combined sources
Helixi870 – 8778Combined sources
Helixi889 – 8968Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4B56X-ray3.00A/B87-906[»]
4GTWX-ray2.70A/B92-906[»]
4GTXX-ray3.20A/B92-906[»]
4GTYX-ray3.19A/B92-906[»]
4GTZX-ray3.19A/B92-906[»]
ProteinModelPortaliP06802.
SMRiP06802. Positions 88-903.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini86 – 12641SMB 1PROSITE-ProRule annotationAdd
BLAST
Domaini127 – 17145SMB 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni173 – 573401PhosphodiesteraseAdd
BLAST
Regioni579 – 62850LinkerAdd
BLAST
Regioni635 – 906272NucleaseAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi27 – 348Di-leucine motif

Domaini

The di-leucine motif is required for basolateral targeting in polarized epithelial cells, and for targeting to matrix vesicles derived from mineralizing cells.

Sequence similaritiesi

Contains 2 SMB (somatomedin-B) domains.Curated

Keywords - Domaini

Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1524.
HOGENOMiHOG000034646.
HOVERGENiHBG051484.
InParanoidiP06802.
KOiK01513.
PhylomeDBiP06802.

Family and domain databases

Gene3Di3.40.570.10. 1 hit.
3.40.720.10. 1 hit.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR001604. DNA/RNA_non-sp_Endonuclease.
IPR024873. E-NPP.
IPR029890. ENPP1.
IPR020821. Extracellular_endonuc_su_A.
IPR002591. Phosphodiest/P_Trfase.
IPR020436. Somatomedin_B_chordata.
IPR001212. Somatomedin_B_dom.
[Graphical view]
PANTHERiPTHR10151. PTHR10151. 1 hit.
PTHR10151:SF64. PTHR10151:SF64. 1 hit.
PfamiPF01223. Endonuclease_NS. 1 hit.
PF01663. Phosphodiest. 1 hit.
PF01033. Somatomedin_B. 2 hits.
[Graphical view]
PRINTSiPR00022. SOMATOMEDINB.
SMARTiSM00892. Endonuclease_NS. 1 hit.
SM00477. NUC. 1 hit.
SM00201. SO. 2 hits.
[Graphical view]
SUPFAMiSSF53649. SSF53649. 1 hit.
PROSITEiPS00524. SMB_1. 2 hits.
PS50958. SMB_2. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 2 (identifier: P06802-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MERDGDQAGH GPRHGSAGNG RELESPAAAS LLAPMDLGEE PLEKAERARP
60 70 80 90 100
AKDPNTYKVL SLVLSVCVLT TILGCIFGLK PSCAKEVKSC KGRCFERTFS
110 120 130 140 150
NCRCDAACVS LGNCCLDFQE TCVEPTHIWT CNKFRCGEKR LSRFVCSCAD
160 170 180 190 200
DCKTHNDCCI NYSSVCQDKK SWVEETCESI DTPECPAEFE SPPTLLFSLD
210 220 230 240 250
GFRAEYLHTW GGLLPVISKL KNCGTYTKNM RPMYPTKTFP NHYSIVTGLY
260 270 280 290 300
PESHGIIDNK MYDPKMNASF SLKSKEKFNP LWYKGQPIWV TANHQEVKSG
310 320 330 340 350
TYFWPGSDVE IDGILPDIYK VYNGSVPFEE RILAVLEWLQ LPSHERPHFY
360 370 380 390 400
TLYLEEPDSS GHSHGPVSSE VIKALQKVDR LVGMLMDGLK DLGLDKCLNL
410 420 430 440 450
ILISDHGMEQ GSCKKYVYLN KYLGDVNNVK VVYGPAARLR PTDVPETYYS
460 470 480 490 500
FNYEALAKNL SCREPNQHFR PYLKPFLPKR LHFAKSDRIE PLTFYLDPQW
510 520 530 540 550
QLALNPSERK YCGSGFHGSD NLFSNMQALF IGYGPAFKHG AEVDSFENIE
560 570 580 590 600
VYNLMCDLLG LIPAPNNGSH GSLNHLLKKP IYNPSHPKEE GFLSQCPIKS
610 620 630 640 650
TSNDLGCTCD PWIVPIKDFE KQLNLTTEDV DDIYHMTVPY GRPRILLKQH
660 670 680 690 700
HVCLLQQQQF LTGYSLDLLM PLWASYTFLR NDQFSRDDFS NCLYQDLRIP
710 720 730 740 750
LSPVHKCSYY KSNSKLSYGF LTPPRLNRVS NHIYSEALLT SNIVPMYQSF
760 770 780 790 800
QVIWHYLHDT LLQRYAHERN GINVVSGPVF DFDYDGRYDS LEILKQNSRV
810 820 830 840 850
IRSQEILIPT HFFIVLTSCK QLSETPLECS ALESSAYILP HRPDNIESCT
860 870 880 890 900
HGKRESSWVE ELLTLHRARV TDVELITGLS FYQDRQESVS ELLRLKTHLP

IFSQED
Length:906
Mass (Da):103,176
Last modified:September 19, 2002 - v4
Checksum:i068D45B0ED0F224D
GO
Isoform 1 (identifier: P06802-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     630-630: Missing.

Show »
Length:905
Mass (Da):103,076
Checksum:iFB6EEEA0FF659421
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti651 – 6511H → R in allele ENPP1b. 1 Publication
Natural varianti680 – 6801R → S in allele ENPP1b. 1 Publication

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei630 – 6301Missing in isoform 1. 2 PublicationsVSP_006748

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02700 mRNA. Translation: AAA39893.2.
AF339910 mRNA. Translation: AAK84174.1.
AK088857 mRNA. Translation: BAC40616.1.
L04516 Unassigned DNA. No translation available.
M12552 mRNA. Translation: AAA39892.1.
CCDSiCCDS35870.1. [P06802-2]
PIRiA27410.
RefSeqiXP_006512660.1. XM_006512597.2.
UniGeneiMm.27254.
Mm.478860.

Genome annotation databases

GeneIDi18605.
KEGGimmu:18605.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02700 mRNA. Translation: AAA39893.2.
AF339910 mRNA. Translation: AAK84174.1.
AK088857 mRNA. Translation: BAC40616.1.
L04516 Unassigned DNA. No translation available.
M12552 mRNA. Translation: AAA39892.1.
CCDSiCCDS35870.1. [P06802-2]
PIRiA27410.
RefSeqiXP_006512660.1. XM_006512597.2.
UniGeneiMm.27254.
Mm.478860.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4B56X-ray3.00A/B87-906[»]
4GTWX-ray2.70A/B92-906[»]
4GTXX-ray3.20A/B92-906[»]
4GTYX-ray3.19A/B92-906[»]
4GTZX-ray3.19A/B92-906[»]
ProteinModelPortaliP06802.
SMRiP06802. Positions 88-903.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59981N.

PTM databases

PhosphoSiteiP06802.

Proteomic databases

MaxQBiP06802.
PaxDbiP06802.
PRIDEiP06802.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi18605.
KEGGimmu:18605.

Organism-specific databases

CTDi5167.
MGIiMGI:97370. Enpp1.

Phylogenomic databases

eggNOGiCOG1524.
HOGENOMiHOG000034646.
HOVERGENiHBG051484.
InParanoidiP06802.
KOiK01513.
PhylomeDBiP06802.

Enzyme and pathway databases

BRENDAi3.1.4.1. 3474.
3.6.1.9. 3474.
ReactomeiREACT_324263. Vitamin B2 (riboflavin) metabolism.

Miscellaneous databases

PROiP06802.
SOURCEiSearch...

Gene expression databases

BgeeiP06802.
ExpressionAtlasiP06802. baseline and differential.
GenevestigatoriP06802.

Family and domain databases

Gene3Di3.40.570.10. 1 hit.
3.40.720.10. 1 hit.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR001604. DNA/RNA_non-sp_Endonuclease.
IPR024873. E-NPP.
IPR029890. ENPP1.
IPR020821. Extracellular_endonuc_su_A.
IPR002591. Phosphodiest/P_Trfase.
IPR020436. Somatomedin_B_chordata.
IPR001212. Somatomedin_B_dom.
[Graphical view]
PANTHERiPTHR10151. PTHR10151. 1 hit.
PTHR10151:SF64. PTHR10151:SF64. 1 hit.
PfamiPF01223. Endonuclease_NS. 1 hit.
PF01663. Phosphodiest. 1 hit.
PF01033. Somatomedin_B. 2 hits.
[Graphical view]
PRINTSiPR00022. SOMATOMEDINB.
SMARTiSM00892. Endonuclease_NS. 1 hit.
SM00477. NUC. 1 hit.
SM00201. SO. 2 hits.
[Graphical view]
SUPFAMiSSF53649. SSF53649. 1 hit.
PROSITEiPS00524. SMB_1. 2 hits.
PS50958. SMB_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Plasma cell membrane glycoprotein PC-1. Primary structure deduced from cDNA clones."
    van Driel I.R., Goding J.W.
    J. Biol. Chem. 262:4882-4887(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT.
    Strain: BALB/c.
  2. Goding J.W.
    Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 24; 46-47; 642 AND 693.
  3. "Identification of nucleotide pyrophosphatase/alkaline phosphodiesterase I activity associated with the mouse plasma cell differentiation antigen PC-1."
    Rebbe N.F., Tong B.D., Finley E.M., Hickman S.
    Proc. Natl. Acad. Sci. U.S.A. 88:5192-5196(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], GLYCOSYLATION, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
    Strain: BALB/c.
    Tissue: Plasmacytoma.
  4. "Structural basis of allotypes of ecto-nucleotide pyrophosphatase/phosphodiesterase (plasma cell membrane glycoprotein PC-1) in the mouse and rat, and analysis of allele-specific xenogeneic antibodies."
    Banakh I., Sali A., Dubljevic V., Grobben B., Slegers H., Goding J.W.
    Eur. J. Immunogenet. 29:307-313(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANTS ARG-651 AND SER-680, ALTERNATIVE SPLICING.
  5. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: NOD.
    Tissue: Thymus.
  6. "Identification and characterization of a soluble form of the plasma cell membrane glycoprotein PC-1 (5'-nucleotide phosphodiesterase)."
    Belli S.I., van Driel I.R., Goding J.W.
    Eur. J. Biochem. 217:421-428(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 168-188, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, GLYCOSYLATION.
  7. "Murine plasma cell membrane antigen PC-1: molecular cloning of cDNA and analysis of expression."
    van Driel I.R., Wilks A.F., Pietersz G.A., Goding J.W.
    Proc. Natl. Acad. Sci. U.S.A. 82:8619-8623(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 203-219.
  8. "The murine plasma cell antigen PC-1: purification and partial amino acid sequence."
    Stearne P.A., van Driel I.R., Grego B., Simpson R.J., Goding J.W.
    J. Immunol. 134:443-448(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 204-219; 332-351; 486-509; 716-725; 803-818 AND 855-867, SUBCELLULAR LOCATION.
  9. "Plasma cell membrane glycoprotein PC-1. cDNA cloning of the human molecule, amino acid sequence, and chromosomal location."
    Buckley M.F., Loveland K.A., McKinstry W.J., Garson O.M., Goding J.W.
    J. Biol. Chem. 265:17506-17511(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF POSSIBLE INITIATION SITE.
  10. "Mutation in Npps in a mouse model of ossification of the posterior longitudinal ligament of the spine."
    Okawa A., Nakamura I., Goto S., Moriya H., Nakamura Y., Ikegawa S.
    Nat. Genet. 19:271-273(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISEASE, FUNCTION.
  11. "Structural and catalytic similarities between nucleotide pyrophosphatases/phosphodiesterases and alkaline phosphatases."
    Gijsbers R., Ceulemans H., Stalmans W., Bollen M.
    J. Biol. Chem. 276:1361-1368(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITE, METAL-BINDING, MUTAGENESIS OF ASP-200; LYS-237; THR-238; PHE-239; ASP-358; HIS-362; ASP-405; HIS-406 AND HIS-517, CATALYTIC ACTIVITY.
  12. "Characterization of a di-leucine-based signal in the cytoplasmic tail of the nucleotide-pyrophosphatase NPP1 that mediates basolateral targeting but not endocytosis."
    Bello V., Goding J.W., Greengrass V., Sali A., Dubljevic V., Lenoir C., Trugnan G., Maurice M.
    Mol. Biol. Cell 12:3004-3015(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: DI-LEUCINE MOTIF, MUTAGENESIS OF ALA-28; SER-30; LEU-31 AND LEU-32, SUBCELLULAR LOCATION.
  13. "Subcellular targeting and function of osteoblast nucleotide pyrophosphatase phosphodiesterase 1."
    Vaingankar S.M., Fitzpatrick T.A., Johnson K., Goding J.W., Maurice M., Terkeltaub R.
    Am. J. Physiol. 286:C1177-C1187(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DI-LEUCINE MOTIF, MUTAGENESIS OF LEU-31; LEU-32; LEU-42 AND TYR-57, SUBCELLULAR LOCATION.
  14. "The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation."
    Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.
    Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-267; ASN-323 AND ASN-624.
    Tissue: Myoblast.
  15. "Crystal structure of Enpp1, an extracellular glycoprotein involved in bone mineralization and insulin signaling."
    Kato K., Nishimasu H., Okudaira S., Mihara E., Ishitani R., Takagi J., Aoki J., Nureki O.
    Proc. Natl. Acad. Sci. U.S.A. 109:16876-16881(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 92-906 IN COMPLEXES WITH AMP; CMP; GMP; TMP; CALCIUM AND ZINC, GLYCOSYLATION AT ASN-267; ASN-323 AND ASN-567, DISULFIDE BOND, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF PHE-239; HIS-242; 304-TRP--ASN-323; ASP-308 AND TYR-322, COFACTOR.
  16. "Structure of NPP1, an ectonucleotide pyrophosphatase/ phosphodiesterase involved in tissue calcification."
    Jansen S., Perrakis A., Ulens C., Winkler C., Andries M., Joosten R.P., Van Acker M., Luyten F.P., Moolenaar W.H., Bollen M.
    Structure 20:1948-1959(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 87-906 IN COMPLEX WITH CALCIUM; PHOSPHATE AND ZINC, DISULFIDE BONDS, METAL-BINDING SITES, SUBUNIT, SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-323; ASN-459; ASN-567 AND ASN-624, COFACTOR.

Entry informationi

Entry nameiENPP1_MOUSE
AccessioniPrimary (citable) accession number: P06802
Secondary accession number(s): Q542E9, Q924C4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: September 19, 2002
Last modified: April 29, 2015
This is version 153 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

It is uncertain whether Met-1 or Met-35 is the initiator.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.