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P06802 (ENPP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:

  1. Alkaline phosphodiesterase I
    EC=3.1.4.1
  2. Nucleotide pyrophosphatase
    Short name=NPPase
    EC=3.6.1.9
Gene names
Name:Enpp1
Synonyms:Npps, Pc1, Pdnp1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length906 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3 Ref.10

Catalytic activity

Hydrolytically removes 5'-nucleotides successively from the 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides. Ref.3 Ref.6 Ref.11 Ref.15

A dinucleotide + H2O = 2 mononucleotides. Ref.3 Ref.6 Ref.11 Ref.15

Cofactor

Binds 2 zinc ions per subunit. Ref.15 Ref.16

Enzyme regulation

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

Subunit structure

Homodimer. The secreted form is monomeric. Interacts with INSR By similarity. Ref.1 Ref.16

Subcellular location

Cell membrane; Single-pass type II membrane protein. Basolateral cell membrane; Single-pass type II membrane protein. Secreted. 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. Ref.1 Ref.3 Ref.6 Ref.8 Ref.12 Ref.13 Ref.16

Tissue specificity

Selectively expressed on the surface of antibody-secreting cells.

Domain

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

Post-translational modification

The N-terminal is blocked.

N-glycosylated. Ref.3 Ref.6 Ref.15 Ref.16

A secreted form is produced through cleavage at Lys-85 by intracellular processing.

Involvement in disease

Defects in Enpp1 are the cause of the tiptoe walking (ttw) phenotype. Ttw mice exhibit ossification of the spinal ligaments. Ref.10

Sequence similarities

Belongs to the nucleotide pyrophosphatase/phosphodiesterase family.

Contains 2 SMB (somatomedin-B) domains.

Caution

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

Biophysicochemical properties

Kinetic parameters:

KM=46 µM for ATP Ref.15

KM=4.3 mM for UTP

KM=4.2 mM for GTP

KM=1.2 mM for CTP

Ontologies

Keywords
   Biological processBiomineralization
   Cellular componentCell membrane
Membrane
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainRepeat
Signal-anchor
Transmembrane
Transmembrane helix
   LigandCalcium
Metal-binding
Zinc
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay Ref.15. Source: UniProtKB

biomineral tissue development

Inferred from electronic annotation. Source: UniProtKB-KW

bone remodeling

Inferred from mutant phenotype PubMed 10024383. Source: MGI

immune response

Inferred from electronic annotation. Source: InterPro

negative regulation of fat cell differentiation

Inferred from mutant phenotype PubMed 17849011. Source: BHF-UCL

negative regulation of ossification

Inferred from mutant phenotype Ref.10. Source: MGI

nucleic acid phosphodiester bond hydrolysis

Inferred from direct assay Ref.3. Source: GOC

   Cellular_componentbasolateral plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell surface

Inferred from direct assay Ref.6. Source: BHF-UCL

extracellular space

Inferred from direct assay Ref.6. Source: BHF-UCL

integral component of membrane

Inferred from direct assay Ref.3. Source: UniProtKB

integral component of plasma membrane

Inferred from direct assay Ref.1. Source: UniProtKB

plasma membrane

Inferred from sequence orthology PubMed 19474315. Source: MGI

   Molecular_functionNADH pyrophosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

calcium ion binding

Inferred from direct assay Ref.15. Source: UniProtKB

nucleic acid binding

Inferred from electronic annotation. Source: InterPro

nucleotide diphosphatase activity

Inferred from direct assay Ref.15. Source: UniProtKB

phosphodiesterase I activity

Inferred from direct assay Ref.3. Source: UniProtKB

polysaccharide binding

Inferred from electronic annotation. Source: InterPro

scavenger receptor activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from direct assay Ref.15. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 2 (identifier: P06802-1)

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.
Isoform 1 (identifier: P06802-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 906906Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
PRO_0000188565

Regions

Topological domain1 – 5858Cytoplasmic Potential
Transmembrane59 – 7921Helical; Signal-anchor for type II membrane protein; Potential
Topological domain80 – 906827Extracellular Potential
Domain86 – 12641SMB 1
Domain127 – 17145SMB 2
Region173 – 573401Phosphodiesterase
Region579 – 62850Linker
Region635 – 906272Nuclease
Motif27 – 348Di-leucine motif

Sites

Active site2381AMP-threonine intermediate Ref.11
Metal binding2001Zinc 1; catalytic
Metal binding2381Zinc 1; catalytic
Metal binding3581Zinc 2; catalytic
Metal binding3621Zinc 2; via tele nitrogen; catalytic
Metal binding4051Zinc 1; catalytic
Metal binding4061Zinc 1; via tele nitrogen; catalytic
Metal binding5171Zinc 2; via tele nitrogen; catalytic
Metal binding7811Calcium
Metal binding7831Calcium
Metal binding7851Calcium
Metal binding7871Calcium; via carbonyl oxygen
Metal binding7891Calcium
Binding site2591Substrate
Binding site2771Substrate
Binding site3221Substrate
Site84 – 852Cleavage
Site8961Essential for catalytic activity By similarity

Amino acid modifications

Glycosylation1611N-linked (GlcNAc...) Potential
Glycosylation2671N-linked (GlcNAc...) Ref.14 Ref.15
Glycosylation3231N-linked (GlcNAc...) Ref.14 Ref.15 Ref.16
Glycosylation4591N-linked (GlcNAc...) Ref.16
Glycosylation5671N-linked (GlcNAc...) Ref.15 Ref.16
Glycosylation6241N-linked (GlcNAc...) Ref.14 Ref.16
Disulfide bond90 ↔ 104 By similarity
Disulfide bond94 ↔ 122 By similarity
Disulfide bond102 ↔ 115 By similarity
Disulfide bond108 ↔ 114 By similarity
Disulfide bond131 ↔ 148 By similarity
Disulfide bond136 ↔ 166 By similarity
Disulfide bond146 ↔ 159 By similarity
Disulfide bond152 ↔ 158 By similarity
Disulfide bond177 ↔ 223 Ref.15 Ref.16
Disulfide bond185 ↔ 397 Ref.15 Ref.16
Disulfide bond413 ↔ 512 Ref.15 Ref.16
Disulfide bond462 ↔ 849 Ref.15 Ref.16
Disulfide bond596 ↔ 653 Ref.15 Ref.16
Disulfide bond607 ↔ 707 Ref.15 Ref.16
Disulfide bond609 ↔ 692 Ref.15 Ref.16
Disulfide bond819 ↔ 829 Ref.15 Ref.16

Natural variations

Alternative sequence6301Missing in isoform 1.
VSP_006748
Natural variant6511H → R in allele ENPP1b. Ref.4
Natural variant6801R → S in allele ENPP1b. Ref.4

Experimental info

Mutagenesis281A → G: No effect on basolateral sorting in epithelial cells. Ref.12
Mutagenesis301S → A or D: Little change in baolateral sorting in epithelial cells. Ref.12
Mutagenesis311L → 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. Ref.12 Ref.13
Mutagenesis321L → 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. Ref.12 Ref.13
Mutagenesis421L → A: No change in increased NPP activity in oestoblastic matrix vesicles. Ref.13
Mutagenesis571Y → G: No change in increased NPP activity in oestoblastic matrix vesicles. Ref.13
Mutagenesis2001D → N: Decreases phosphodiesterase activity by 95%. Abolishes formation of nucleotidylated intermediate. Ref.11
Mutagenesis2371K → A: Decreases phosphodiesterase activity by 40%. Decreased formation of nucleotidylated intermediate. Ref.11
Mutagenesis2381T → A: Abolishes all phosphodiesterase activity. Abolishes formation of nucleotidylated intermediate. Ref.11
Mutagenesis2381T → S: Decreases phosphodiesterase activity by 95%. Accumulates nucleotidylated intermediate. Ref.11
Mutagenesis2391F → A: Decreases phosphodiesterase activity by 50%. Decreased formation of nucleotidylated intermediate. Ref.11 Ref.15
Mutagenesis2421H → L: Strongly decreased phosphodiesterase activity. Ref.15
Mutagenesis304 – 32320Missing: Nearly abolishes activity with nucleotide phosphates. Confers very low activity with lysophospholipids. Ref.15
Mutagenesis3081D → A: Decreased phosphodiesterase activity. Ref.15
Mutagenesis3221Y → A: Strongly decreased phosphodiesterase activity. Ref.15
Mutagenesis3581D → Q: Decreases phosphodiesterase activity by 90%. Accumulates nucleotidylated intermediate. Ref.11
Mutagenesis3621H → Q: Decreases phosphodiesterase activity by 95%. 65% activity can be restored by addition of Zn(2+) ions. Accumulates nucleotidylated intermediate. Ref.11
Mutagenesis4051D → N: Abolishes all phosphodiesterase activity. 10% activity can be restored by addition of Zn(2+) ions. Abolishes formation of nucleotidylated intermediate. Ref.11
Mutagenesis4061H → Q: Abolishes all phosphodiesterase activity. 15% activity can be restored by addition of Zn(2+) ions. Abolishes formation of nucleotidylated intermediate. Ref.11
Mutagenesis5171H → Q: Abolishes all phosphodiesterase activity. 60% activity can be restored by addition of Zn(2+) ions. Abolishes formation of nucleotidylated intermediate. Ref.11

Secondary structure

................................................................................................................................................................... 906
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 2 [UniParc].

Last modified September 19, 2002. Version 4.
Checksum: 068D45B0ED0F224D

FASTA906103,176
        10         20         30         40         50         60 
MERDGDQAGH GPRHGSAGNG RELESPAAAS LLAPMDLGEE PLEKAERARP AKDPNTYKVL 

        70         80         90        100        110        120 
SLVLSVCVLT TILGCIFGLK PSCAKEVKSC KGRCFERTFS NCRCDAACVS LGNCCLDFQE 

       130        140        150        160        170        180 
TCVEPTHIWT CNKFRCGEKR LSRFVCSCAD DCKTHNDCCI NYSSVCQDKK SWVEETCESI 

       190        200        210        220        230        240 
DTPECPAEFE SPPTLLFSLD GFRAEYLHTW GGLLPVISKL KNCGTYTKNM RPMYPTKTFP 

       250        260        270        280        290        300 
NHYSIVTGLY PESHGIIDNK MYDPKMNASF SLKSKEKFNP LWYKGQPIWV TANHQEVKSG 

       310        320        330        340        350        360 
TYFWPGSDVE IDGILPDIYK VYNGSVPFEE RILAVLEWLQ LPSHERPHFY TLYLEEPDSS 

       370        380        390        400        410        420 
GHSHGPVSSE VIKALQKVDR LVGMLMDGLK DLGLDKCLNL ILISDHGMEQ GSCKKYVYLN 

       430        440        450        460        470        480 
KYLGDVNNVK VVYGPAARLR PTDVPETYYS FNYEALAKNL SCREPNQHFR PYLKPFLPKR 

       490        500        510        520        530        540 
LHFAKSDRIE PLTFYLDPQW QLALNPSERK YCGSGFHGSD NLFSNMQALF IGYGPAFKHG 

       550        560        570        580        590        600 
AEVDSFENIE VYNLMCDLLG LIPAPNNGSH GSLNHLLKKP IYNPSHPKEE GFLSQCPIKS 

       610        620        630        640        650        660 
TSNDLGCTCD PWIVPIKDFE KQLNLTTEDV DDIYHMTVPY GRPRILLKQH HVCLLQQQQF 

       670        680        690        700        710        720 
LTGYSLDLLM PLWASYTFLR NDQFSRDDFS NCLYQDLRIP LSPVHKCSYY KSNSKLSYGF 

       730        740        750        760        770        780 
LTPPRLNRVS NHIYSEALLT SNIVPMYQSF QVIWHYLHDT LLQRYAHERN GINVVSGPVF 

       790        800        810        820        830        840 
DFDYDGRYDS LEILKQNSRV IRSQEILIPT HFFIVLTSCK QLSETPLECS ALESSAYILP 

       850        860        870        880        890        900 
HRPDNIESCT HGKRESSWVE ELLTLHRARV TDVELITGLS FYQDRQESVS ELLRLKTHLP 


IFSQED 

« Hide

Isoform 1 [UniParc].

Checksum: FB6EEEA0FF659421
Show »

FASTA905103,076

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS35870.1. [P06802-2]
PIRA27410.
RefSeqXP_006512660.1. XM_006512597.1.
UniGeneMm.27254.
Mm.478860.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP06802.
SMRP06802. Positions 88-903.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-59981N.

PTM databases

PhosphoSiteP06802.

Proteomic databases

MaxQBP06802.
PaxDbP06802.
PRIDEP06802.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000135846; ENSMUSP00000114273; ENSMUSG00000037370.
GeneID18605.
KEGGmmu:18605.

Organism-specific databases

CTD5167.
MGIMGI:97370. Enpp1.

Phylogenomic databases

eggNOGCOG1524.
GeneTreeENSGT00660000095322.
HOGENOMHOG000034646.
HOVERGENHBG051484.
InParanoidP06802.
KOK01513.
PhylomeDBP06802.

Gene expression databases

ArrayExpressP06802.
BgeeP06802.
GenevestigatorP06802.

Family and domain databases

Gene3D3.40.570.10. 1 hit.
3.40.720.10. 1 hit.
InterProIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR001604. DNA/RNA_non-sp_Endonuclease.
IPR024873. E-NPP.
IPR020821. Extracellular_endonuc_su_A.
IPR002591. Phosphodiest/P_Trfase.
IPR020436. Somatomedin_B_chordata.
IPR001212. Somatomedin_B_dom.
[Graphical view]
PANTHERPTHR10151. PTHR10151. 1 hit.
PfamPF01223. Endonuclease_NS. 1 hit.
PF01663. Phosphodiest. 1 hit.
PF01033. Somatomedin_B. 2 hits.
[Graphical view]
PRINTSPR00022. SOMATOMEDINB.
SMARTSM00892. Endonuclease_NS. 1 hit.
SM00477. NUC. 1 hit.
SM00201. SO. 2 hits.
[Graphical view]
SUPFAMSSF53649. SSF53649. 1 hit.
PROSITEPS00524. SMB_1. 2 hits.
PS50958. SMB_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

PROP06802.
SOURCESearch...

Entry information

Entry nameENPP1_MOUSE
AccessionPrimary (citable) accession number: P06802
Secondary accession number(s): Q542E9, Q924C4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: September 19, 2002
Last modified: July 9, 2014
This is version 144 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot