Reviewed, UniProtKB/Swiss-Prot P06802 (ENPP1_MOUSE)

Names and origin

Protein names

Recommended name:
    Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
      Short name=E-NPP 1
Alternative name(s):
    Phosphodiesterase I/nucleotide pyrophosphatase 1
    Plasma-cell membrane glycoprotein PC-1
    Lymphocyte antigen 41
      Short name=Ly-41
Including the following 2 domains:
    1- Recommended name:
            Alkaline phosphodiesterase I
              EC=3.1.4.1
    2- Recommended name:
            Nucleotide pyrophosphatase
                Short name=NPPase
              EC=3.6.1.9

Gene names

Name:	Enpp1
Synonyms:	Npps, Pc1, Pdnp1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	906 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Involved primarily in ATP hydrolysis at the plasma membrane. Plays a role in regulating pyrophosphate levels, and functions in bone mineralization and soft tissue calcification. In vitro, has a broad specificity, hydrolyzing 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. Appears to modulate insulin sensitivity By similarity. Ref.3
Catalytic activity	Hydrolytically removes 5'-nucleotides successively from the 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides. A dinucleotide + H2O = 2 mononucleotides.
Cofactor	Binds 2 divalent metal cations per subunit Probable.
Enzyme regulation	At low concentrations of ATP, a phosphorylated intermediate is formed which inhibits further hydrolysis.
Subunit structure	Homodimer; disulfide-linked.
Subcellular location	Membrane; Single-pass type II membrane protein. Basolateral cell membrane; Single-pass type II membrane protein By similarity. 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. Ref.12 Ref.13
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.14 It has been suggested that the active SMB domain may be permitted considerable disulfide bond heterogeneity or variability, thus two alternate disulfide patterns based on 3D structures are described with 1 disulfide bond conserved in both.
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.

Ontologies

Keywords
Biological process	Biomineralization
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Domain	Repeat Signal-anchor Transmembrane
Ligand	Metal-binding
Molecular function	Hydrolase
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Direct protein sequencing Multifunctional enzyme
Gene Ontology (GO)
Biological process	biomineral formation Inferred from electronic annotation. Source: UniProtKB-KW bone remodeling Inferred from mutant phenotype. Source: MGI immune response Inferred from electronic annotation. Source: InterPro negative regulation of fat cell differentiation Inferred from mutant phenotype. Source: UniProtKB negative regulation of ossification Ref.10 Inferred from mutant phenotype. Source: MGI
Cellular component	cell surface Ref.6 Inferred from direct assay. Source: UniProtKB extracellular space Ref.6 Inferred from direct assay. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW nucleic acid binding Inferred from electronic annotation. Source: InterPro nucleotide diphosphatase activity Inferred from electronic annotation. Source: EC phosphodiesterase I activity Inferred from electronic annotation. Source: EC polysaccharide binding Inferred from electronic annotation. Source: InterPro scavenger receptor activity Inferred from electronic annotation. Source: InterPro
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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 906	906	Ectonucleotide pyrophosphatase/phosphodiesterase family member 1		PRO_0000188565
Regions
	Topological domain	1 – 58	58	Cytoplasmic Potential
	Transmembrane	59 – 79	21	Signal-anchor for type II membrane protein Potential
	Topological domain	80 – 906	827	Extracellular Potential
	Domain	86 – 126	41	SMB 1
	Domain	127 – 171	45	SMB 2
	Region	173 – 573	401	Phosphodiesterase
	Region	635 – 906	272	Nuclease
	Motif	27 – 34	8	Di-leucine motif
Sites
	Active site	238	1	AMP-threonine intermediate Ref.11
	Metal binding	200	1	Divalent metal cation 2 Probable
	Metal binding	358	1	Divalent metal cation 1 Probable
	Metal binding	362	1	Divalent metal cation 1 Probable
	Metal binding	405	1	Divalent metal cation 2 Probable
	Metal binding	406	1	Divalent metal cation 2 Probable
	Metal binding	517	1	Divalent metal cation 1 Probable
	Site	896	1	Essential for catalytic activity By similarity
Amino acid modifications
	Glycosylation	161	1	N-linked (GlcNAc...) Potential
	Glycosylation	267	1	N-linked (GlcNAc...) Ref.14
	Glycosylation	323	1	N-linked (GlcNAc...) Ref.14
	Glycosylation	459	1	N-linked (GlcNAc...) Potential
	Glycosylation	567	1	N-linked (GlcNAc...) Potential
	Glycosylation	624	1	N-linked (GlcNAc...) Ref.14
	Disulfide bond	90 ↔ 104		Alternate By similarity
	Disulfide bond	90 ↔ 94		Alternate By similarity
	Disulfide bond	94 ↔ 122		Alternate By similarity
	Disulfide bond	102 ↔ 115		Alternate By similarity
	Disulfide bond	102 ↔ 104		Alternate By similarity
	Disulfide bond	108 ↔ 114		By similarity
	Disulfide bond	115 ↔ 122		Alternate By similarity
	Disulfide bond	131 ↔ 148		Alternate By similarity
	Disulfide bond	131 ↔ 136		Alternate By similarity
	Disulfide bond	136 ↔ 166		Alternate By similarity
	Disulfide bond	146 ↔ 159		Alternate By similarity
	Disulfide bond	146 ↔ 148		Alternate By similarity
	Disulfide bond	152 ↔ 158		By similarity
	Disulfide bond	159 ↔ 166		Alternate By similarity
	Disulfide bond	462 ↔ 849		By similarity
Natural variations
	Alternative sequence	630	1	Missing in isoform 1.		VSP_006748
	Natural variant	651	1	H → R in allele ENPP1b. Ref.4
	Natural variant	680	1	R → S in allele ENPP1b. Ref.4
Experimental info
	Mutagenesis	28	1	A → G: No effect on basolateral sorting in epithelial cells. Ref.12
	Mutagenesis	30	1	S → A or D: Little change in baolateral sorting in epithelial cells. Ref.12
	Mutagenesis	31	1	L → 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
	Mutagenesis	32	1	L → 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
	Mutagenesis	42	1	L → A: No change in increased NPP activity in oestoblastic matrix vesicles. Ref.13
	Mutagenesis	57	1	Y → G: No change in increased NPP activity in oestoblastic matrix vesicles. Ref.13
	Mutagenesis	200	1	D → N: Decreases phosphodiesterase activity by 95%. Abolishes formation of nucleotidylated intermediate. Ref.11
	Mutagenesis	237	1	K → A: Decreases phosphodiesterase activity by 40%. Decreased formation of nucleotidylated intermediate. Ref.11
	Mutagenesis	238	1	T → A: Abolishes all phosphodiesterase activity. Abolishes formation of nucleotidylated intermediate. Ref.11
	Mutagenesis	238	1	T → S: Decreases phosphodiesterase activity by 95%. Accumulates nucleotidylated intermediate. Ref.11
	Mutagenesis	239	1	F → A: Decreases phosphodiesterase activity by 50%. Decreased formation of nucleotidylated intermediate. Ref.11
	Mutagenesis	358	1	D → Q: Decreases phosphodiesterase activity by 90%. Accumulates nucleotidylated intermediate. Ref.11
	Mutagenesis	362	1	H → Q: Decreases phosphodiesterase activity by 95%. 65% activity can be restored by addition of Zn(2+) ions. Accumulates nucleotidylated intermediate. Ref.11
	Mutagenesis	405	1	D → N: Abolishes all phosphodiesterase activity. 10% activity can be restored by addition of Zn(2+) ions. Abolishes formation of nucleotidylated intermediate. Ref.11
	Mutagenesis	406	1	H → Q: Abolishes all phosphodiesterase activity. 15% activity can be restored by addition of Zn(2+) ions. Abolishes formation of nucleotidylated intermediate. Ref.11
	Mutagenesis	517	1	H → Q: Abolishes all phosphodiesterase activity. 60% activity can be restored by addition of Zn(2+) ions. Abolishes formation of nucleotidylated intermediate. Ref.11

Sequences

	Sequence		Length	Mass (Da)
	Isoform 2 [UniParc]. Last modified September 19, 2002. Version 4. Checksum: 068D45B0ED0F224D	FASTA	906	103,176
	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
	Isoform 1. Checksum: FB6EEEA0FF659421	FASTA	905	103,076
	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 KQLNLTTEDD DIYHMTVPYG RPRILLKQHH VCLLQQQQFL 670 680 690 700 710 720 TGYSLDLLMP LWASYTFLRN DQFSRDDFSN CLYQDLRIPL SPVHKCSYYK SNSKLSYGFL 730 740 750 760 770 780 TPPRLNRVSN HIYSEALLTS NIVPMYQSFQ VIWHYLHDTL LQRYAHERNG INVVSGPVFD 790 800 810 820 830 840 FDYDGRYDSL EILKQNSRVI RSQEILIPTH FFIVLTSCKQ LSETPLECSA LESSAYILPH 850 860 870 880 890 900 RPDNIESCTH GKRESSWVEE LLTLHRARVT DVELITGLSF YQDRQESVSE LLRLKTHLPI FSQED

References

	« Hide 'large scale' referencesShow '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: 3104326] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). 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: 1647027] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], GLYCOSYLATION, FUNCTION. 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: 12121276] [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: 16141072] [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: 8223581] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 168-188.
[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: 3001713] [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: 3917281] [Abstract] Cited for: PROTEIN SEQUENCE OF 204-219; 332-351; 486-509; 716-725; 803-818 AND 855-867.
[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: 2211644] [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: 9662402] [Abstract] Cited for: DISEASE.
[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: 11027689] [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.
[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: 11598187] [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: 15075217] [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: 19656770] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-267; ASN-323 AND ASN-624, MASS SPECTROMETRY. Tissue: Myoblast.
+	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.
IPI	IPI00128859. IPI00265291.
PIR	A27410.
UniGene	Mm.27254
3D structure databases
SMR	P06802. Positions 81-125, 129-171, 192-578, 637-893.
ModBase	Search...
Protein-protein interaction databases
STRING	P06802.
PTM databases
PhosphoSite	P06802.
Proteomic databases
PRIDE	P06802.
Genome annotation databases
Ensembl	ENSMUST00000039882; ENSMUSP00000046090; ENSMUSG00000037370; Mus musculus. [Genome view]
Organism-specific databases
MGI	MGI:97370. Enpp1.
Phylogenomic databases
eggNOG	roNOG12236.
HOGENOM	HBG357577.
HOVERGEN	P06802.
InParanoid	P06802.
PhylomeDB	P06802.
Enzyme and pathway databases
BRENDA	3.1.4.1. 244. 3.6.1.9. 244.
Gene expression databases
ArrayExpress	P06802.
Bgee	P06802.
Genevestigator	P06802.
GermOnline	ENSMUSG00000037370. Mus musculus.
Family and domain databases
InterPro	IPR017849. Alkaline_Pase-like_a/b/a. IPR017850. Alkaline_phosphatase_core. IPR001604. DNA/RNA_non-sp_Endonuclease. IPR020821. Extracellular_endonuc_su_A. IPR002591. Phosphodiest/P_Trfase. IPR001212. Somatomedin_B. IPR020436. Somatomedin_B_chordata. [Graphical view]
Gene3D	G3DSA:3.40.720.10. Alk_phosphtse. 1 hit. G3DSA:3.40.570.10. Endonuclease. 1 hit.
Pfam	PF01223. Endonuclease_NS. 1 hit. PF01663. Phosphodiest. 1 hit. PF01033. Somatomedin_B. 2 hits. [Graphical view]
PRINTS	PR00022. SOMATOMEDINB.
SMART	SM00892. Endonuclease_NS. 1 hit. SM00477. NUC. 1 hit. SM00201. SO. 2 hits. [Graphical view]
PROSITE	PS00524. SMB_1. 2 hits. PS50958. SMB_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other Resources
SOURCE	Search...

Entry information

Entry name

ENPP1_MOUSE

Accession

Primary (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:	February 9, 2010
This is version 108 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)