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Protein

Ectonucleotide pyrophosphatase/phosphodiesterase family member 2

Gene

Enpp2

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

Functioni

Hydrolyzes lysophospholipids to produce lysophosphatidic acid (LPA) in extracellular fluids. Major substrate is lysophosphatidylcholine. Also can act on sphingosylphosphphorylcholine producing sphingosine-1-phosphate, a modulator of cell motility. Can hydrolyze, in vitro, bis-pNPP, to some extent pNP-TMP, and barely ATP. Involved in several motility-related processes such as angiogenesis and neurite outgrowth. Acts as an angiogenic factor by stimulating migration of smooth muscle cells and microtubule formation. Stimulates migration of melanoma cells, probably via a pertussis toxin-sensitive G protein. May have a role in induction of parturition. Possible involvement in cell proliferation and adipose tissue development. Tumor cell motility-stimulating factor.2 Publications

Catalytic activityi

1-alkyl-sn-glycero-3-phosphoethanolamine + H2O = 1-alkyl-sn-glycerol 3-phosphate + ethanolamine.2 Publications

Cofactori

Protein has several cofactor binding sites:
  • Zn2+Note: Binds 2 Zn2+ ions per subunit.
  • Ca2+Note: Binds 1 Ca2+ ion per subunit.

Enzyme regulationi

Inhibited by lysophosphatidic acid (LPA) and sphingosine-1-phosphate (S1P) (By similarity). Inhibited by EDTA and EGTA.By similarity1 Publication

Kineticsi

  1. KM=12.9 mM for pNppp (isoform 1)1 Publication
  2. KM=4.4 mM for pNppp (isoform 2)1 Publication
  3. KM=11.8 mM for pNppp (isoform 3)1 Publication
  1. Vmax=1.9 nmol/min/µg enzyme with pNppp as substrate (isoform 1)1 Publication
  2. Vmax=0.35 nmol/min/µg enzyme with pNppp as substrate (isoform 2)1 Publication
  3. Vmax=1.8 nmol/min/µg enzyme with pNppp as substrate (isoform 3)1 Publication

pH dependencei

Optimum pH is 8.0 for isoforms 1, 2 and 3.1 Publication

Temperature dependencei

Isoforms 1 and 3 have maximum activity from 45 to 55 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi171Zinc 1; catalytic1
Active sitei209NucleophileBy similarity1
Metal bindingi209Zinc 1; catalytic1
Binding sitei230Substrate1
Binding sitei306Substrate1
Metal bindingi311Zinc 2; catalytic1
Metal bindingi315Zinc 2; via tele nitrogen; catalytic1
Metal bindingi358Zinc 1; catalytic1
Metal bindingi359Zinc 1; via tele nitrogen; catalytic1
Metal bindingi474Zinc 2; via tele nitrogen; catalytic1
Metal bindingi739Calcium1
Metal bindingi741Calcium1
Metal bindingi745Calcium; via carbonyl oxygen1
Metal bindingi747Calcium1
Sitei852Essential for catalytic activity1

GO - Molecular functioni

  • alkylglycerophosphoethanolamine phosphodiesterase activity Source: UniProtKB-EC
  • calcium ion binding Source: UniProtKB
  • lysophospholipase activity Source: UniProtKB
  • nucleic acid binding Source: InterPro
  • nucleotide diphosphatase activity Source: MGI
  • phosphodiesterase I activity Source: MGI
  • polysaccharide binding Source: InterPro
  • scavenger receptor activity Source: InterPro
  • zinc ion binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Chemotaxis, Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.1.4.39. 3474.
SABIO-RKQ9R1E6.

Names & Taxonomyi

Protein namesi
Recommended name:
Ectonucleotide pyrophosphatase/phosphodiesterase family member 2 (EC:3.1.4.39)
Short name:
E-NPP 2
Alternative name(s):
Autotaxin
Extracellular lysophospholipase D
Short name:
LysoPLD
Gene namesi
Name:Enpp2
Synonyms:Npps2, Pdnp2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1321390. Enpp2.

Subcellular locationi

  • Secreted 2 Publications

  • Note: Secreted by most body fluids including serum and CSF. Also by adipocytes and numerous cancer cells (By similarity).By similarity

GO - Cellular componenti

  • extracellular space Source: UniProtKB
  • integral component of plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

May contribute to obesity (PubMed:15700135).

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi12 – 27Missing : Complete inhibition of secretion. 1 PublicationAdd BLAST16
Mutagenesisi12 – 22Missing : Complete inhibition of secretion. 1 PublicationAdd BLAST11
Mutagenesisi23 – 27Missing : No effect on secretion. 1 Publication5
Mutagenesisi23Missing : No effect on secretion. 1
Mutagenesisi25Missing : No effect on secretion. 1 Publication1
Mutagenesisi27 – 35Missing : No effect on secretion nor lysophospholipase activity. 1 Publication9
Mutagenesisi27 – 30Missing : No effect on secretion. 1 Publication4
Mutagenesisi27Missing : No effect on secretion. 1 Publication1
Mutagenesisi30 – 41Missing : No effect on secretion nor lysophospholipase activity. 1 PublicationAdd BLAST12
Mutagenesisi30 – 33Missing : No effect on secretion nor lysophospholipase activity. 1 Publication4
Mutagenesisi32 – 35Missing : No effect on secretion nor lysophospholipase activity. 1 Publication4
Mutagenesisi36 – 40Missing : No effect on secretion nor lysophospholipase activity. 1 Publication5
Mutagenesisi53Missing : No effect on secretion; slightly decreases lysophospholipase activity. Almost complete loss of lysophospholipase activity; when associated with N-410 del. 1 Publication1
Mutagenesisi210F → A: Reduced lysophospholipase activity. 1 Publication1
Mutagenesisi213L → A: Reduced lysophospholipase activity. 1 Publication1
Mutagenesisi230N → A: Reduced lysophospholipase activity. 1 Publication1
Mutagenesisi243L → A: Reduced lysophospholipase activity. 1 Publication1
Mutagenesisi247E → A: Reduced lysophospholipase activity. 1 Publication1
Mutagenesisi249F → A: Reduced lysophospholipase activity. 1 Publication1
Mutagenesisi410Missing : No effect on secretion; greatly inhibits lysoPLD activity. Inhibits secretion. Almost complete loss of lysoPLD activity; when associated with N-53 del. 1 Publication1
Mutagenesisi512M → A: Reduced lysophospholipase activity. 1
Mutagenesisi851 – 853LKT → AAA, RRR or SSS: No catalytic activity. 1 Publication3
Mutagenesisi851L → A: No effect. 1 Publication1
Mutagenesisi852K → A or R: Strongly reduced catalytic activity. 1 Publication1
Mutagenesisi853T → A: No effect. 1 Publication1

Keywords - Diseasei

Obesity

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27By similarityAdd BLAST27
PropeptideiPRO_000028165028 – 35Removed by furin8
ChainiPRO_000018856836 – 862Ectonucleotide pyrophosphatase/phosphodiesterase family member 2Add BLAST827

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi53N-linked (GlcNAc...)2 Publications1
Disulfide bondi58 ↔ 75
Disulfide bondi62 ↔ 93
Disulfide bondi73 ↔ 86
Disulfide bondi79 ↔ 85
Disulfide bondi102 ↔ 119
Disulfide bondi107 ↔ 137
Disulfide bondi117 ↔ 130
Disulfide bondi123 ↔ 129
Disulfide bondi148 ↔ 194
Disulfide bondi156 ↔ 350
Disulfide bondi366 ↔ 468
Glycosylationi410N-linked (GlcNAc...)2 Publications1
Disulfide bondi413 ↔ 805
Glycosylationi524N-linked (GlcNAc...)2 Publications1
Disulfide bondi566 ↔ 666
Disulfide bondi568 ↔ 651
Disulfide bondi774 ↔ 784
Glycosylationi806N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

N-glycosylation, but not furin-cleavage, plays a critical role on secretion and on lysoPLD activity. Secretion requires simultaneous glycosylation on Asn-53 and Asn-410, while probable glycosylation of Asn-410 has a preferential role on lysoPLD activity. Not O-glycosylated.3 Publications
The interdomain disulfide bond between Cys-413 and Cys-805 is essential for catalytic activity.

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

PeptideAtlasiQ9R1E6.
PRIDEiQ9R1E6.

PTM databases

PhosphoSitePlusiQ9R1E6.

Expressioni

Tissue specificityi

Expressed in brain and adipose tissue.1 Publication

Inductioni

Up-regulated in adipocytes of obese-diabetic db/db mice.1 Publication

Gene expression databases

BgeeiENSMUSG00000022425.
ExpressionAtlasiQ9R1E6. baseline and differential.
GenevisibleiQ9R1E6. MM.

Interactioni

Chemistry databases

BindingDBiQ9R1E6.

Structurei

Secondary structure

1862
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni59 – 63Combined sources5
Helixi77 – 82Combined sources6
Helixi89 – 93Combined sources5
Turni98 – 100Combined sources3
Helixi104 – 106Combined sources3
Beta strandi115 – 118Combined sources4
Helixi123 – 126Combined sources4
Helixi133 – 137Combined sources5
Helixi143 – 145Combined sources3
Beta strandi165 – 171Combined sources7
Helixi175 – 183Combined sources9
Helixi186 – 194Combined sources9
Beta strandi195 – 197Combined sources3
Helixi209 – 218Combined sources10
Helixi222 – 225Combined sources4
Beta strandi229 – 234Combined sources6
Turni235 – 238Combined sources4
Beta strandi239 – 241Combined sources3
Beta strandi243 – 246Combined sources4
Helixi247 – 249Combined sources3
Helixi251 – 253Combined sources3
Helixi259 – 265Combined sources7
Helixi281 – 292Combined sources12
Turni296 – 298Combined sources3
Beta strandi301 – 310Combined sources10
Helixi311 – 317Combined sources7
Beta strandi319 – 321Combined sources3
Helixi322 – 324Combined sources3
Helixi325 – 344Combined sources20
Turni348 – 350Combined sources3
Beta strandi352 – 358Combined sources7
Beta strandi368 – 371Combined sources4
Helixi372 – 374Combined sources3
Helixi379 – 381Combined sources3
Beta strandi382 – 385Combined sources4
Beta strandi387 – 396Combined sources10
Helixi404 – 411Combined sources8
Beta strandi420 – 424Combined sources5
Helixi425 – 427Combined sources3
Helixi430 – 432Combined sources3
Beta strandi438 – 440Combined sources3
Beta strandi442 – 447Combined sources6
Beta strandi452 – 455Combined sources4
Helixi457 – 459Combined sources3
Beta strandi471 – 473Combined sources3
Helixi481 – 483Combined sources3
Beta strandi487 – 491Combined sources5
Beta strandi496 – 499Combined sources4
Helixi505 – 507Combined sources3
Helixi508 – 515Combined sources8
Turni527 – 530Combined sources4
Helixi531 – 533Combined sources3
Beta strandi534 – 536Combined sources3
Beta strandi548 – 551Combined sources4
Helixi559 – 561Combined sources3
Helixi579 – 581Combined sources3
Turni583 – 586Combined sources4
Helixi591 – 595Combined sources5
Beta strandi605 – 607Combined sources3
Beta strandi609 – 613Combined sources5
Beta strandi618 – 622Combined sources5
Turni623 – 626Combined sources4
Beta strandi627 – 635Combined sources9
Helixi646 – 648Combined sources3
Helixi660 – 662Combined sources3
Helixi666 – 671Combined sources6
Beta strandi676 – 681Combined sources6
Helixi683 – 685Combined sources3
Turni689 – 691Combined sources3
Helixi692 – 695Combined sources4
Helixi698 – 700Combined sources3
Beta strandi701 – 704Combined sources4
Helixi706 – 717Combined sources12
Helixi719 – 727Combined sources9
Beta strandi729 – 737Combined sources9
Beta strandi743 – 745Combined sources3
Helixi749 – 751Combined sources3
Beta strandi759 – 761Combined sources3
Beta strandi765 – 776Combined sources12
Helixi781 – 783Combined sources3
Beta strandi788 – 796Combined sources9
Turni805 – 808Combined sources4
Helixi811 – 813Combined sources3
Helixi815 – 821Combined sources7
Helixi826 – 833Combined sources8
Helixi845 – 853Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3NKMX-ray2.00A36-862[»]
3NKNX-ray1.80A36-862[»]
3NKOX-ray1.75A36-862[»]
3NKPX-ray1.75A36-862[»]
3NKQX-ray1.70A36-862[»]
3NKRX-ray1.70A36-862[»]
3WAVX-ray1.80A36-862[»]
3WAWX-ray1.95A36-862[»]
3WAXX-ray1.90A36-862[»]
3WAYX-ray1.75A36-862[»]
4GTWX-ray2.70A/B51-58[»]
4GTXX-ray3.20A/B51-58[»]
4GTYX-ray3.19A/B51-58[»]
4GTZX-ray3.19A/B51-58[»]
5HRTX-ray2.00A36-862[»]
ProteinModelPortaliQ9R1E6.
SMRiQ9R1E6.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9R1E6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini54 – 97SMB 1PROSITE-ProRule annotationAdd BLAST44
Domaini98 – 142SMB 2PROSITE-ProRule annotationAdd BLAST45

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni144 – 501PhosphodiesteraseAdd BLAST358
Regioni210 – 213Substrate binding4
Regioni243 – 254Substrate bindingAdd BLAST12
Regioni597 – 862NucleaseAdd BLAST266
Regioni829 – 850Required for secretionAdd BLAST22

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi126 – 128Cell attachment siteSequence analysis3

Sequence similaritiesi

Contains 2 SMB (somatomedin-B) domains.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

GeneTreeiENSGT00760000119157.
HOGENOMiHOG000037439.
HOVERGENiHBG051484.
InParanoidiQ9R1E6.
KOiK01122.
OMAiGMEDVTC.
OrthoDBiEOG091G017X.
PhylomeDBiQ9R1E6.
TreeFamiTF330032.

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.
IPR029881. ENPP2.
IPR020821. Extracellular_endonuc_su_A.
IPR002591. Phosphodiest/P_Trfase.
IPR020436. Somatomedin_B_chordata.
IPR001212. Somatomedin_B_dom.
[Graphical view]
PANTHERiPTHR10151. PTHR10151. 1 hit.
PTHR10151:SF21. PTHR10151:SF21. 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.
SSF90188. SSF90188. 2 hits.
PROSITEiPS00524. SMB_1. 2 hits.
PS50958. SMB_2. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9R1E6-1) [UniParc]FASTAAdd to basket
Also known as: Beta

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
MARQGCFGSY QVISLFTFAI GVNLCLGFTA SRIKRAEWDE GPPTVLSDSP
60 70 80 90 100
WTNTSGSCKG RCFELQEVGP PDCRCDNLCK SYSSCCHDFD ELCLKTARGW
110 120 130 140 150
ECTKDRCGEV RNEENACHCS EDCLSRGDCC TNYQVVCKGE SHWVDDDCEE
160 170 180 190 200
IRVPECPAGF VRPPLIIFSV DGFRASYMKK GSKVMPNIEK LRSCGTHAPY
210 220 230 240 250
MRPVYPTKTF PNLYTLATGL YPESHGIVGN SMYDPVFDAT FHLRGREKFN
260 270 280 290 300
HRWWGGQPLW ITATKQGVRA GTFFWSVSIP HERRILTILQ WLSLPDNERP
310 320 330 340 350
SVYAFYSEQP DFSGHKYGPF GPEMTNPLRE IDKTVGQLMD GLKQLKLHRC
360 370 380 390 400
VNVIFVGDHG MEDVTCDRTE FLSNYLTNVD DITLVPGTLG RIRPKIPNNL
410 420 430 440 450
KYDPKAIIAN LTCKKPDQHF KPYMKQHLPK RLHYANNRRI EDLHLLVERR
460 470 480 490 500
WHVARKPLDV YKKPSGKCFF QGDHGFDNKV NSMQTVFVGY GPTFKYRTKV
510 520 530 540 550
PPFENIELYN VMCDLLGLKP APNNGTHGSL NHLLRTNTFR PTLPEEVSRP
560 570 580 590 600
NYPGIMYLQS DFDLGCTCDD KVEPKNKLEE LNKRLHTKGS TEERHLLYGR
610 620 630 640 650
PAVLYRTSYD ILYHTDFESG YSEIFLMPLW TSYTISKQAE VSSIPEHLTN
660 670 680 690 700
CVRPDVRVSP GFSQNCLAYK NDKQMSYGFL FPPYLSSSPE AKYDAFLVTN
710 720 730 740 750
MVPMYPAFKR VWTYFQRVLV KKYASERNGV NVISGPIFDY NYNGLRDIED
760 770 780 790 800
EIKQYVEGSS IPVPTHYYSI ITSCLDFTQP ADKCDGPLSV SSFILPHRPD
810 820 830 840 850
NDESCNSSED ESKWVEELMK MHTARVRDIE HLTGLDFYRK TSRSYSEILT
860
LKTYLHTYES EI
Length:862
Mass (Da):98,885
Last modified:February 10, 2009 - v3
Checksum:i343D44DEAA8FA352
GO
Isoform 2 (identifier: Q9R1E6-2) [UniParc]FASTAAdd to basket
Also known as: Alpha

The sequence of this isoform differs from the canonical sequence as follows:
     323-323: E → EESSYGSPLTPAKRPKRKVAPKRRQERPVAPPKKRRRKLHRMDHYTAETRQDK

Show »
Length:914
Mass (Da):105,089
Checksum:iE36A577AB858AF02
GO
Isoform 3 (identifier: Q9R1E6-3) [UniParc]FASTAAdd to basket
Also known as: Gamma

The sequence of this isoform differs from the canonical sequence as follows:
     592-592: E → EAETGKFRGSKHENKKSLNGNVEPRK

Show »
Length:887
Mass (Da):101,680
Checksum:i599952429BBFBD6B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti103T → I in ACD12866 (Ref. 3) Curated1
Sequence conflicti517G → S in AAD46480 (PubMed:10702660).Curated1
Sequence conflicti550P → T in AAD46480 (PubMed:10702660).Curated1
Sequence conflicti573E → K in AAD46480 (PubMed:10702660).Curated1
Sequence conflicti743N → D in ACD12866 (Ref. 3) Curated1
Sequence conflicti743N → D in AAH03264 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_036396323E → EESSYGSPLTPAKRPKRKVA PKRRQERPVAPPKKRRRKLH RMDHYTAETRQDK in isoform 2. 1 Publication1
Alternative sequenceiVSP_036397592E → EAETGKFRGSKHENKKSLNG NVEPRK in isoform 3. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF123542 mRNA. Translation: AAD46480.1.
EU131009 mRNA. Translation: ABW38314.1.
EU131010 mRNA. Translation: ABW38315.1.
EU677474 Genomic DNA. Translation: ACD12865.1.
EU677475 Genomic DNA. Translation: ACD12866.1.
AK161144 mRNA. Translation: BAE36214.1.
CH466545 Genomic DNA. Translation: EDL29265.1.
BC003264 mRNA. Translation: AAH03264.1.
BC058759 mRNA. Translation: AAH58759.1.
CCDSiCCDS27472.1. [Q9R1E6-1]
CCDS49607.1. [Q9R1E6-2]
CCDS70628.1. [Q9R1E6-3]
RefSeqiNP_001129549.1. NM_001136077.3. [Q9R1E6-2]
NP_001272923.1. NM_001285994.2. [Q9R1E6-3]
NP_001272924.1. NM_001285995.2.
NP_056559.2. NM_015744.4. [Q9R1E6-1]
UniGeneiMm.250256.

Genome annotation databases

EnsembliENSMUST00000041591; ENSMUSP00000036180; ENSMUSG00000022425. [Q9R1E6-1]
ENSMUST00000167541; ENSMUSP00000132640; ENSMUSG00000022425. [Q9R1E6-3]
ENSMUST00000171545; ENSMUSP00000128941; ENSMUSG00000022425. [Q9R1E6-2]
GeneIDi18606.
KEGGimmu:18606.
UCSCiuc007vro.3. mouse. [Q9R1E6-1]
uc007vrq.3. mouse. [Q9R1E6-3]
uc011zsx.2. mouse. [Q9R1E6-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF123542 mRNA. Translation: AAD46480.1.
EU131009 mRNA. Translation: ABW38314.1.
EU131010 mRNA. Translation: ABW38315.1.
EU677474 Genomic DNA. Translation: ACD12865.1.
EU677475 Genomic DNA. Translation: ACD12866.1.
AK161144 mRNA. Translation: BAE36214.1.
CH466545 Genomic DNA. Translation: EDL29265.1.
BC003264 mRNA. Translation: AAH03264.1.
BC058759 mRNA. Translation: AAH58759.1.
CCDSiCCDS27472.1. [Q9R1E6-1]
CCDS49607.1. [Q9R1E6-2]
CCDS70628.1. [Q9R1E6-3]
RefSeqiNP_001129549.1. NM_001136077.3. [Q9R1E6-2]
NP_001272923.1. NM_001285994.2. [Q9R1E6-3]
NP_001272924.1. NM_001285995.2.
NP_056559.2. NM_015744.4. [Q9R1E6-1]
UniGeneiMm.250256.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3NKMX-ray2.00A36-862[»]
3NKNX-ray1.80A36-862[»]
3NKOX-ray1.75A36-862[»]
3NKPX-ray1.75A36-862[»]
3NKQX-ray1.70A36-862[»]
3NKRX-ray1.70A36-862[»]
3WAVX-ray1.80A36-862[»]
3WAWX-ray1.95A36-862[»]
3WAXX-ray1.90A36-862[»]
3WAYX-ray1.75A36-862[»]
4GTWX-ray2.70A/B51-58[»]
4GTXX-ray3.20A/B51-58[»]
4GTYX-ray3.19A/B51-58[»]
4GTZX-ray3.19A/B51-58[»]
5HRTX-ray2.00A36-862[»]
ProteinModelPortaliQ9R1E6.
SMRiQ9R1E6.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiQ9R1E6.

PTM databases

PhosphoSitePlusiQ9R1E6.

Proteomic databases

PeptideAtlasiQ9R1E6.
PRIDEiQ9R1E6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000041591; ENSMUSP00000036180; ENSMUSG00000022425. [Q9R1E6-1]
ENSMUST00000167541; ENSMUSP00000132640; ENSMUSG00000022425. [Q9R1E6-3]
ENSMUST00000171545; ENSMUSP00000128941; ENSMUSG00000022425. [Q9R1E6-2]
GeneIDi18606.
KEGGimmu:18606.
UCSCiuc007vro.3. mouse. [Q9R1E6-1]
uc007vrq.3. mouse. [Q9R1E6-3]
uc011zsx.2. mouse. [Q9R1E6-2]

Organism-specific databases

CTDi5168.
MGIiMGI:1321390. Enpp2.

Phylogenomic databases

GeneTreeiENSGT00760000119157.
HOGENOMiHOG000037439.
HOVERGENiHBG051484.
InParanoidiQ9R1E6.
KOiK01122.
OMAiGMEDVTC.
OrthoDBiEOG091G017X.
PhylomeDBiQ9R1E6.
TreeFamiTF330032.

Enzyme and pathway databases

BRENDAi3.1.4.39. 3474.
SABIO-RKQ9R1E6.

Miscellaneous databases

ChiTaRSiEnpp2. mouse.
EvolutionaryTraceiQ9R1E6.
PROiQ9R1E6.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000022425.
ExpressionAtlasiQ9R1E6. baseline and differential.
GenevisibleiQ9R1E6. MM.

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.
IPR029881. ENPP2.
IPR020821. Extracellular_endonuc_su_A.
IPR002591. Phosphodiest/P_Trfase.
IPR020436. Somatomedin_B_chordata.
IPR001212. Somatomedin_B_dom.
[Graphical view]
PANTHERiPTHR10151. PTHR10151. 1 hit.
PTHR10151:SF21. PTHR10151:SF21. 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.
SSF90188. SSF90188. 2 hits.
PROSITEiPS00524. SMB_1. 2 hits.
PS50958. SMB_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiENPP2_MOUSE
AccessioniPrimary (citable) accession number: Q9R1E6
Secondary accession number(s): A8UH85
, A8UH93, B2ZP54, Q6PDE0, Q99LG9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: February 10, 2009
Last modified: November 30, 2016
This is version 150 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, 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

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 one 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.