Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ectonucleotide pyrophosphatase/phosphodiesterase family member 2

Gene

Enpp2

Organism
Rattus norvegicus (Rat)
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.1 Publication

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi171 – 1711Zinc 1; catalytic
Active sitei209 – 2091NucleophileBy similarity
Metal bindingi209 – 2091Zinc 1; catalytic
Binding sitei230 – 2301SubstrateBy similarity
Binding sitei306 – 3061SubstrateBy similarity
Metal bindingi311 – 3111Zinc 2; catalytic
Metal bindingi315 – 3151Zinc 2; catalytic
Metal bindingi315 – 3151Zinc 2; via tele nitrogen; catalyticBy similarity
Metal bindingi358 – 3581Zinc 1; catalytic
Metal bindingi359 – 3591Zinc 1; catalytic
Metal bindingi359 – 3591Zinc 1; via tele nitrogen; catalyticBy similarity
Metal bindingi474 – 4741Zinc 2; catalytic
Metal bindingi474 – 4741Zinc 2; via tele nitrogen; catalyticBy similarity
Metal bindingi764 – 7641Calcium
Metal bindingi766 – 7661Calcium
Metal bindingi768 – 7681Calcium
Metal bindingi770 – 7701Calcium; via carbonyl oxygen
Metal bindingi772 – 7721Calcium
Sitei877 – 8771Essential for catalytic activityBy similarity

GO - Molecular functioni

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

GO - Biological processi

  • cell chemotaxis Source: RGD
  • cellular response to cadmium ion Source: RGD
  • cellular response to estradiol stimulus Source: RGD
  • estrous cycle Source: RGD
  • immune response Source: InterPro
  • negative regulation of cell-matrix adhesion Source: RGD
  • nucleic acid phosphodiester bond hydrolysis Source: GOC
  • phosphatidylcholine catabolic process Source: UniProtKB
  • positive regulation of cell proliferation Source: RGD
  • positive regulation of focal adhesion assembly Source: RGD
  • positive regulation of oligodendrocyte differentiation Source: RGD
  • positive regulation of substrate adhesion-dependent cell spreading Source: RGD
  • regulation of angiogenesis Source: InterPro
  • regulation of cell migration Source: InterPro
  • response to polycyclic arene Source: RGD
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. 5301.
SABIO-RKQ64610.

Chemistry

SwissLipidsiSLP:000000394.

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:Atx, Npps2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi69298. Enpp2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: RGD
  • extracellular space Source: UniProtKB
  • Golgi apparatus Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi13 – 131I → L: No effect on secretion. 1 Publication
Mutagenesisi16 – 183FTF → VLS: No effect on secretion. 1 Publication
Mutagenesisi18 – 214FAIS → SVCV: No effect on secretion. 1 Publication
Mutagenesisi21 – 244SVNI → VLTT: No effect on secretion. 1 Publication
Mutagenesisi24 – 252IC → TI: No effect on secretion. 1 Publication
Mutagenesisi28 – 303FTA → CIF: No effect on secretion. 1 Publication
Mutagenesisi171 – 1711D → N: Abolishes lysophospholipase D activity. 1 Publication
Mutagenesisi209 – 2091T → A: Abolishes lysophospholipase D activity. 1 Publication
Mutagenesisi209 – 2091T → S: 15% of wild-type lysophospholipase D activity. 1 Publication
Mutagenesisi311 – 3111D → N: Abolishes lysophospholipase D activity. 1 Publication
Mutagenesisi315 – 3151H → Q: 20% of wild-type lysophospholipase D activity. 1 Publication
Mutagenesisi430 – 4301K → A: Impaired secretion. No effect on lysophospholipase activity. 1 Publication
Mutagenesisi764 – 7685DYNYD → SYAYS: Abolishes secretion. Strongly reduced lysophospholipase activity. 1 Publication

Keywords - Diseasei

Obesity

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 27272 PublicationsAdd
BLAST
Propeptidei28 – 358Removed by furin2 PublicationsPRO_0000281651
Chaini36 – 887852Ectonucleotide pyrophosphatase/phosphodiesterase family member 2PRO_0000188569Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi53 – 531N-linked (GlcNAc...)Sequence analysis
Disulfide bondi58 ↔ 75PROSITE-ProRule annotation1 Publication
Disulfide bondi62 ↔ 93PROSITE-ProRule annotation1 Publication
Disulfide bondi73 ↔ 86PROSITE-ProRule annotation1 Publication
Disulfide bondi79 ↔ 85PROSITE-ProRule annotation1 Publication
Disulfide bondi102 ↔ 119PROSITE-ProRule annotation1 Publication
Disulfide bondi107 ↔ 137PROSITE-ProRule annotation1 Publication
Disulfide bondi117 ↔ 130PROSITE-ProRule annotation1 Publication
Disulfide bondi123 ↔ 129PROSITE-ProRule annotation1 Publication
Disulfide bondi148 ↔ 194PROSITE-ProRule annotation1 Publication
Disulfide bondi156 ↔ 350PROSITE-ProRule annotation1 Publication
Disulfide bondi366 ↔ 468PROSITE-ProRule annotation1 Publication
Glycosylationi398 – 3981N-linked (GlcNAc...)Sequence analysis
Glycosylationi410 – 4101N-linked (GlcNAc...)Sequence analysis
Disulfide bondi413 ↔ 830PROSITE-ProRule annotation1 Publication
Glycosylationi524 – 5241N-linked (GlcNAc...)1 Publication
Disulfide bondi566 ↔ 691PROSITE-ProRule annotation1 Publication
Disulfide bondi568 ↔ 676PROSITE-ProRule annotation1 Publication
Glycosylationi610 – 6101N-linked (GlcNAc...)Sequence analysis
Disulfide bondi799 ↔ 809PROSITE-ProRule annotation1 Publication
Glycosylationi831 – 8311N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

N-glycosylation, but not furin-cleavage, plays a critical role on secretion and on lysoPLD activity.By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ64610.

Expressioni

Tissue specificityi

Abundantly expressed in cerebrum and cerebellum. Localized in secretory epithelial cells in the brain and the eye including choroid plexus epithelial cells, ciliary epithelial cells, iris pigment epithelial cells, and retinal pigment cells.2 Publications

Interactioni

Protein-protein interaction databases

MINTiMINT-4997409.

Structurei

Secondary structure

1
887
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni59 – 635Combined sources
Beta strandi70 – 723Combined sources
Turni77 – 837Combined sources
Helixi89 – 924Combined sources
Helixi104 – 1063Combined sources
Beta strandi115 – 1184Combined sources
Helixi123 – 1264Combined sources
Helixi133 – 1386Combined sources
Helixi143 – 1453Combined sources
Beta strandi165 – 1717Combined sources
Helixi175 – 1806Combined sources
Turni182 – 1843Combined sources
Helixi186 – 1949Combined sources
Beta strandi195 – 1973Combined sources
Helixi209 – 21810Combined sources
Helixi222 – 2254Combined sources
Beta strandi230 – 2345Combined sources
Turni235 – 2384Combined sources
Beta strandi239 – 2413Combined sources
Beta strandi243 – 2464Combined sources
Helixi247 – 2493Combined sources
Helixi251 – 2533Combined sources
Helixi259 – 2657Combined sources
Helixi281 – 29212Combined sources
Turni296 – 2983Combined sources
Beta strandi301 – 31010Combined sources
Helixi311 – 3177Combined sources
Helixi322 – 3243Combined sources
Helixi325 – 34420Combined sources
Turni348 – 3503Combined sources
Beta strandi352 – 3587Combined sources
Beta strandi368 – 3714Combined sources
Helixi372 – 3743Combined sources
Helixi379 – 3813Combined sources
Beta strandi382 – 3854Combined sources
Beta strandi387 – 3959Combined sources
Helixi404 – 4107Combined sources
Beta strandi420 – 4245Combined sources
Helixi425 – 4273Combined sources
Helixi430 – 4323Combined sources
Beta strandi442 – 4476Combined sources
Beta strandi452 – 4554Combined sources
Helixi481 – 4833Combined sources
Beta strandi487 – 4915Combined sources
Beta strandi496 – 4994Combined sources
Helixi505 – 5073Combined sources
Helixi508 – 5158Combined sources
Turni527 – 5304Combined sources
Helixi531 – 5333Combined sources
Beta strandi534 – 5363Combined sources
Helixi559 – 5613Combined sources
Helixi578 – 5803Combined sources
Turni583 – 5864Combined sources
Helixi617 – 6204Combined sources
Beta strandi634 – 6385Combined sources
Beta strandi643 – 6475Combined sources
Turni648 – 6514Combined sources
Beta strandi652 – 6609Combined sources
Helixi671 – 6733Combined sources
Helixi685 – 6873Combined sources
Helixi691 – 6966Combined sources
Beta strandi701 – 7066Combined sources
Helixi708 – 7103Combined sources
Helixi714 – 7207Combined sources
Helixi723 – 7253Combined sources
Beta strandi726 – 7294Combined sources
Helixi731 – 74212Combined sources
Helixi744 – 7529Combined sources
Beta strandi754 – 7629Combined sources
Beta strandi768 – 7703Combined sources
Helixi774 – 7763Combined sources
Beta strandi790 – 80112Combined sources
Helixi806 – 8083Combined sources
Beta strandi813 – 8219Combined sources
Turni830 – 8334Combined sources
Helixi836 – 8383Combined sources
Helixi840 – 8467Combined sources
Helixi851 – 8588Combined sources
Helixi870 – 8789Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XR9X-ray2.05A36-887[»]
2XRGX-ray3.20A1-887[»]
ProteinModelPortaliQ64610.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ64610.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini54 – 9744SMB 1PROSITE-ProRule annotationAdd
BLAST
Domaini98 – 14245SMB 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni210 – 2134Substrate bindingBy similarity
Regioni243 – 25412Substrate bindingBy similarityAdd
BLAST
Regioni854 – 87522Required for secretionBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi126 – 1283Cell attachment siteSequence analysis

Sequence similaritiesi

Contains 2 SMB (somatomedin-B) domains.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

HOGENOMiHOG000037439.
HOVERGENiHBG051484.
InParanoidiQ64610.
KOiK01122.
PhylomeDBiQ64610.

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. 2 hits.
PTHR10151:SF21. PTHR10151:SF21. 2 hits.
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 (2)i

Sequence statusi: Complete.

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

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

Isoform 1 (identifier: Q64610-1) [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
MARQGCLGSF QVISLFTFAI SVNICLGFTA 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
IKVPECPAGF VRPPLIIFSV DGFRASYMKK GSKVMPNIEK LRSCGTHAPY
210 220 230 240 250
MRPVYPTKTF PNLYTLATGL YPESHGIVGN SMYDPVFDAS FHLRGREKFN
260 270 280 290 300
HRWWGGQPLW ITATKQGVRA GTFFWSVSIP HERRILTILQ WLSLPDNERP
310 320 330 340 350
SVYAFYSEQP DFSGHKYGPF GPEMTNPLRE IDKTVGQLMD GLKQLRLHRC
360 370 380 390 400
VNVIFVGDHG MEDVTCDRTE FLSNYLTNVD DITLVPGTLG RIRAKSINNS
410 420 430 440 450
KYDPKTIIAN LTCKKPDQHF KPYMKQHLPK RLHYANNRRI EDIHLLVDRR
460 470 480 490 500
WHVARKPLDV YKKPSGKCFF QGDHGFDNKV NSMQTVFVGY GPTFKYRTKV
510 520 530 540 550
PPFENIELYN VMCDLLGLKP APNNGTHGSL NHLLRTNTFR PTMPDEVSRP
560 570 580 590 600
NYPGIMYLQS EFDLGCTCDD KVEPKNKLEE LNKRLHTKGS TEAETGKFRG
610 620 630 640 650
SKHENKKNLN GSVEPRKERH LLYGRPAVLY RTSYDILYHT DFESGYSEIF
660 670 680 690 700
LMPLWTSYTI SKQAEVSSIP EHLTNCVRPD VRVSPGFSQN CLAYKNDKQM
710 720 730 740 750
SYGFLFPPYL SSSPEAKYDA FLVTNMVPMY PAFKRVWAYF QRVLVKKYAS
760 770 780 790 800
ERNGVNVISG PIFDYNYDGL RDTEDEIKQY VEGSSIPVPT HYYSIITSCL
810 820 830 840 850
DFTQPADKCD GPLSVSSFIL PHRPDNDESC NSSEDESKWV EELMKMHTAR
860 870 880
VRDIEHLTGL DFYRKTSRSY SEILTLKTYL HTYESEI
Length:887
Mass (Da):101,576
Last modified:March 20, 2007 - v2
Checksum:i40AD1C957F833869
GO
Isoform 2 (identifier: Q64610-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     591-615: Missing.

Note: No experimental confirmation available.
Show »
Length:862
Mass (Da):98,836
Checksum:i2A530389DBA57952
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti97 – 971A → V in BAA05910 (PubMed:7961762).Curated
Sequence conflicti107 – 1071C → S in BAA05910 (PubMed:7961762).Curated
Sequence conflicti120 – 1201S → P in BAA05910 (PubMed:7961762).Curated
Sequence conflicti147 – 16216DCEEI…AGFVR → AARNQSSECLQVCP in BAA05910 (PubMed:7961762).CuratedAdd
BLAST
Sequence conflicti198 – 1981A → V in BAA05910 (PubMed:7961762).Curated
Sequence conflicti201 – 2011M → T in BAA05910 (PubMed:7961762).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei591 – 61525Missing in isoform 2. 1 PublicationVSP_024018Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D28560 mRNA. Translation: BAA05910.1.
DQ131564 mRNA. Translation: AAZ99725.1.
BC081747 mRNA. Translation: AAH81747.1.
PIRiA55453.
RefSeqiNP_476445.2. NM_057104.2.
UniGeneiRn.20403.

Genome annotation databases

GeneIDi84050.
KEGGirno:84050.
UCSCiRGD:69298. rat. [Q64610-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D28560 mRNA. Translation: BAA05910.1.
DQ131564 mRNA. Translation: AAZ99725.1.
BC081747 mRNA. Translation: AAH81747.1.
PIRiA55453.
RefSeqiNP_476445.2. NM_057104.2.
UniGeneiRn.20403.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XR9X-ray2.05A36-887[»]
2XRGX-ray3.20A1-887[»]
ProteinModelPortaliQ64610.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4997409.

Chemistry

SwissLipidsiSLP:000000394.

Proteomic databases

PRIDEiQ64610.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi84050.
KEGGirno:84050.
UCSCiRGD:69298. rat. [Q64610-1]

Organism-specific databases

CTDi5168.
RGDi69298. Enpp2.

Phylogenomic databases

HOGENOMiHOG000037439.
HOVERGENiHBG051484.
InParanoidiQ64610.
KOiK01122.
PhylomeDBiQ64610.

Enzyme and pathway databases

BRENDAi3.1.4.39. 5301.
SABIO-RKQ64610.

Miscellaneous databases

EvolutionaryTraceiQ64610.
NextBioi616633.
PROiQ64610.

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. 2 hits.
PTHR10151:SF21. PTHR10151:SF21. 2 hits.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning, expression, and localization of a brain-specific phosphodiesterase I/nucleotide pyrophosphatase (PD-Ialpha) from rat brain."
    Narita M., Goji J., Nakamura H., Sano K.
    J. Biol. Chem. 269:28235-28242(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  2. "The N-terminal hydrophobic sequence of autotaxin (ENPP2) functions as a signal peptide."
    Koike S., Keino-Masu K., Ohto T., Masu M.
    Genes Cells 11:133-142(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 28-32 AND 36-41, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: Sprague-Dawley.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "Autotaxin has lysophospholipase D activity leading to tumor cell growth and motility by lysophosphatidic acid production."
    Umezu-Goto M., Kishi Y., Taira A., Hama K., Dohmae N., Takio K., Yamori T., Mills G.B., Inoue K., Aoki J., Arai H.
    J. Cell Biol. 158:227-233(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  5. "The hydrolysis of lysophospholipids and nucleotides by autotaxin (NPP2) involves a single catalytic site."
    Gijsbers R., Aoki J., Arai H., Bollen M.
    FEBS Lett. 538:60-64(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-171; THR-209; ASP-311 AND HIS-315.
  6. "Proteolytic maturation and activation of autotaxin (NPP2), a secreted metastasis-enhancing lysophospholipase D."
    Jansen S., Stefan C., Creemers J.W., Waelkens E., Van Eynde A., Stalmans W., Bollen M.
    J. Cell Sci. 118:3081-3089(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING, PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION CHARACTERIZATION, SUBCELLULAR LOCATION, MUTAGENESIS OF ILE-13; 16-PHE--PHE-18; 18-PHE--SER-21; 21-SER--ILE-24; 24-ILE--CYS-25 AND 28-PHE--ALA-30.
  7. Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 36-862 IN COMPLEX WITH INHIBITOR AND ZINC IONS, CATALYTIC ACTIVITY, COFACTOR, CALCIUM BINDING, DISULFIDE BONDS, GLYCOSYLATION AT ASN-524, ACTIVE SITE, MUTAGENESIS OF LYS-430 AND 764-ASP--ASP-768, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiENPP2_RAT
AccessioniPrimary (citable) accession number: Q64610
Secondary accession number(s): Q66HQ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: March 20, 2007
Last modified: January 20, 2016
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.