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Q13822

- ENPP2_HUMAN

UniProt

Q13822 - ENPP2_HUMAN

Protein

Ectonucleotide pyrophosphatase/phosphodiesterase family member 2

Gene

ENPP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 3 (02 Mar 2010)
      Previous versions | rss
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    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.3 Publications

    Catalytic activityi

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

    Cofactori

    Binds 2 zinc ions per subunit.By similarity
    Binds 1 calcium ion per subunit.By similarity

    Enzyme regulationi

    Inhibited by lysophosphatidic acid (LPA) and sphingosine-1-phosphate (S1P). Inhibited by EDTA and EGTA Probable.3 Publications

    Kineticsi

    1. KM=0.5 mM for 16:0-LPC (at pH 8.5)2 Publications
    2. KM=5.5 mM for pNP-TMP (at pH 8.5)2 Publications
    3. KM=11.3 mM for pNppp (isoform 1)2 Publications
    4. KM=5.7 mM for pNppp (isoform 2)2 Publications
    5. KM=19.8 mM for pNppp (isoform 3)2 Publications

    Vmax=1.9 nmol/min/µg enzyme with pNppp as substrate (isoform 1)2 Publications

    Vmax=0.67 nmol/min/µg enzyme with pNppp as substrate (isoform 2)2 Publications

    Vmax=1.6 nmol/min/µg enzyme with pNppp as substrate (isoform 3)2 Publications

    pH dependencei

    Optimum pH is 9.0 (isoform 1), 8.0 (isoform 3). Isoform 1 is less sensitive to pH. Isoform 1, isoform 2 and isoform 3 all retain some activity at pH 9.5.2 Publications

    Temperature dependencei

    Isoform 1 and isoform 3 are active from 45 to 60 degrees Celsius.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi172 – 1721Zinc 1; catalyticBy similarity
    Active sitei210 – 2101NucleophileBy similarity
    Metal bindingi210 – 2101Zinc 1; catalyticBy similarity
    Binding sitei231 – 2311SubstrateBy similarity
    Binding sitei307 – 3071SubstrateBy similarity
    Metal bindingi312 – 3121Zinc 2; catalyticBy similarity
    Metal bindingi316 – 3161Zinc 2; catalyticBy similarity
    Metal bindingi316 – 3161Zinc 2; via tele nitrogen; catalyticBy similarity
    Metal bindingi359 – 3591Zinc 1; catalyticBy similarity
    Metal bindingi360 – 3601Zinc 1; catalyticBy similarity
    Metal bindingi360 – 3601Zinc 1; via tele nitrogen; catalyticBy similarity
    Metal bindingi475 – 4751Zinc 2; catalyticBy similarity
    Metal bindingi475 – 4751Zinc 2; via tele nitrogen; catalyticBy similarity
    Metal bindingi740 – 7401CalciumBy similarity
    Metal bindingi744 – 7441CalciumBy similarity
    Metal bindingi746 – 7461Calcium; via carbonyl oxygenBy similarity
    Metal bindingi748 – 7481CalciumBy similarity
    Sitei853 – 8531Essential for catalytic activityBy similarity

    GO - Molecular functioni

    1. alkylglycerophosphoethanolamine phosphodiesterase activity Source: UniProtKB-EC
    2. calcium ion binding Source: UniProtKB
    3. hydrolase activity Source: UniProtKB
    4. lysophospholipase activity Source: UniProtKB
    5. nucleic acid binding Source: InterPro
    6. nucleotide diphosphatase activity Source: ProtInc
    7. phosphodiesterase I activity Source: ProtInc
    8. polysaccharide binding Source: InterPro
    9. scavenger receptor activity Source: InterPro
    10. transcription factor binding Source: ProtInc
    11. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. cellular component movement Source: ProtInc
    2. chemotaxis Source: UniProtKB
    3. G-protein coupled receptor signaling pathway Source: ProtInc
    4. immune response Source: InterPro
    5. nucleic acid phosphodiester bond hydrolysis Source: GOC
    6. phosphate-containing compound metabolic process Source: ProtInc
    7. phosphatidylcholine catabolic process Source: UniProtKB
    8. phospholipid catabolic process Source: UniProt
    9. regulation of cell migration Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Chemotaxis, Lipid degradation, Lipid metabolism

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Enzyme and pathway databases

    SABIO-RKQ13822.

    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, PDNP2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:3357. ENPP2.

    Subcellular locationi

    Secreted 1 Publication
    Note: Secreted by most body fluids including serum and CSF. Also by adipocytes and numerous cancer cells.

    GO - Cellular componenti

    1. extracellular space Source: UniProtKB
    2. integral component of plasma membrane Source: ProtInc
    3. plasma membrane Source: ProtInc

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi170 – 1701S → E: Reduces lysophospholipase activity by about 70%.
    Mutagenesisi210 – 2101T → A: Loss of lysophospholipase activity. 1 Publication
    Mutagenesisi211 – 2111F → Y: Reduces lysophospholipase activity by about 70%. 1 Publication
    Mutagenesisi218 – 2181A → V: Reduces lysophospholipase activity by about 50%. 1 Publication
    Mutagenesisi231 – 2311N → A: Strongly reduced lysophospholipase activity. 1 Publication
    Mutagenesisi307 – 3071Y → Q: Reduces lysophospholipase activity by about 70%. 1 Publication

    Keywords - Diseasei

    Obesity

    Organism-specific databases

    PharmGKBiPA27792.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2727By similarityAdd
    BLAST
    Propeptidei28 – 358Removed by furin2 PublicationsPRO_0000281649
    Chaini36 – 863828Ectonucleotide pyrophosphatase/phosphodiesterase family member 2PRO_0000188567Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi54 – 541N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi59 ↔ 76PROSITE-ProRule annotation
    Disulfide bondi63 ↔ 94PROSITE-ProRule annotation
    Disulfide bondi74 ↔ 87PROSITE-ProRule annotation
    Disulfide bondi80 ↔ 86PROSITE-ProRule annotation
    Disulfide bondi103 ↔ 120PROSITE-ProRule annotation
    Disulfide bondi108 ↔ 138PROSITE-ProRule annotation
    Disulfide bondi118 ↔ 131PROSITE-ProRule annotation
    Disulfide bondi124 ↔ 130PROSITE-ProRule annotation
    Disulfide bondi149 ↔ 195PROSITE-ProRule annotation
    Disulfide bondi157 ↔ 351PROSITE-ProRule annotation
    Disulfide bondi367 ↔ 469PROSITE-ProRule annotation
    Glycosylationi411 – 4111N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi414 ↔ 806PROSITE-ProRule annotation
    Glycosylationi525 – 5251N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi567 ↔ 667PROSITE-ProRule annotation
    Disulfide bondi569 ↔ 652PROSITE-ProRule annotation
    Disulfide bondi775 ↔ 785PROSITE-ProRule annotation
    Glycosylationi807 – 8071N-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

    PaxDbiQ13822.
    PRIDEiQ13822.

    PTM databases

    PhosphoSiteiQ13822.

    Expressioni

    Tissue specificityi

    Predominantly expressed in brain, placenta, ovary, and small intestine. Expressed in a number of carcinomas such as hepatocellular and prostate carcinoma, neuroblastoma and non-small-cell lung cancer. Expressed in body fluids such as plasma, cerebral spinal fluid (CSF), saliva, follicular and amniotic fluids. Not detected in leukocytes. Isoform 1 is more highly expressed in peripheral tissues than in the central nervous system (CNS). Adipocytes only express isoform 1. Isoform 3 is more highly expressed in the brain than in peripheral tissues.3 Publications

    Inductioni

    Up-regulated in massively obese subjects with glucose intolerance, and during adipogenesis.1 Publication

    Gene expression databases

    ArrayExpressiQ13822.
    BgeeiQ13822.
    CleanExiHS_ENPP2.
    GenevestigatoriQ13822.

    Organism-specific databases

    HPAiHPA023700.

    Interactioni

    Protein-protein interaction databases

    BioGridi111194. 2 interactions.
    IntActiQ13822. 1 interaction.
    MINTiMINT-7969086.

    Structurei

    3D structure databases

    ProteinModelPortaliQ13822.
    SMRiQ13822. Positions 52-860.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini55 – 9844SMB 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini99 – 14345SMB 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni211 – 2144Substrate bindingBy similarity
    Regioni244 – 25512Substrate bindingBy similarityAdd
    BLAST
    Regioni830 – 85122Required for secretionBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi127 – 1293Cell attachment siteSequence Analysis

    Sequence similaritiesi

    Contains 2 SMB (somatomedin-B) domains.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG1524.
    HOVERGENiHBG051484.
    KOiK01122.
    OMAiGYGPTFK.
    OrthoDBiEOG7XM2X4.
    PhylomeDBiQ13822.
    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.
    IPR020821. Extracellular_endonuc_su_A.
    IPR002591. Phosphodiest/P_Trfase.
    IPR020436. Somatomedin_B_chordata.
    IPR001212. Somatomedin_B_dom.
    [Graphical view]
    PANTHERiPTHR10151. PTHR10151. 1 hit.
    PfamiPF01223. Endonuclease_NS. 1 hit.
    PF01663. Phosphodiest. 2 hits.
    PF01033. Somatomedin_B. 2 hits.
    [Graphical view]
    PRINTSiPR00022. SOMATOMEDINB.
    SMARTiSM00892. Endonuclease_NS. 1 hit.
    SM00477. NUC. 1 hit.
    SM00201. SO. 2 hits.
    [Graphical view]
    SUPFAMiSSF53649. SSF53649. 1 hit.
    PROSITEiPS00524. SMB_1. 2 hits.
    PS50958. SMB_2. 2 hits.
    [Graphical view]

    Sequences (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. Align

    Isoform 1 (identifier: Q13822-1) [UniParc]FASTAAdd to Basket

    Also known as: ATXter, 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

    MARRSSFQSC QIISLFTFAV GVNICLGFTA HRIKRAEGWE EGPPTVLSDS    50
    PWTNISGSCK GRCFELQEAG PPDCRCDNLC KSYTSCCHDF DELCLKTARG 100
    WECTKDRCGE VRNEENACHC SEDCLARGDC CTNYQVVCKG ESHWVDDDCE 150
    EIKAAECPAG FVRPPLIIFS VDGFRASYMK KGSKVMPNIE KLRSCGTHSP 200
    YMRPVYPTKT FPNLYTLATG LYPESHGIVG NSMYDPVFDA TFHLRGREKF 250
    NHRWWGGQPL WITATKQGVK AGTFFWSVVI PHERRILTIL QWLTLPDHER 300
    PSVYAFYSEQ PDFSGHKYGP FGPEMTNPLR EIDKIVGQLM DGLKQLKLHR 350
    CVNVIFVGDH GMEDVTCDRT EFLSNYLTNV DDITLVPGTL GRIRSKFSNN 400
    AKYDPKAIIA NLTCKKPDQH FKPYLKQHLP KRLHYANNRR IEDIHLLVER 450
    RWHVARKPLD VYKKPSGKCF FQGDHGFDNK VNSMQTVFVG YGSTFKYKTK 500
    VPPFENIELY NVMCDLLGLK PAPNNGTHGS LNHLLRTNTF RPTMPEEVTR 550
    PNYPGIMYLQ SDFDLGCTCD DKVEPKNKLD ELNKRLHTKG STEERHLLYG 600
    RPAVLYRTRY DILYHTDFES GYSEIFLMPL WTSYTVSKQA EVSSVPDHLT 650
    SCVRPDVRVS PSFSQNCLAY KNDKQMSYGF LFPPYLSSSP EAKYDAFLVT 700
    NMVPMYPAFK RVWNYFQRVL VKKYASERNG VNVISGPIFD YDYDGLHDTE 750
    DKIKQYVEGS SIPVPTHYYS IITSCLDFTQ PADKCDGPLS VSSFILPHRP 800
    DNEESCNSSE DESKWVEELM KMHTARVRDI EHLTSLDFFR KTSRSYPEIL 850
    TLKTYLHTYE SEI 863
    Length:863
    Mass (Da):98,994
    Last modified:March 2, 2010 - v3
    Checksum:i94A7A2B3701F0993
    GO
    Isoform 2 (identifier: Q13822-2) [UniParc]FASTAAdd to Basket

    Also known as: ATXmel, Alpha

    The sequence of this isoform differs from the canonical sequence as follows:
         324-324: E → EESSYGSPFTPAKRPKRKVAPKRRQERPVAPPKKRRRKIHRMDHYAAETRQDK

    Show »
    Length:915
    Mass (Da):105,201
    Checksum:i30C7CB1E60101B75
    GO
    Isoform 3 (identifier: Q13822-3) [UniParc]FASTAAdd to Basket

    Also known as: Gamma

    The sequence of this isoform differs from the canonical sequence as follows:
         593-593: E → EAETRKFRGSRNENKENINGNFEPRK

    Show »
    Length:888
    Mass (Da):101,968
    Checksum:i17A8986783028C4D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti23 – 231N → S in AAA64785. (PubMed:7982964)Curated
    Sequence conflicti23 – 231N → S in ABW38316. (PubMed:18175805)Curated
    Sequence conflicti73 – 731D → H in BAA08260. (PubMed:8586446)Curated
    Sequence conflicti100 – 1001G → A in AAB00855. (PubMed:8579579)Curated
    Sequence conflicti291 – 2911Q → R in AAA64785. (PubMed:7982964)Curated
    Sequence conflicti291 – 2911Q → R in ABW38316. (PubMed:18175805)Curated
    Sequence conflicti349 – 3491H → R in AAA64785. (PubMed:7982964)Curated
    Sequence conflicti349 – 3491H → R in ABW38316. (PubMed:18175805)Curated
    Sequence conflicti457 – 4571K → P AA sequence (PubMed:1733949)Curated
    Sequence conflicti501 – 5011V → S AA sequence (PubMed:1733949)Curated
    Sequence conflicti508 – 5081E → N AA sequence (PubMed:1733949)Curated
    Sequence conflicti554 – 5541P → L AA sequence (PubMed:1733949)Curated
    Sequence conflicti629 – 6291P → L in AAA64785. (PubMed:7982964)Curated
    Sequence conflicti629 – 6291P → L in ABW38316. (PubMed:18175805)Curated
    Sequence conflicti644 – 6441S → R in BAA08260. (PubMed:8586446)Curated
    Sequence conflicti703 – 7031V → A in BAA08260. (PubMed:8586446)Curated
    Sequence conflicti769 – 7691Y → H in BAA08260. (PubMed:8586446)Curated
    Isoform 3 (identifier: Q13822-3)
    Sequence conflicti23 – 231N → S in ABW38316. (PubMed:18175805)Curated
    Sequence conflicti291 – 2911Q → R in ABW38316. (PubMed:18175805)Curated
    Sequence conflicti349 – 3491H → R in ABW38316. (PubMed:18175805)Curated
    Sequence conflicti493 – 4931S → P in ABW38316. (PubMed:18175805)Curated
    Sequence conflicti599 – 5991F → Y in ABW38316. (PubMed:18175805)Curated
    Sequence conflicti602 – 6021S → T in ABW38316. (PubMed:18175805)Curated
    Sequence conflicti654 – 6541P → L in ABW38316. (PubMed:18175805)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti493 – 4931S → P.7 Publications
    Corresponds to variant rs10283100 [ dbSNP | Ensembl ].
    VAR_060469
    Natural varianti577 – 5771N → S.
    Corresponds to variant rs2289886 [ dbSNP | Ensembl ].
    VAR_057472
    Natural varianti726 – 7261S → L.
    Corresponds to variant rs16892767 [ dbSNP | Ensembl ].
    VAR_057473

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei324 – 3241E → EESSYGSPFTPAKRPKRKVA PKRRQERPVAPPKKRRRKIH RMDHYAAETRQDK in isoform 2. 2 PublicationsVSP_006750
    Alternative sequencei593 – 5931E → EAETRKFRGSRNENKENING NFEPRK in isoform 3. 1 PublicationVSP_036398

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L35594 mRNA. Translation: AAA64785.1.
    D45421 mRNA. Translation: BAA08260.1.
    D45914 Genomic DNA. Translation: BAA08342.1.
    L46720 mRNA. Translation: AAB00855.1.
    EU131011 mRNA. Translation: ABW38316.2.
    AC099818 Genomic DNA. No translation available.
    AC107960 Genomic DNA. No translation available.
    BC034961 mRNA. Translation: AAH34961.1.
    CCDSiCCDS34936.1. [Q13822-1]
    CCDS47914.1. [Q13822-3]
    CCDS6329.1. [Q13822-2]
    PIRiA55144.
    RefSeqiNP_001035181.1. NM_001040092.2. [Q13822-1]
    NP_001124335.1. NM_001130863.2. [Q13822-3]
    NP_006200.3. NM_006209.4. [Q13822-2]
    UniGeneiHs.190977.

    Genome annotation databases

    EnsembliENST00000075322; ENSP00000075322; ENSG00000136960. [Q13822-1]
    ENST00000259486; ENSP00000259486; ENSG00000136960. [Q13822-2]
    ENST00000522826; ENSP00000428291; ENSG00000136960. [Q13822-3]
    GeneIDi5168.
    KEGGihsa:5168.
    UCSCiuc003yos.2. human. [Q13822-2]
    uc003yot.2. human. [Q13822-1]

    Polymorphism databases

    DMDMi290457674.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L35594 mRNA. Translation: AAA64785.1 .
    D45421 mRNA. Translation: BAA08260.1 .
    D45914 Genomic DNA. Translation: BAA08342.1 .
    L46720 mRNA. Translation: AAB00855.1 .
    EU131011 mRNA. Translation: ABW38316.2 .
    AC099818 Genomic DNA. No translation available.
    AC107960 Genomic DNA. No translation available.
    BC034961 mRNA. Translation: AAH34961.1 .
    CCDSi CCDS34936.1. [Q13822-1 ]
    CCDS47914.1. [Q13822-3 ]
    CCDS6329.1. [Q13822-2 ]
    PIRi A55144.
    RefSeqi NP_001035181.1. NM_001040092.2. [Q13822-1 ]
    NP_001124335.1. NM_001130863.2. [Q13822-3 ]
    NP_006200.3. NM_006209.4. [Q13822-2 ]
    UniGenei Hs.190977.

    3D structure databases

    ProteinModelPortali Q13822.
    SMRi Q13822. Positions 52-860.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111194. 2 interactions.
    IntActi Q13822. 1 interaction.
    MINTi MINT-7969086.

    Chemistry

    ChEMBLi CHEMBL3691.

    PTM databases

    PhosphoSitei Q13822.

    Polymorphism databases

    DMDMi 290457674.

    Proteomic databases

    PaxDbi Q13822.
    PRIDEi Q13822.

    Protocols and materials databases

    DNASUi 5168.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000075322 ; ENSP00000075322 ; ENSG00000136960 . [Q13822-1 ]
    ENST00000259486 ; ENSP00000259486 ; ENSG00000136960 . [Q13822-2 ]
    ENST00000522826 ; ENSP00000428291 ; ENSG00000136960 . [Q13822-3 ]
    GeneIDi 5168.
    KEGGi hsa:5168.
    UCSCi uc003yos.2. human. [Q13822-2 ]
    uc003yot.2. human. [Q13822-1 ]

    Organism-specific databases

    CTDi 5168.
    GeneCardsi GC08M120569.
    H-InvDB HIX0025550.
    HGNCi HGNC:3357. ENPP2.
    HPAi HPA023700.
    MIMi 601060. gene.
    neXtProti NX_Q13822.
    PharmGKBi PA27792.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1524.
    HOVERGENi HBG051484.
    KOi K01122.
    OMAi GYGPTFK.
    OrthoDBi EOG7XM2X4.
    PhylomeDBi Q13822.
    TreeFami TF330032.

    Enzyme and pathway databases

    SABIO-RK Q13822.

    Miscellaneous databases

    ChiTaRSi ENPP2. human.
    GeneWikii Autotaxin.
    GenomeRNAii 5168.
    NextBioi 19994.
    PROi Q13822.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13822.
    Bgeei Q13822.
    CleanExi HS_ENPP2.
    Genevestigatori Q13822.

    Family and domain databases

    Gene3Di 3.40.570.10. 1 hit.
    3.40.720.10. 1 hit.
    InterProi IPR017849. 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 ]
    PANTHERi PTHR10151. PTHR10151. 1 hit.
    Pfami PF01223. Endonuclease_NS. 1 hit.
    PF01663. Phosphodiest. 2 hits.
    PF01033. Somatomedin_B. 2 hits.
    [Graphical view ]
    PRINTSi PR00022. SOMATOMEDINB.
    SMARTi SM00892. Endonuclease_NS. 1 hit.
    SM00477. NUC. 1 hit.
    SM00201. SO. 2 hits.
    [Graphical view ]
    SUPFAMi SSF53649. SSF53649. 1 hit.
    PROSITEi PS00524. SMB_1. 2 hits.
    PS50958. SMB_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNA cloning of the human tumor motility-stimulating protein, autotaxin, reveals a homology with phosphodiesterases."
      Murata J., Lee H.Y., Clair T., Krutzsch H.C., Arestad A.A., Sobel M.E., Liotta L.A., Stracke M.L.
      J. Biol. Chem. 269:30479-30484(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION, VARIANT PRO-493.
      Tissue: Melanoma.
    2. "Molecular cloning and chromosomal assignment of the human brain-type phosphodiesterase I/nucleotide pyrophosphatase gene (PDNP2)."
      Kawagoe H., Soma O., Goji J., Nishimura N., Narita M., Inazawa J., Nakamura H., Sano K.
      Genomics 30:380-384(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45, TISSUE SPECIFICITY, VARIANT PRO-493.
    3. "Cloning, chromosomal localization, and tissue expression of autotaxin from human teratocarcinoma cells."
      Lee H.Y., Murata J., Clair T., Polymeropoulos M.H., Torres R., Manrow R.E., Liotta L.A., Stracke M.L.
      Biochem. Biophys. Res. Commun. 218:714-719(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANT PRO-493.
      Tissue: Teratocarcinoma.
    4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, ENZYME REGULATION, VARIANT PRO-493.
    5. "Murine and human autotaxin alpha, beta, and gamma isoforms: gene organization, tissue distribution, and biochemical characterization."
      Giganti A., Rodriguez M., Fould B., Moulharat N., Coge F., Chomarat P., Galizzi J.-P., Valet P., Saulnier-Blache J.-S., Boutin J.A., Ferry G.
      J. Biol. Chem. 283:7776-7789(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), PROTEIN SEQUENCE OF 36-42 AND 49-54, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, VARIANT PRO-493.
      Tissue: Brain and Melanoma.
    6. "DNA sequence and analysis of human chromosome 8."
      Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
      , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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), VARIANT PRO-493.
      Tissue: Testis.
    8. "Identification of human plasma lysophospholipase D, a lysophosphatidic acid-producing enzyme, as autotaxin, a multifunctional phosphodiesterase."
      Tokumura A., Majima E., Kariya Y., Tominaga K., Kogure K., Yasuda K., Fukuzawa K.
      J. Biol. Chem. 277:39436-39442(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 36-49; 318-330; 335-344; 440-450 AND 854-863, IDENTIFICATION, BIOPHYSICOCHEMICAL PROPERTIES.
    9. "Identification, purification, and partial sequence analysis of autotaxin, a novel motility-stimulating protein."
      Stracke M.L., Krutzsch H.C., Unsworth E.J., Aarestad A., Cioce V., Schiffmann E., Liotta L.A.
      J. Biol. Chem. 267:2524-2529(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 256-266; 370-392; 457-463; 481-496; 501-510; 545-554; 639-643; 706-710 AND 829-840, FUNCTION, VARIANT PRO-493.
      Tissue: Melanoma.
    10. "Autotaxin (NPP-2), a metastasis-enhancing mitogen, is an angiogenic factor."
      Nam S.W., Clair T., Kim Y.S., McMarlin A., Schiffmann E., Liotta L.A., Stracke M.L.
      Cancer Res. 61:6938-6944(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ANGIOGENESIS.
    11. "Potential involvement of adipocyte insulin resistance in obesity-associated up-regulation of adipocyte lysophospholipase D/autotaxin expression."
      Boucher J., Quilliot D., Pradere J.P., Simon M.F., Gres S., Guigne C., Prevot D., Ferry G., Boutin J.A., Carpene C., Valet P., Saulnier-Blache J.S.
      Diabetologia 48:569-577(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, POSSIBLE FUNCTION IN OBESITY.
    12. Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, MUTAGENESIS OF THR-210; PHE-211; ALA-218; ASN-231 AND TYR-307.

    Entry informationi

    Entry nameiENPP2_HUMAN
    AccessioniPrimary (citable) accession number: Q13822
    Secondary accession number(s): A8UHA1
    , E9PHP7, Q13827, Q14555, Q15117, Q9UCQ8, Q9UCR0, Q9UCR1, Q9UCR2, Q9UCR3, Q9UCR4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2002
    Last sequence update: March 2, 2010
    Last modified: October 1, 2014
    This is version 137 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3