UniProtKB - Q64610 (ENPP2_RAT)
(max 400 entries)
Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>
Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)
>sp|Q64610|ENPP2_RAT Ectonucleotide pyrophosphatase/phosphodiesterase family member 2 OS=Rattus norvegicus OX=10116 GN=Enpp2 PE=1 SV=2 MARQGCLGSFQVISLFTFAISVNICLGFTASRIKRAEWDEGPPTVLSDSPWTNTSGSCKG RCFELQEVGPPDCRCDNLCKSYSSCCHDFDELCLKTARGWECTKDRCGEVRNEENACHCS EDCLSRGDCCTNYQVVCKGESHWVDDDCEEIKVPECPAGFVRPPLIIFSVDGFRASYMKK GSKVMPNIEKLRSCGTHAPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDAS FHLRGREKFNHRWWGGQPLWITATKQGVRAGTFFWSVSIPHERRILTILQWLSLPDNERP SVYAFYSEQPDFSGHKYGPFGPEMTNPLREIDKTVGQLMDGLKQLRLHRCVNVIFVGDHG MEDVTCDRTEFLSNYLTNVDDITLVPGTLGRIRAKSINNSKYDPKTIIANLTCKKPDQHF KPYMKQHLPKRLHYANNRRIEDIHLLVDRRWHVARKPLDVYKKPSGKCFFQGDHGFDNKV NSMQTVFVGYGPTFKYRTKVPPFENIELYNVMCDLLGLKPAPNNGTHGSLNHLLRTNTFR PTMPDEVSRPNYPGIMYLQSEFDLGCTCDDKVEPKNKLEELNKRLHTKGSTEAETGKFRG SKHENKKNLNGSVEPRKERHLLYGRPAVLYRTSYDILYHTDFESGYSEIFLMPLWTSYTI SKQAEVSSIPEHLTNCVRPDVRVSPGFSQNCLAYKNDKQMSYGFLFPPYLSSSPEAKYDA FLVTNMVPMYPAFKRVWAYFQRVLVKKYASERNGVNVISGPIFDYNYDGLRDTEDEIKQY VEGSSIPVPTHYYSIITSCLDFTQPADKCDGPLSVSSFILPHRPDNDESCNSSEDESKWV EELMKMHTARVRDIEHLTGLDFYRKTSRSYSEILTLKTYLHTYESEIHelp videoAdd a publicationFeedback
Protein
Ectonucleotide pyrophosphatase/phosphodiesterase family member 2
Gene
Enpp2
Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
Hydrolyzes lysophospholipids to produce the signaling molecule lysophosphatidic acid (LPA) in extracellular fluids (PubMed:12633853, PubMed:29259743, PubMed:27660691, PubMed:27268273, PubMed:27075612). Major substrate is lysophosphatidylcholine (PubMed:12119361, PubMed:27660691, PubMed:27268273, PubMed:27075612). Also can act on sphingosylphosphorylcholine producing sphingosine-1-phosphate, a modulator of cell motility (PubMed:12119361). Can hydrolyze, in vitro, bis-pNPP, to some extent pNP-TMP, and barely ATP (PubMed:12633853, PubMed:27268273). 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 (By similarity).By similarity
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
7 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.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, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION. - Ref.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: CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-171; THR-209; ASP-311 AND HIS-315, ACTIVE SITE. - Ref.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. - Ref.7"Discovery of BI-2545: A Novel Autotaxin Inhibitor That Significantly Reduces LPA Levels in Vivo."
Kuttruff C.A., Ferrara M., Bretschneider T., Hoerer S., Handschuh S., Nosse B., Romig H., Nicklin P., Roth G.J.
ACS Med. Chem. Lett. 8:1252-1257(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY. - Ref.9"Novel Autotaxin Inhibitors for the Treatment of Osteoarthritis Pain: Lead Optimization via Structure-Based Drug Design."
Jones S.B., Pfeifer L.A., Bleisch T.J., Beauchamp T.J., Durbin J.D., Klimkowski V.J., Hughes N.E., Rito C.J., Dao Y., Gruber J.M., Bui H., Chambers M.G., Chandrasekhar S., Lin C., McCann D.J., Mudra D.R., Oskins J.L., Swearingen C.A., Thirunavukkarasu K., Norman B.H.
ACS Med. Chem. Lett. 7:857-861(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) IN COMPLEX WITH INHIBITOR; CALCIUM AND ZINC, CATALYTIC ACTIVITY, COFACTOR, FUNCTION, GLYCOSYLATION AT ASN-410 AND ASN-524, DISULFIDE BONDS. - Ref.10"Structural snapshots of the catalytic cycle of the phosphodiesterase Autotaxin."
Hausmann J., Keune W.J., Hipgrave Ederveen A.L., van Zeijl L., Joosten R.P., Perrakis A.
J. Struct. Biol. 195:199-206(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 36-887 IN COMPLEXES WITH PHOSPHATE; VANADATE; HYDROXYCHOLESTEROL; CALCIUM AND ZINC, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, COFACTOR, ACTIVE SITE, GLYCOSYLATION AT ASN-524, DISULFIDE BONDS. - Ref.11"Steroid binding to Autotaxin links bile salts and lysophosphatidic acid signalling."
Keune W.J., Hausmann J., Bolier R., Tolenaars D., Kremer A., Heidebrecht T., Joosten R.P., Sunkara M., Morris A.J., Matas-Rico E., Moolenaar W.H., Oude Elferink R.P., Perrakis A.
Nat. Commun. 7:11248-11248(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 36-887 IN COMPLEXES WITH OLEOYL LYSOPHOSPHATIDIC ACID; STEROIDS; CALCIUM AND ZINC, CATALYTIC ACTIVITY, FUNCTION, ACTIVITY REGULATION, COFACTOR, GLYCOSYLATION AT ASN-524, DISULFIDE BONDS.
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
- 1-O-alkyl-sn-glycero-3-phosphoethanolamineEC:3.1.4.39
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.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, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION. - Ref.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: CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-171; THR-209; ASP-311 AND HIS-315, ACTIVE SITE. - Ref.7"Discovery of BI-2545: A Novel Autotaxin Inhibitor That Significantly Reduces LPA Levels in Vivo."
Kuttruff C.A., Ferrara M., Bretschneider T., Hoerer S., Handschuh S., Nosse B., Romig H., Nicklin P., Roth G.J.
ACS Med. Chem. Lett. 8:1252-1257(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY. - Ref.8"Structural basis of substrate discrimination and integrin binding by autotaxin."
Hausmann J., Kamtekar S., Christodoulou E., Day J.E., Wu T., Fulkerson Z., Albers H.M., van Meeteren L.A., Houben A.J., van Zeijl L., Jansen S., Andries M., Hall T., Pegg L.E., Benson T.E., Kasiem M., Harlos K., Kooi C.W. , Smyth S.S., Ovaa H., Bollen M., Morris A.J., Moolenaar W.H., Perrakis A.
Nat. Struct. Mol. Biol. 18:198-204(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 36-862 IN COMPLEX WITH INHIBITOR; CALCIUM 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. - Ref.9"Novel Autotaxin Inhibitors for the Treatment of Osteoarthritis Pain: Lead Optimization via Structure-Based Drug Design."
Jones S.B., Pfeifer L.A., Bleisch T.J., Beauchamp T.J., Durbin J.D., Klimkowski V.J., Hughes N.E., Rito C.J., Dao Y., Gruber J.M., Bui H., Chambers M.G., Chandrasekhar S., Lin C., McCann D.J., Mudra D.R., Oskins J.L., Swearingen C.A., Thirunavukkarasu K., Norman B.H.
ACS Med. Chem. Lett. 7:857-861(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) IN COMPLEX WITH INHIBITOR; CALCIUM AND ZINC, CATALYTIC ACTIVITY, COFACTOR, FUNCTION, GLYCOSYLATION AT ASN-410 AND ASN-524, DISULFIDE BONDS. - Ref.10"Structural snapshots of the catalytic cycle of the phosphodiesterase Autotaxin."
Hausmann J., Keune W.J., Hipgrave Ederveen A.L., van Zeijl L., Joosten R.P., Perrakis A.
J. Struct. Biol. 195:199-206(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 36-887 IN COMPLEXES WITH PHOSPHATE; VANADATE; HYDROXYCHOLESTEROL; CALCIUM AND ZINC, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, COFACTOR, ACTIVE SITE, GLYCOSYLATION AT ASN-524, DISULFIDE BONDS. - Ref.11"Steroid binding to Autotaxin links bile salts and lysophosphatidic acid signalling."
Keune W.J., Hausmann J., Bolier R., Tolenaars D., Kremer A., Heidebrecht T., Joosten R.P., Sunkara M., Morris A.J., Matas-Rico E., Moolenaar W.H., Oude Elferink R.P., Perrakis A.
Nat. Commun. 7:11248-11248(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 36-887 IN COMPLEXES WITH OLEOYL LYSOPHOSPHATIDIC ACID; STEROIDS; CALCIUM AND ZINC, CATALYTIC ACTIVITY, FUNCTION, ACTIVITY REGULATION, COFACTOR, GLYCOSYLATION AT ASN-524, DISULFIDE BONDS.
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
Manual assertion based on experiment ini
- Ref.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, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION. - Ref.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: CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-171; THR-209; ASP-311 AND HIS-315, ACTIVE SITE. - Ref.7"Discovery of BI-2545: A Novel Autotaxin Inhibitor That Significantly Reduces LPA Levels in Vivo."
Kuttruff C.A., Ferrara M., Bretschneider T., Hoerer S., Handschuh S., Nosse B., Romig H., Nicklin P., Roth G.J.
ACS Med. Chem. Lett. 8:1252-1257(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY. - Ref.8"Structural basis of substrate discrimination and integrin binding by autotaxin."
Hausmann J., Kamtekar S., Christodoulou E., Day J.E., Wu T., Fulkerson Z., Albers H.M., van Meeteren L.A., Houben A.J., van Zeijl L., Jansen S., Andries M., Hall T., Pegg L.E., Benson T.E., Kasiem M., Harlos K., Kooi C.W. , Smyth S.S., Ovaa H., Bollen M., Morris A.J., Moolenaar W.H., Perrakis A.
Nat. Struct. Mol. Biol. 18:198-204(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 36-862 IN COMPLEX WITH INHIBITOR; CALCIUM 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. - Ref.9"Novel Autotaxin Inhibitors for the Treatment of Osteoarthritis Pain: Lead Optimization via Structure-Based Drug Design."
Jones S.B., Pfeifer L.A., Bleisch T.J., Beauchamp T.J., Durbin J.D., Klimkowski V.J., Hughes N.E., Rito C.J., Dao Y., Gruber J.M., Bui H., Chambers M.G., Chandrasekhar S., Lin C., McCann D.J., Mudra D.R., Oskins J.L., Swearingen C.A., Thirunavukkarasu K., Norman B.H.
ACS Med. Chem. Lett. 7:857-861(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) IN COMPLEX WITH INHIBITOR; CALCIUM AND ZINC, CATALYTIC ACTIVITY, COFACTOR, FUNCTION, GLYCOSYLATION AT ASN-410 AND ASN-524, DISULFIDE BONDS. - Ref.10"Structural snapshots of the catalytic cycle of the phosphodiesterase Autotaxin."
Hausmann J., Keune W.J., Hipgrave Ederveen A.L., van Zeijl L., Joosten R.P., Perrakis A.
J. Struct. Biol. 195:199-206(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 36-887 IN COMPLEXES WITH PHOSPHATE; VANADATE; HYDROXYCHOLESTEROL; CALCIUM AND ZINC, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, COFACTOR, ACTIVE SITE, GLYCOSYLATION AT ASN-524, DISULFIDE BONDS. - Ref.11"Steroid binding to Autotaxin links bile salts and lysophosphatidic acid signalling."
Keune W.J., Hausmann J., Bolier R., Tolenaars D., Kremer A., Heidebrecht T., Joosten R.P., Sunkara M., Morris A.J., Matas-Rico E., Moolenaar W.H., Oude Elferink R.P., Perrakis A.
Nat. Commun. 7:11248-11248(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 36-887 IN COMPLEXES WITH OLEOYL LYSOPHOSPHATIDIC ACID; STEROIDS; CALCIUM AND ZINC, CATALYTIC ACTIVITY, FUNCTION, ACTIVITY REGULATION, COFACTOR, GLYCOSYLATION AT ASN-524, DISULFIDE BONDS.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
1-O-alkyl-sn-glycero-3-phosphoethanolamine- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
zoom
+H2O- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
=1-O-alkyl-sn-glycero-3-phosphate- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
zoom
+ethanolamine- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
zoom
+H+- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori
Protein has several cofactor binding sites:- Zn2+
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.8"Structural basis of substrate discrimination and integrin binding by autotaxin."
Hausmann J., Kamtekar S., Christodoulou E., Day J.E., Wu T., Fulkerson Z., Albers H.M., van Meeteren L.A., Houben A.J., van Zeijl L., Jansen S., Andries M., Hall T., Pegg L.E., Benson T.E., Kasiem M., Harlos K., Kooi C.W. , Smyth S.S., Ovaa H., Bollen M., Morris A.J., Moolenaar W.H., Perrakis A.
Nat. Struct. Mol. Biol. 18:198-204(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 36-862 IN COMPLEX WITH INHIBITOR; CALCIUM 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. - Ref.10"Structural snapshots of the catalytic cycle of the phosphodiesterase Autotaxin."
Hausmann J., Keune W.J., Hipgrave Ederveen A.L., van Zeijl L., Joosten R.P., Perrakis A.
J. Struct. Biol. 195:199-206(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 36-887 IN COMPLEXES WITH PHOSPHATE; VANADATE; HYDROXYCHOLESTEROL; CALCIUM AND ZINC, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, COFACTOR, ACTIVE SITE, GLYCOSYLATION AT ASN-524, DISULFIDE BONDS. - Ref.11"Steroid binding to Autotaxin links bile salts and lysophosphatidic acid signalling."
Keune W.J., Hausmann J., Bolier R., Tolenaars D., Kremer A., Heidebrecht T., Joosten R.P., Sunkara M., Morris A.J., Matas-Rico E., Moolenaar W.H., Oude Elferink R.P., Perrakis A.
Nat. Commun. 7:11248-11248(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 36-887 IN COMPLEXES WITH OLEOYL LYSOPHOSPHATIDIC ACID; STEROIDS; CALCIUM AND ZINC, CATALYTIC ACTIVITY, FUNCTION, ACTIVITY REGULATION, COFACTOR, GLYCOSYLATION AT ASN-524, DISULFIDE BONDS.
Manual assertion based on experiment ini
- Ref.8"Structural basis of substrate discrimination and integrin binding by autotaxin."
Hausmann J., Kamtekar S., Christodoulou E., Day J.E., Wu T., Fulkerson Z., Albers H.M., van Meeteren L.A., Houben A.J., van Zeijl L., Jansen S., Andries M., Hall T., Pegg L.E., Benson T.E., Kasiem M., Harlos K., Kooi C.W. , Smyth S.S., Ovaa H., Bollen M., Morris A.J., Moolenaar W.H., Perrakis A.
Nat. Struct. Mol. Biol. 18:198-204(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 36-862 IN COMPLEX WITH INHIBITOR; CALCIUM 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. - Ref.10"Structural snapshots of the catalytic cycle of the phosphodiesterase Autotaxin."
Hausmann J., Keune W.J., Hipgrave Ederveen A.L., van Zeijl L., Joosten R.P., Perrakis A.
J. Struct. Biol. 195:199-206(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 36-887 IN COMPLEXES WITH PHOSPHATE; VANADATE; HYDROXYCHOLESTEROL; CALCIUM AND ZINC, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, COFACTOR, ACTIVE SITE, GLYCOSYLATION AT ASN-524, DISULFIDE BONDS. - Ref.11"Steroid binding to Autotaxin links bile salts and lysophosphatidic acid signalling."
Keune W.J., Hausmann J., Bolier R., Tolenaars D., Kremer A., Heidebrecht T., Joosten R.P., Sunkara M., Morris A.J., Matas-Rico E., Moolenaar W.H., Oude Elferink R.P., Perrakis A.
Nat. Commun. 7:11248-11248(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 36-887 IN COMPLEXES WITH OLEOYL LYSOPHOSPHATIDIC ACID; STEROIDS; CALCIUM AND ZINC, CATALYTIC ACTIVITY, FUNCTION, ACTIVITY REGULATION, COFACTOR, GLYCOSYLATION AT ASN-524, DISULFIDE BONDS.
- Ca2+
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.8"Structural basis of substrate discrimination and integrin binding by autotaxin."
Hausmann J., Kamtekar S., Christodoulou E., Day J.E., Wu T., Fulkerson Z., Albers H.M., van Meeteren L.A., Houben A.J., van Zeijl L., Jansen S., Andries M., Hall T., Pegg L.E., Benson T.E., Kasiem M., Harlos K., Kooi C.W. , Smyth S.S., Ovaa H., Bollen M., Morris A.J., Moolenaar W.H., Perrakis A.
Nat. Struct. Mol. Biol. 18:198-204(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 36-862 IN COMPLEX WITH INHIBITOR; CALCIUM 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. - Ref.10"Structural snapshots of the catalytic cycle of the phosphodiesterase Autotaxin."
Hausmann J., Keune W.J., Hipgrave Ederveen A.L., van Zeijl L., Joosten R.P., Perrakis A.
J. Struct. Biol. 195:199-206(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 36-887 IN COMPLEXES WITH PHOSPHATE; VANADATE; HYDROXYCHOLESTEROL; CALCIUM AND ZINC, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, COFACTOR, ACTIVE SITE, GLYCOSYLATION AT ASN-524, DISULFIDE BONDS. - Ref.11"Steroid binding to Autotaxin links bile salts and lysophosphatidic acid signalling."
Keune W.J., Hausmann J., Bolier R., Tolenaars D., Kremer A., Heidebrecht T., Joosten R.P., Sunkara M., Morris A.J., Matas-Rico E., Moolenaar W.H., Oude Elferink R.P., Perrakis A.
Nat. Commun. 7:11248-11248(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 36-887 IN COMPLEXES WITH OLEOYL LYSOPHOSPHATIDIC ACID; STEROIDS; CALCIUM AND ZINC, CATALYTIC ACTIVITY, FUNCTION, ACTIVITY REGULATION, COFACTOR, GLYCOSYLATION AT ASN-524, DISULFIDE BONDS.
Manual assertion based on experiment ini
- Ref.8"Structural basis of substrate discrimination and integrin binding by autotaxin."
Hausmann J., Kamtekar S., Christodoulou E., Day J.E., Wu T., Fulkerson Z., Albers H.M., van Meeteren L.A., Houben A.J., van Zeijl L., Jansen S., Andries M., Hall T., Pegg L.E., Benson T.E., Kasiem M., Harlos K., Kooi C.W. , Smyth S.S., Ovaa H., Bollen M., Morris A.J., Moolenaar W.H., Perrakis A.
Nat. Struct. Mol. Biol. 18:198-204(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 36-862 IN COMPLEX WITH INHIBITOR; CALCIUM 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. - Ref.10"Structural snapshots of the catalytic cycle of the phosphodiesterase Autotaxin."
Hausmann J., Keune W.J., Hipgrave Ederveen A.L., van Zeijl L., Joosten R.P., Perrakis A.
J. Struct. Biol. 195:199-206(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 36-887 IN COMPLEXES WITH PHOSPHATE; VANADATE; HYDROXYCHOLESTEROL; CALCIUM AND ZINC, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, COFACTOR, ACTIVE SITE, GLYCOSYLATION AT ASN-524, DISULFIDE BONDS. - Ref.11"Steroid binding to Autotaxin links bile salts and lysophosphatidic acid signalling."
Keune W.J., Hausmann J., Bolier R., Tolenaars D., Kremer A., Heidebrecht T., Joosten R.P., Sunkara M., Morris A.J., Matas-Rico E., Moolenaar W.H., Oude Elferink R.P., Perrakis A.
Nat. Commun. 7:11248-11248(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 36-887 IN COMPLEXES WITH OLEOYL LYSOPHOSPHATIDIC ACID; STEROIDS; CALCIUM AND ZINC, CATALYTIC ACTIVITY, FUNCTION, ACTIVITY REGULATION, COFACTOR, GLYCOSYLATION AT ASN-524, DISULFIDE BONDS.
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi
Inhibited by vanadate (PubMed:27268273). Inhibited by micromolar levels of bile salts, such as tauroursodeoxycholate. Not inhibited by taurodeoxycholate. Not inhibited by hydroxysterols, such as 7-hydroxycholesterol, testosterone, dexamethasone and prednisolone (PubMed:27075612).2 Publications
Manual assertion based on experiment ini
- Ref.10"Structural snapshots of the catalytic cycle of the phosphodiesterase Autotaxin."
Hausmann J., Keune W.J., Hipgrave Ederveen A.L., van Zeijl L., Joosten R.P., Perrakis A.
J. Struct. Biol. 195:199-206(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 36-887 IN COMPLEXES WITH PHOSPHATE; VANADATE; HYDROXYCHOLESTEROL; CALCIUM AND ZINC, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, COFACTOR, ACTIVE SITE, GLYCOSYLATION AT ASN-524, DISULFIDE BONDS. - Ref.11"Steroid binding to Autotaxin links bile salts and lysophosphatidic acid signalling."
Keune W.J., Hausmann J., Bolier R., Tolenaars D., Kremer A., Heidebrecht T., Joosten R.P., Sunkara M., Morris A.J., Matas-Rico E., Moolenaar W.H., Oude Elferink R.P., Perrakis A.
Nat. Commun. 7:11248-11248(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 36-887 IN COMPLEXES WITH OLEOYL LYSOPHOSPHATIDIC ACID; STEROIDS; CALCIUM AND ZINC, CATALYTIC ACTIVITY, FUNCTION, ACTIVITY REGULATION, COFACTOR, GLYCOSYLATION AT ASN-524, DISULFIDE BONDS.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 171 | Zinc 1; catalyticCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 4 PublicationsManual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 209 | Nucleophile2 Publications Manual assertion based on experiment ini
| 1 | |
| Metal bindingi | 209 | Zinc 1; catalyticCombined sources Manual assertion inferred from combination of experimental and computational evidencei 4 PublicationsManual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 230 | SubstrateCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 Publication<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
| 1 | |
| Binding sitei | 306 | SubstrateCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion inferred by curator fromi
| 1 | |
| Metal bindingi | 311 | Zinc 2; catalyticCombined sources Manual assertion inferred from combination of experimental and computational evidencei 4 PublicationsManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 315 | Zinc 2; via tele nitrogen; catalyticCombined sources Manual assertion inferred from combination of experimental and computational evidencei 4 PublicationsManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 358 | Zinc 1; catalyticCombined sources Manual assertion inferred from combination of experimental and computational evidencei 4 PublicationsManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 359 | Zinc 1; via tele nitrogen; catalyticCombined sources Manual assertion inferred from combination of experimental and computational evidencei 4 PublicationsManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 474 | Zinc 2; via tele nitrogen; catalyticCombined sources Manual assertion inferred from combination of experimental and computational evidencei 4 PublicationsManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 764 | CalciumCombined sources Manual assertion inferred from combination of experimental and computational evidencei 3 PublicationsManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 766 | CalciumCombined sources Manual assertion inferred from combination of experimental and computational evidencei 3 PublicationsManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 768 | CalciumCombined sources Manual assertion inferred from combination of experimental and computational evidencei 3 PublicationsManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 770 | Calcium; via carbonyl oxygenCombined sources Manual assertion inferred from combination of experimental and computational evidencei 3 PublicationsManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 772 | CalciumCombined sources Manual assertion inferred from combination of experimental and computational evidencei 3 PublicationsManual assertion based on experiment ini
| 1 | |
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 877 | Essential for catalytic activityBy similarity Manual assertion inferred from sequence similarity toi | 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- alkylglycerophosphoethanolamine phosphodiesterase activity Source: RGD
<p>Inferred from Direct Assay</p>
<p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p>
Inferred from direct assayi
- "A novel highly potent autotaxin/ENPP2 inhibitor produces prolonged decreases in plasma lysophosphatidic acid formation in vivo and regulates urethral tension."
Saga H., Ohhata A., Hayashi A., Katoh M., Maeda T., Mizuno H., Takada Y., Komichi Y., Ota H., Matsumura N., Shibaya M., Sugiyama T., Nakade S., Kishikawa K.
PLoS ONE 9:e93230-e93230(2014) [PubMed] [Europe PMC] [Abstract]
- calcium ion binding Source: UniProtKBInferred from direct assayi
- Ref.8"Structural basis of substrate discrimination and integrin binding by autotaxin."
Hausmann J., Kamtekar S., Christodoulou E., Day J.E., Wu T., Fulkerson Z., Albers H.M., van Meeteren L.A., Houben A.J., van Zeijl L., Jansen S., Andries M., Hall T., Pegg L.E., Benson T.E., Kasiem M., Harlos K., Kooi C.W. , Smyth S.S., Ovaa H., Bollen M., Morris A.J., Moolenaar W.H., Perrakis A.
Nat. Struct. Mol. Biol. 18:198-204(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 36-862 IN COMPLEX WITH INHIBITOR; CALCIUM 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.
- lysophospholipase activity Source: UniProtKBInferred from direct assayi
- Ref.8"Structural basis of substrate discrimination and integrin binding by autotaxin."
Hausmann J., Kamtekar S., Christodoulou E., Day J.E., Wu T., Fulkerson Z., Albers H.M., van Meeteren L.A., Houben A.J., van Zeijl L., Jansen S., Andries M., Hall T., Pegg L.E., Benson T.E., Kasiem M., Harlos K., Kooi C.W. , Smyth S.S., Ovaa H., Bollen M., Morris A.J., Moolenaar W.H., Perrakis A.
Nat. Struct. Mol. Biol. 18:198-204(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 36-862 IN COMPLEX WITH INHIBITOR; CALCIUM 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.
- nucleic acid binding Source: InterPro
- nucleotide diphosphatase activity Source: InterPro
- phosphodiesterase I activity Source: RGD
<p>Inferred from Mutant Phenotype</p>
<p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p>
Inferred from mutant phenotypei
- "An essential oligomannosidic glycan chain in the catalytic domain of autotaxin, a secreted lysophospholipase-D."
Jansen S., Callewaert N., Dewerte I., Andries M., Ceulemans H., Bollen M.
J. Biol. Chem. 282:11084-11091(2007) [PubMed] [Europe PMC] [Abstract]
- polysaccharide binding Source: InterPro
- scavenger receptor activity Source: InterPro
- zinc ion binding Source: UniProtKBInferred from direct assayi
- Ref.8"Structural basis of substrate discrimination and integrin binding by autotaxin."
Hausmann J., Kamtekar S., Christodoulou E., Day J.E., Wu T., Fulkerson Z., Albers H.M., van Meeteren L.A., Houben A.J., van Zeijl L., Jansen S., Andries M., Hall T., Pegg L.E., Benson T.E., Kasiem M., Harlos K., Kooi C.W. , Smyth S.S., Ovaa H., Bollen M., Morris A.J., Moolenaar W.H., Perrakis A.
Nat. Struct. Mol. Biol. 18:198-204(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 36-862 IN COMPLEX WITH INHIBITOR; CALCIUM 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.
GO - Biological processi
- cell chemotaxis Source: RGDInferred from mutant phenotypei
- "An essential oligomannosidic glycan chain in the catalytic domain of autotaxin, a secreted lysophospholipase-D."
Jansen S., Callewaert N., Dewerte I., Andries M., Ceulemans H., Bollen M.
J. Biol. Chem. 282:11084-11091(2007) [PubMed] [Europe PMC] [Abstract]
- cellular response to cadmium ion Source: RGD
<p>Inferred from Expression Pattern</p>
<p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p>
Inferred from expression patterni
- "The potential protective role of lysophospholipid mediators in nephrotoxicity induced by chronically exposed cadmium."
Tsutsumi T., Ishihara A., Yamamoto A., Asaji H., Yamakawa S., Tokumura A.
Food Chem. Toxicol. 65:52-62(2014) [PubMed] [Europe PMC] [Abstract]
- cellular response to estradiol stimulus Source: RGDInferred from expression patterni
- "Identification of Igf2, Igfbp2 and Enpp2 as estrogen-responsive genes in rat hippocampus."
Takeo C., Ikeda K., Horie-Inoue K., Inoue S.
Endocr. J. 56:113-120(2009) [PubMed] [Europe PMC] [Abstract]
- estrous cycle Source: RGDInferred from expression patterni
- "Expression and regulation of Enpp2 in rat uterus during the estrous cycle."
Ahn H.J., Yang H., An B.S., Choi K.C., Jeung E.B.
J. Vet. Sci. 12:379-385(2011) [PubMed] [Europe PMC] [Abstract]
- immune response Source: InterPro
- negative regulation of cell-matrix adhesion Source: RGDInferred from direct assayi
- "Phosphodiesterase-Ialpha/autotaxin: a counteradhesive protein expressed by oligodendrocytes during onset of myelination."
Fox M.A., Colello R.J., Macklin W.B., Fuss B.
Mol. Cell. Neurosci. 23:507-519(2003) [PubMed] [Europe PMC] [Abstract]
- phosphatidylcholine catabolic process Source: UniProtKBInferred from direct assayi
- Ref.8"Structural basis of substrate discrimination and integrin binding by autotaxin."
Hausmann J., Kamtekar S., Christodoulou E., Day J.E., Wu T., Fulkerson Z., Albers H.M., van Meeteren L.A., Houben A.J., van Zeijl L., Jansen S., Andries M., Hall T., Pegg L.E., Benson T.E., Kasiem M., Harlos K., Kooi C.W. , Smyth S.S., Ovaa H., Bollen M., Morris A.J., Moolenaar W.H., Perrakis A.
Nat. Struct. Mol. Biol. 18:198-204(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 36-862 IN COMPLEX WITH INHIBITOR; CALCIUM 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.
- positive regulation of cell population proliferation Source: RGDInferred from direct assayi
- Ref.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, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
- positive regulation of focal adhesion assembly Source: RGDInferred from direct assayi
- "P2Y12 receptor expression is a critical determinant of functional responsiveness to ATX's MORFO domain."
Dennis J., Morgan M.K., Graf M.R., Fuss B.
Purinergic Signal. 8:181-190(2012) [PubMed] [Europe PMC] [Abstract]
- positive regulation of oligodendrocyte differentiation Source: RGDInferred from direct assayi
- "P2Y12 receptor expression is a critical determinant of functional responsiveness to ATX's MORFO domain."
Dennis J., Morgan M.K., Graf M.R., Fuss B.
Purinergic Signal. 8:181-190(2012) [PubMed] [Europe PMC] [Abstract]
- positive regulation of substrate adhesion-dependent cell spreading Source: RGDInferred from direct assayi
- "P2Y12 receptor expression is a critical determinant of functional responsiveness to ATX's MORFO domain."
Dennis J., Morgan M.K., Graf M.R., Fuss B.
Purinergic Signal. 8:181-190(2012) [PubMed] [Europe PMC] [Abstract]
- regulation of angiogenesis Source: InterPro
- regulation of cell migration Source: InterPro
- response to polycyclic arene Source: RGDInferred from expression patterni
- "Serum metabolomics analysis reveals impaired lipid metabolism in rats after oral exposure to benzo(a)pyrene."
Wang X., Zhang J., Huang Q., Alamdar A., Tian M., Liu L., Shen H.
Mol Biosyst 11:753-759(2015) [PubMed] [Europe PMC] [Abstract]
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Hydrolase |
| Biological process | Chemotaxis, Lipid degradation, Lipid metabolism |
| Ligand | Calcium, Metal-binding, Zinc |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.1.4.39 5301 |
SABIO-RK: Biochemical Reaction Kinetics Database More...SABIO-RKi | Q64610 |
Chemistry databases
SwissLipids knowledge resource for lipid biology More...SwissLipidsi | SLP:000000394 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Ectonucleotide pyrophosphatase/phosphodiesterase family member 2 (EC:3.1.4.39
Manual assertion based on experiment ini
Short name: E-NPP 2 Alternative name(s): Autotaxin1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
Extracellular lysophospholipase D Short name: LysoPLD1 Publication Manual assertion based on opinion ini
|
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:Enpp2 Synonyms:Atx, Npps2 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Rattus norvegicus (Rat) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 10116 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Rat genome database More...RGDi | 69298 Enpp2 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Extracellular region or secreted
- Secreted 5 Publications
Manual assertion based on experiment ini
- Ref.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] - Ref.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, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION. - Ref.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: CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-171; THR-209; ASP-311 AND HIS-315, ACTIVE SITE. - Ref.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. - Ref.8"Structural basis of substrate discrimination and integrin binding by autotaxin."
Hausmann J., Kamtekar S., Christodoulou E., Day J.E., Wu T., Fulkerson Z., Albers H.M., van Meeteren L.A., Houben A.J., van Zeijl L., Jansen S., Andries M., Hall T., Pegg L.E., Benson T.E., Kasiem M., Harlos K., Kooi C.W. , Smyth S.S., Ovaa H., Bollen M., Morris A.J., Moolenaar W.H., Perrakis A.
Nat. Struct. Mol. Biol. 18:198-204(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 36-862 IN COMPLEX WITH INHIBITOR; CALCIUM 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.
- Secreted 5 Publications
Extracellular region or secreted
- extracellular space Source: UniProtKBInferred from direct assayi
- Ref.8"Structural basis of substrate discrimination and integrin binding by autotaxin."
Hausmann J., Kamtekar S., Christodoulou E., Day J.E., Wu T., Fulkerson Z., Albers H.M., van Meeteren L.A., Houben A.J., van Zeijl L., Jansen S., Andries M., Hall T., Pegg L.E., Benson T.E., Kasiem M., Harlos K., Kooi C.W. , Smyth S.S., Ovaa H., Bollen M., Morris A.J., Moolenaar W.H., Perrakis A.
Nat. Struct. Mol. Biol. 18:198-204(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 36-862 IN COMPLEX WITH INHIBITOR; CALCIUM 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.
- extracellular space Source: UniProtKBInferred from direct assayi
Golgi apparatus
- Golgi apparatus Source: RGDInferred from direct assayi
- Ref.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.
- Golgi apparatus Source: RGDInferred from direct assayi
Other locations
- cytoplasm Source: RGDInferred from direct assayi
- Ref.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.
- cytoplasm Source: RGDInferred from direct assayi
Keywords - Cellular componenti
Secreted<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 13 | I → L: No effect on secretion. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 16 – 18 | FTF → VLS: No effect on secretion. 1 Publication Manual assertion based on experiment ini
| 3 | |
| Mutagenesisi | 18 – 21 | FAIS → SVCV: No effect on secretion. 1 Publication Manual assertion based on experiment ini
| 4 | |
| Mutagenesisi | 21 – 24 | SVNI → VLTT: No effect on secretion. 1 Publication Manual assertion based on experiment ini
| 4 | |
| Mutagenesisi | 24 – 25 | IC → TI: No effect on secretion. 1 Publication Manual assertion based on experiment ini
| 2 | |
| Mutagenesisi | 28 – 30 | FTA → CIF: No effect on secretion. 1 Publication Manual assertion based on experiment ini
| 3 | |
| Mutagenesisi | 171 | D → N: Abolishes lysophospholipase D activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 209 | T → A: Abolishes lysophospholipase D activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 209 | T → S: 15% of wild-type lysophospholipase D activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 311 | D → N: Abolishes lysophospholipase D activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 315 | H → Q: 20% of wild-type lysophospholipase D activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 430 | K → A: Impaired secretion. No effect on lysophospholipase activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 764 – 768 | DYNYD → SYAYS: Abolishes secretion. Strongly reduced lysophospholipase activity. 1 Publication Manual assertion based on experiment ini
| 5 |
Keywords - Diseasei
ObesityChemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL3826870 |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 2901 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei | 1 – 27 | 2 Publications Manual assertion based on experiment ini
| 27 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000281651 | 28 – 35 | Removed by furin2 Publications Manual assertion based on experiment ini
| 8 | |
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000188569 | 36 – 887 | Ectonucleotide pyrophosphatase/phosphodiesterase family member 2Add BLAST | 852 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 53 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 58 ↔ 75 | PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi 1 PublicationManual assertion based on experiment ini
| ||
| Disulfide bondi | 62 ↔ 93 | PROSITE-ProRule annotation Manual assertion according to rulesi 1 PublicationManual assertion based on experiment ini
| ||
| Disulfide bondi | 73 ↔ 86 | PROSITE-ProRule annotation Manual assertion according to rulesi 1 PublicationManual assertion based on experiment ini
| ||
| Disulfide bondi | 79 ↔ 85 | PROSITE-ProRule annotation Manual assertion according to rulesi 1 PublicationManual assertion based on experiment ini
| ||
| Disulfide bondi | 102 ↔ 119 | PROSITE-ProRule annotation Manual assertion according to rulesi 1 PublicationManual assertion based on experiment ini
| ||
| Disulfide bondi | 107 ↔ 137 | PROSITE-ProRule annotation Manual assertion according to rulesi 1 PublicationManual assertion based on experiment ini
| ||
| Disulfide bondi | 117 ↔ 130 | PROSITE-ProRule annotation Manual assertion according to rulesi 1 PublicationManual assertion based on experiment ini
| ||
| Disulfide bondi | 123 ↔ 129 | PROSITE-ProRule annotation Manual assertion according to rulesi 1 PublicationManual assertion based on experiment ini
| ||
| Disulfide bondi | 148 ↔ 194 | PROSITE-ProRule annotation Manual assertion according to rulesi 1 PublicationManual assertion based on experiment ini
| ||
| Disulfide bondi | 156 ↔ 350 | PROSITE-ProRule annotation Manual assertion according to rulesi 1 PublicationManual assertion based on experiment ini
| ||
| Disulfide bondi | 366 ↔ 468 | PROSITE-ProRule annotation Manual assertion according to rulesi 1 PublicationManual assertion based on experiment ini
| ||
| Glycosylationi | 398 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| Glycosylationi | 410 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| Disulfide bondi | 413 ↔ 830 | PROSITE-ProRule annotation Manual assertion according to rulesi 1 PublicationManual assertion based on experiment ini
| ||
| Glycosylationi | 524 | N-linked (GlcNAc...) asparagine1 Publication Manual assertion based on experiment ini
| 1 | |
| Disulfide bondi | 566 ↔ 691 | PROSITE-ProRule annotation Manual assertion according to rulesi 1 PublicationManual assertion based on experiment ini
| ||
| Disulfide bondi | 568 ↔ 676 | PROSITE-ProRule annotation Manual assertion according to rulesi 1 PublicationManual assertion based on experiment ini
| ||
| Glycosylationi | 610 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| Disulfide bondi | 799 ↔ 809 | PROSITE-ProRule annotation Manual assertion according to rulesi 1 PublicationManual assertion based on experiment ini
| ||
| Glycosylationi | 831 | N-linked (GlcNAc...) asparagineSequence analysis | 1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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, GlycoproteinProteomic databases
PRoteomics IDEntifications database More...PRIDEi | Q64610 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q64610 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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
Manual assertion based on experiment ini
- Ref.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. - Ref.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]
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure_section">'Structure'</a> section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 59 – 63 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure_section">'Structure'</a> section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 70 – 72 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Turni | 77 – 83 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure_section">'Structure'</a> section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 89 – 92 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Turni | 98 – 100 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 104 – 106 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 107 – 109 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 115 – 118 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 123 – 126 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 133 – 137 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 143 – 145 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 165 – 171 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| Helixi | 175 – 180 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Turni | 182 – 184 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 186 – 194 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| Beta strandi | 195 – 197 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 209 – 218 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| Helixi | 222 – 225 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 230 – 234 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Turni | 235 – 238 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 239 – 241 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 243 – 246 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 247 – 249 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 251 – 253 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 259 – 265 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| Helixi | 281 – 292 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| Turni | 296 – 298 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 301 – 310 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| Helixi | 311 – 317 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| Helixi | 322 – 324 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 325 – 344 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 20 | |
| Turni | 348 – 350 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 352 – 358 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| Beta strandi | 368 – 371 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 372 – 374 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 379 – 381 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 382 – 385 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 387 – 395 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| Beta strandi | 396 – 398 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 404 – 410 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| Beta strandi | 419 – 424 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Helixi | 425 – 427 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 430 – 432 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 442 – 447 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 452 – 456 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 457 – 459 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 471 – 473 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 481 – 483 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 487 – 494 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| Beta strandi | 496 – 499 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 505 – 507 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 508 – 515 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| Turni | 527 – 530 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 531 – 533 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 534 – 536 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 559 – 561 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 577 – 581 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Turni | 583 – 586 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 587 – 591 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 617 – 620 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 634 – 638 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 643 – 647 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Turni | 648 – 651 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 652 – 660 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| Helixi | 671 – 673 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 685 – 687 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 691 – 696 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 701 – 706 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Helixi | 708 – 710 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 714 – 717 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 718 – 721 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 723 – 725 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 726 – 729 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 731 – 742 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| Helixi | 744 – 752 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| Beta strandi | 754 – 762 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| Beta strandi | 768 – 770 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 774 – 776 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 790 – 801 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| Helixi | 806 – 808 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 813 – 821 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| Turni | 830 – 833 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 836 – 838 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 840 – 846 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| Helixi | 851 – 858 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| Beta strandi | 859 – 861 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 865 – 868 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 870 – 878 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 |
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q64610 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q64610 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 54 – 97 | SMB 1PROSITE-ProRule annotation Manual assertion according to rulesi Add BLAST | 44 | |
| Domaini | 98 – 142 | SMB 2PROSITE-ProRule annotation Manual assertion according to rulesi Add BLAST | 45 |
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 210 – 213 | Substrate bindingBy similarity Manual assertion inferred from sequence similarity toi | 4 | |
| Regioni | 243 – 254 | Substrate bindingBy similarity Manual assertion inferred from sequence similarity toi Add BLAST | 12 | |
| Regioni | 854 – 875 | Required for secretionBy similarityAdd BLAST | 22 |
Motif
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi | 126 – 128 | Cell attachment siteSequence analysis | 3 |
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Belongs to the nucleotide pyrophosphatase/phosphodiesterase family.Curated
Keywords - Domaini
Repeat, SignalPhylogenomic databases
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000037439 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q64610 |
KEGG Orthology (KO) More...KOi | K01122 |
Database of Orthologous Groups More...OrthoDBi | 999163at2759 |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q64610 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.40.720.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR017850 Alkaline_phosphatase_core_sf IPR001604 DNA/RNA_non-sp_Endonuclease IPR029881 ENPP2 IPR020821 Extracellular_endonuc_su_A IPR002591 Phosphodiest/P_Trfase IPR036024 Somatomedin_B-like_dom_sf IPR020436 Somatomedin_B_chordata IPR001212 Somatomedin_B_dom |
The PANTHER Classification System More...PANTHERi | PTHR10151:SF21 PTHR10151:SF21, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF01223 Endonuclease_NS, 1 hit PF01663 Phosphodiest, 1 hit PF01033 Somatomedin_B, 2 hits |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00022 SOMATOMEDINB |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00892 Endonuclease_NS, 1 hit SM00477 NUC, 1 hit SM00201 SO, 2 hits |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF53649 SSF53649, 1 hit SSF90188 SSF90188, 2 hits |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00524 SMB_1, 2 hits PS50958 SMB_2, 2 hits |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded to basketThis entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All
Isoform 1 (identifier: Q64610-1) [UniParc]FASTAAdd to basketAdded to basket
This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
Show »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
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i40AD1C957F833869
Isoform 2 (identifier: Q64610-2) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
591-615: Missing.
« 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 RKERHLLYGR
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 VWAYFQRVLV KKYASERNGV NVISGPIFDY NYDGLRDTED
760 770 780 790 800
EIKQYVEGSS IPVPTHYYSI ITSCLDFTQP ADKCDGPLSV SSFILPHRPD
810 820 830 840 850
NDESCNSSED ESKWVEELMK MHTARVRDIE HLTGLDFYRK TSRSYSEILT
860
LKTYLHTYES EI
Note: No experimental confirmation available.
Show »<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi
There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket| Entry | Entry name | Protein names | Gene names | Length | Annotation | ||
|---|---|---|---|---|---|---|---|
| F1LSF4 | F1LSF4_RAT | Ectonucleotide pyrophosphatase/phos... Ectonucleotide pyrophosphatase/phosphodiesterase family member 2 | Enpp2 | 883 | Annotation score: Annotation score:2 out of 5 <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p> | ||
| D3ZES5 | D3ZES5_RAT | Ectonucleotide pyrophosphatase/phos... Ectonucleotide pyrophosphatase/phosphodiesterase family member 2 | Enpp2 | 858 | Annotation score: Annotation score:2 out of 5 <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p> | ||
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 97 | A → V in BAA05910 (PubMed:7961762).Curated | 1 | |
| Sequence conflicti | 107 | C → S in BAA05910 (PubMed:7961762).Curated | 1 | |
| Sequence conflicti | 120 | S → P in BAA05910 (PubMed:7961762).Curated | 1 | |
| Sequence conflicti | 147 – 162 | DCEEI…AGFVR → AARNQSSECLQVCP in BAA05910 (PubMed:7961762).CuratedAdd BLAST | 16 | |
| Sequence conflicti | 198 | A → V in BAA05910 (PubMed:7961762).Curated | 1 | |
| Sequence conflicti | 201 | M → T in BAA05910 (PubMed:7961762).Curated | 1 |
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_024018 | 591 – 615 | Missing in isoform 2. 1 Publication Manual assertion based on opinion ini
| 25 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | D28560 mRNA Translation: BAA05910.1 DQ131564 mRNA Translation: AAZ99725.1 BC081747 mRNA Translation: AAH81747.1 |
Protein sequence database of the Protein Information Resource More...PIRi | A55453 |
NCBI Reference Sequences More...RefSeqi | NP_476445.2, NM_057104.2 |
Genome annotation databases
Database of genes from NCBI RefSeq genomes More...GeneIDi | 84050 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | rno:84050 |
UCSC genome browser More...UCSCi | RGD:69298 rat [Q64610-1] |
Keywords - Coding sequence diversityi
Alternative splicing<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| Q64610 | Ectonucleotide pyrophosphatase/phosphodiesterase family member 2 | ) | 862 | UniRef50_Q9R1E6 | ||
| Ectonucleotide pyrophosphatase/phosphodiesterase family member 2 | ) | 863 | ||||
| Ectonucleotide pyrophosphatase/phosphodiesterase family member 2 | 888 | |||||
| Uncharacterized protein | 957 | |||||
| Uncharacterized protein | 957 | |||||
| +1580 | ||||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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 |
| PIRi | A55453 |
| RefSeqi | NP_476445.2, NM_057104.2 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 2XR9 | X-ray | 2.05 | A | 36-887 | [»] | |
| 2XRG | X-ray | 3.20 | A | 1-887 | [»] | |
| 5DLT | X-ray | 1.60 | A | 36-887 | [»] | |
| 5DLV | X-ray | 2.00 | A/B | 36-887 | [»] | |
| 5DLW | X-ray | 1.80 | A | 36-887 | [»] | |
| 5IJQ | X-ray | 2.05 | A | 36-887 | [»] | |
| 5IJS | X-ray | 2.20 | A | 36-887 | [»] | |
| 5L0B | X-ray | 2.41 | A/B | 1-887 | [»] | |
| 5L0E | X-ray | 3.06 | A/B | 1-887 | [»] | |
| 5L0K | X-ray | 2.73 | A/B | 51-884 | [»] | |
| 5LQQ | X-ray | 2.40 | A | 36-887 | [»] | |
| 5M0D | X-ray | 2.40 | A | 36-887 | [»] | |
| 5M0E | X-ray | 1.95 | A | 36-887 | [»] | |
| 5M0M | X-ray | 2.10 | A | 36-887 | [»] | |
| 5M0S | X-ray | 2.10 | A | 36-887 | [»] | |
| SMRi | Q64610 | |||||
| ModBasei | Search... | |||||
| PDBe-KBi | Search... | |||||
Chemistry databases
| ChEMBLi | CHEMBL3826870 |
| GuidetoPHARMACOLOGYi | 2901 |
| SwissLipidsi | SLP:000000394 |
PTM databases
| iPTMneti | Q64610 |
Proteomic databases
| PRIDEi | Q64610 |
Genome annotation databases
| GeneIDi | 84050 |
| KEGGi | rno:84050 |
| UCSCi | RGD:69298 rat [Q64610-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 5168 |
| RGDi | 69298 Enpp2 |
Phylogenomic databases
| HOGENOMi | HOG000037439 |
| InParanoidi | Q64610 |
| KOi | K01122 |
| OrthoDBi | 999163at2759 |
| PhylomeDBi | Q64610 |
Enzyme and pathway databases
| BRENDAi | 3.1.4.39 5301 |
| SABIO-RKi | Q64610 |
Miscellaneous databases
| EvolutionaryTracei | Q64610 |
Protein Ontology More...PROi | PR:Q64610 |
Family and domain databases
| Gene3Di | 3.40.720.10, 1 hit |
| InterProi | View protein in InterPro IPR017850 Alkaline_phosphatase_core_sf IPR001604 DNA/RNA_non-sp_Endonuclease IPR029881 ENPP2 IPR020821 Extracellular_endonuc_su_A IPR002591 Phosphodiest/P_Trfase IPR036024 Somatomedin_B-like_dom_sf IPR020436 Somatomedin_B_chordata IPR001212 Somatomedin_B_dom |
| PANTHERi | PTHR10151:SF21 PTHR10151:SF21, 1 hit |
| Pfami | View protein in Pfam PF01223 Endonuclease_NS, 1 hit PF01663 Phosphodiest, 1 hit PF01033 Somatomedin_B, 2 hits |
| PRINTSi | PR00022 SOMATOMEDINB |
| SMARTi | View protein in SMART SM00892 Endonuclease_NS, 1 hit SM00477 NUC, 1 hit SM00201 SO, 2 hits |
| SUPFAMi | SSF53649 SSF53649, 1 hit SSF90188 SSF90188, 2 hits |
| PROSITEi | View protein in PROSITE PS00524 SMB_1, 2 hits PS50958 SMB_2, 2 hits |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | ENPP2_RAT | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | Q64610Primary (citable) accession number: Q64610 Secondary accession number(s): Q66HQ0 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | September 19, 2002 |
| Last sequence update: | March 20, 2007 | |
| Last modified: | September 18, 2019 | |
| This is version 151 of the entry and version 2 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
Keywords - Technical termi
3D-structure, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families - PDB cross-references
Index of Protein Data Bank (PDB) cross-references
