ENPP2_RAT
ID ENPP2_RAT Reviewed; 887 AA.
AC Q64610; Q66HQ0;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Ectonucleotide pyrophosphatase/phosphodiesterase family member 2;
DE Short=E-NPP 2;
DE EC=3.1.4.39 {ECO:0000269|PubMed:12119361, ECO:0000269|PubMed:12633853, ECO:0000269|PubMed:21240271, ECO:0000269|PubMed:27075612, ECO:0000269|PubMed:27268273, ECO:0000269|PubMed:27660691, ECO:0000269|PubMed:29259743};
DE AltName: Full=Autotaxin {ECO:0000303|PubMed:12119361};
DE AltName: Full=Extracellular lysophospholipase D;
DE Short=LysoPLD {ECO:0000303|PubMed:12119361, ECO:0000303|PubMed:12354767};
DE Flags: Precursor;
GN Name=Enpp2; Synonyms=Atx, Npps2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=7961762; DOI=10.1016/s0021-9258(18)46919-0;
RA Narita M., Goji J., Nakamura H., Sano K.;
RT "Molecular cloning, expression, and localization of a brain-specific
RT phosphodiesterase I/nucleotide pyrophosphatase (PD-Ialpha) from rat
RT brain.";
RL J. Biol. Chem. 269:28235-28242(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 28-32 AND
RP 36-41, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=16436050; DOI=10.1111/j.1365-2443.2006.00924.x;
RA Koike S., Keino-Masu K., Ohto T., Masu M.;
RT "The N-terminal hydrophobic sequence of autotaxin (ENPP2) functions as a
RT signal peptide.";
RL Genes Cells 11:133-142(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12176993; DOI=10.1074/jbc.m205623200;
RA Tokumura A., Majima E., Kariya Y., Tominaga K., Kogure K., Yasuda K.,
RA Fukuzawa K.;
RT "Identification of human plasma lysophospholipase D, a lysophosphatidic
RT acid-producing enzyme, as autotaxin, a multifunctional phosphodiesterase.";
RL J. Biol. Chem. 277:39436-39442(2002).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=12354767; DOI=10.1074/jbc.m206812200;
RA Aoki J., Taira A., Takanezawa Y., Kishi Y., Hama K., Kishimoto T.,
RA Mizuno K., Saku K., Taguchi R., Arai H.;
RT "Serum lysophosphatidic acid is produced through diverse phospholipase
RT pathways.";
RL J. Biol. Chem. 277:48737-48744(2002).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=12119361; DOI=10.1083/jcb.200204026;
RA Umezu-Goto M., Kishi Y., Taira A., Hama K., Dohmae N., Takio K., Yamori T.,
RA Mills G.B., Inoue K., Aoki J., Arai H.;
RT "Autotaxin has lysophospholipase D activity leading to tumor cell growth
RT and motility by lysophosphatidic acid production.";
RL J. Cell Biol. 158:227-233(2002).
RN [7]
RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-171; THR-209;
RP ASP-311 AND HIS-315, AND ACTIVE SITE.
RX PubMed=12633853; DOI=10.1016/s0014-5793(03)00133-9;
RA Gijsbers R., Aoki J., Arai H., Bollen M.;
RT "The hydrolysis of lysophospholipids and nucleotides by autotaxin (NPP2)
RT involves a single catalytic site.";
RL FEBS Lett. 538:60-64(2003).
RN [8]
RP PROTEOLYTIC PROCESSING, PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION
RP CHARACTERIZATION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ILE-13;
RP 16-PHE--PHE-18; 18-PHE--SER-21; 21-SER--ILE-24; 24-ILE--CYS-25 AND
RP 28-PHE--ALA-30.
RX PubMed=15985467; DOI=10.1242/jcs.02438;
RA Jansen S., Stefan C., Creemers J.W., Waelkens E., Van Eynde A.,
RA Stalmans W., Bollen M.;
RT "Proteolytic maturation and activation of autotaxin (NPP2), a secreted
RT metastasis-enhancing lysophospholipase D.";
RL J. Cell Sci. 118:3081-3089(2005).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=29259743; DOI=10.1021/acsmedchemlett.7b00312;
RA Kuttruff C.A., Ferrara M., Bretschneider T., Hoerer S., Handschuh S.,
RA Nosse B., Romig H., Nicklin P., Roth G.J.;
RT "Discovery of BI-2545: A Novel Autotaxin Inhibitor That Significantly
RT Reduces LPA Levels in Vivo.";
RL ACS Med. Chem. Lett. 8:1252-1257(2017).
RN [10] {ECO:0007744|PDB:2XR9, ECO:0007744|PDB:2XRG}
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 36-862 IN COMPLEX WITH INHIBITOR;
RP CALCIUM AND ZINC IONS, CATALYTIC ACTIVITY, COFACTOR, CALCIUM BINDING,
RP DISULFIDE BONDS, GLYCOSYLATION AT ASN-524, ACTIVE SITE, MUTAGENESIS OF
RP LYS-430 AND 764-ASP--ASP-768, AND SUBCELLULAR LOCATION.
RX PubMed=21240271; DOI=10.1038/nsmb.1980;
RA Hausmann J., Kamtekar S., Christodoulou E., Day J.E., Wu T., Fulkerson Z.,
RA Albers H.M., van Meeteren L.A., Houben A.J., van Zeijl L., Jansen S.,
RA Andries M., Hall T., Pegg L.E., Benson T.E., Kasiem M., Harlos K.,
RA Kooi C.W., Smyth S.S., Ovaa H., Bollen M., Morris A.J., Moolenaar W.H.,
RA Perrakis A.;
RT "Structural basis of substrate discrimination and integrin binding by
RT autotaxin.";
RL Nat. Struct. Mol. Biol. 18:198-204(2011).
RN [11] {ECO:0007744|PDB:5L0B, ECO:0007744|PDB:5L0E, ECO:0007744|PDB:5L0K}
RP X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) IN COMPLEX WITH INHIBITOR; CALCIUM
RP AND ZINC, CATALYTIC ACTIVITY, COFACTOR, FUNCTION, GLYCOSYLATION AT ASN-410
RP AND ASN-524, AND DISULFIDE BONDS.
RX PubMed=27660691; DOI=10.1021/acsmedchemlett.6b00207;
RA Jones S.B., Pfeifer L.A., Bleisch T.J., Beauchamp T.J., Durbin J.D.,
RA Klimkowski V.J., Hughes N.E., Rito C.J., Dao Y., Gruber J.M., Bui H.,
RA Chambers M.G., Chandrasekhar S., Lin C., McCann D.J., Mudra D.R.,
RA Oskins J.L., Swearingen C.A., Thirunavukkarasu K., Norman B.H.;
RT "Novel Autotaxin Inhibitors for the Treatment of Osteoarthritis Pain: Lead
RT Optimization via Structure-Based Drug Design.";
RL ACS Med. Chem. Lett. 7:857-861(2016).
RN [12] {ECO:0007744|PDB:5IJQ, ECO:0007744|PDB:5IJS}
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 36-887 IN COMPLEXES WITH
RP PHOSPHATE; VANADATE; HYDROXYCHOLESTEROL; CALCIUM AND ZINC, FUNCTION,
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, COFACTOR, ACTIVE SITE,
RP GLYCOSYLATION AT ASN-524, AND DISULFIDE BONDS.
RX PubMed=27268273; DOI=10.1016/j.jsb.2016.06.002;
RA Hausmann J., Keune W.J., Hipgrave Ederveen A.L., van Zeijl L.,
RA Joosten R.P., Perrakis A.;
RT "Structural snapshots of the catalytic cycle of the phosphodiesterase
RT Autotaxin.";
RL J. Struct. Biol. 195:199-206(2016).
RN [13] {ECO:0007744|PDB:5DLT, ECO:0007744|PDB:5DLV, ECO:0007744|PDB:5DLW}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 36-887 IN COMPLEXES WITH OLEOYL
RP LYSOPHOSPHATIDIC ACID; STEROIDS; CALCIUM AND ZINC, CATALYTIC ACTIVITY,
RP FUNCTION, ACTIVITY REGULATION, COFACTOR, GLYCOSYLATION AT ASN-524, AND
RP DISULFIDE BONDS.
RX PubMed=27075612; DOI=10.1038/ncomms11248;
RA Keune W.J., Hausmann J., Bolier R., Tolenaars D., Kremer A.,
RA Heidebrecht T., Joosten R.P., Sunkara M., Morris A.J., Matas-Rico E.,
RA Moolenaar W.H., Oude Elferink R.P., Perrakis A.;
RT "Steroid binding to Autotaxin links bile salts and lysophosphatidic acid
RT signalling.";
RL Nat. Commun. 7:11248-11248(2016).
CC -!- FUNCTION: Hydrolyzes lysophospholipids to produce the signaling
CC molecule lysophosphatidic acid (LPA) in extracellular fluids
CC (PubMed:12633853, PubMed:29259743, PubMed:27660691, PubMed:27268273,
CC PubMed:27075612, PubMed:12354767). Major substrate is
CC lysophosphatidylcholine (PubMed:12119361, PubMed:27660691,
CC PubMed:27268273, PubMed:27075612, PubMed:12176993). Can also act on
CC sphingosylphosphorylcholine producing sphingosine-1-phosphate, a
CC modulator of cell motility (PubMed:12119361). Can hydrolyze, in vitro,
CC bis-pNPP, to some extent pNP-TMP, and barely ATP (PubMed:12633853,
CC PubMed:27268273). Involved in several motility-related processes such
CC as angiogenesis and neurite outgrowth. Acts as an angiogenic factor by
CC stimulating migration of smooth muscle cells and microtubule formation.
CC Stimulates migration of melanoma cells, probably via a pertussis toxin-
CC sensitive G protein. May have a role in induction of parturition.
CC Possible involvement in cell proliferation and adipose tissue
CC development. Tumor cell motility-stimulating factor (By similarity).
CC Required for LPA production in activated platelets, cleaves the sn-1
CC lysophospholipids to generate sn-1 lysophosphatidic acids containing
CC predominantly 18:2 and 20:4 fatty acids (By similarity). Shows a
CC preference for the sn-1 to the sn-2 isomer of 1-O-alkyl-sn-glycero-3-
CC phosphocholine (lyso-PAF) (By similarity).
CC {ECO:0000250|UniProtKB:Q13822, ECO:0000269|PubMed:12119361,
CC ECO:0000269|PubMed:12176993, ECO:0000269|PubMed:12354767,
CC ECO:0000269|PubMed:12633853, ECO:0000269|PubMed:15985467,
CC ECO:0000269|PubMed:27075612, ECO:0000269|PubMed:27268273,
CC ECO:0000269|PubMed:27660691, ECO:0000269|PubMed:29259743}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-alkyl-sn-glycero-3-phosphoethanolamine + H2O = 1-O-alkyl-
CC sn-glycero-3-phosphate + ethanolamine + H(+); Xref=Rhea:RHEA:15965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57603,
CC ChEBI:CHEBI:58014, ChEBI:CHEBI:76168; EC=3.1.4.39;
CC Evidence={ECO:0000269|PubMed:12119361, ECO:0000269|PubMed:12633853,
CC ECO:0000269|PubMed:21240271, ECO:0000269|PubMed:27075612,
CC ECO:0000269|PubMed:27268273, ECO:0000269|PubMed:27660691,
CC ECO:0000269|PubMed:29259743};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-(9Z-octadecenyl)-sn-glycero-3-phosphocholine + H2O = 1-O-
CC (9Z-octadecenyl)-sn-glycero-3-phosphate + choline + H(+);
CC Xref=Rhea:RHEA:41684, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:64396, ChEBI:CHEBI:78402;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41685;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-acyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-
CC glycerol 3-phosphate + choline + H(+); Xref=Rhea:RHEA:41712,
CC ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57875, ChEBI:CHEBI:64982;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41713;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-acyl-sn-glycero-3-phospho-L-serine + H2O = a 2-acyl-sn-
CC glycerol 3-phosphate + H(+) + L-serine; Xref=Rhea:RHEA:41716,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:64982, ChEBI:CHEBI:65214;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41717;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-dodecanoyl-sn-glycero-3-phosphocholine + H2O = 1-dodecanoyl-
CC sn-glycerol 3-phosphate + choline + H(+); Xref=Rhea:RHEA:38991,
CC ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:72682, ChEBI:CHEBI:74966;
CC Evidence={ECO:0000269|PubMed:12176993};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38992;
CC Evidence={ECO:0000305|PubMed:12176993};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + sphing-4-enine-phosphocholine = choline + H(+) + sphing-
CC 4-enine 1-phosphate; Xref=Rhea:RHEA:38919, ChEBI:CHEBI:15354,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58906,
CC ChEBI:CHEBI:60119; Evidence={ECO:0000250|UniProtKB:Q13822};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38920;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = 1-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphate + choline + H(+);
CC Xref=Rhea:RHEA:38915, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28610, ChEBI:CHEBI:74544;
CC Evidence={ECO:0000269|PubMed:12176993, ECO:0000269|PubMed:12354767};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38916;
CC Evidence={ECO:0000305|PubMed:12176993, ECO:0000305|PubMed:12354767};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-tetradecanoyl-sn-glycero-3-phosphocholine + H2O = 1-
CC tetradecanoyl-sn-glycerol 3-phosphate + choline + H(+);
CC Xref=Rhea:RHEA:38983, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:64489, ChEBI:CHEBI:72683;
CC Evidence={ECO:0000269|PubMed:12176993};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38984;
CC Evidence={ECO:0000305|PubMed:12176993};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-decanoyl-sn-glycero-3-phosphocholine + H2O = 1-decanoyl-sn-
CC glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:41131,
CC ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:77724, ChEBI:CHEBI:77726;
CC Evidence={ECO:0000269|PubMed:12176993};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41132;
CC Evidence={ECO:0000305|PubMed:12176993};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-
CC hexadecanoyl-sn-glycero-3-phosphate + choline + H(+);
CC Xref=Rhea:RHEA:38975, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57518, ChEBI:CHEBI:72998;
CC Evidence={ECO:0000269|PubMed:12176993};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38976;
CC Evidence={ECO:0000305|PubMed:12176993};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-
CC octadecanoyl-sn-glycero-3-phosphate + choline + H(+);
CC Xref=Rhea:RHEA:38979, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:73858, ChEBI:CHEBI:74565;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38980;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphocholine + H2O =
CC 1-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphate + choline + H(+);
CC Xref=Rhea:RHEA:41135, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28733, ChEBI:CHEBI:74547;
CC Evidence={ECO:0000269|PubMed:12176993};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41136;
CC Evidence={ECO:0000305|PubMed:12176993};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine
CC + H2O = 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate +
CC choline + H(+); Xref=Rhea:RHEA:41139, ChEBI:CHEBI:15354,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:74344,
CC ChEBI:CHEBI:74938; Evidence={ECO:0000269|PubMed:12176993};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41140;
CC Evidence={ECO:0000305|PubMed:12176993};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-sn-glycero-3-phosphocholine + H2O = 1-O-
CC hexadecyl-sn-glycero-3-phosphate + choline + H(+);
CC Xref=Rhea:RHEA:41143, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:64496, ChEBI:CHEBI:77580;
CC Evidence={ECO:0000269|PubMed:12176993};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41144;
CC Evidence={ECO:0000305|PubMed:12176993};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexanoyl-sn-
CC glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:41400,
CC ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:78215, ChEBI:CHEBI:78223;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41401;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dioctanoyl-sn-glycero-3-phosphocholine + H2O = 1,2-
CC dioctanoyl-sn-glycero-3-phosphate + choline + H(+);
CC Xref=Rhea:RHEA:41416, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:78228, ChEBI:CHEBI:78229;
CC Evidence={ECO:0000269|PubMed:12176993};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41417;
CC Evidence={ECO:0000305|PubMed:12176993};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-didecanoyl-sn-glycero-3-phosphocholine + H2O = 1,2-
CC didecanoyl-sn-glycero-3-phosphate + choline + H(+);
CC Xref=Rhea:RHEA:41412, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:78226, ChEBI:CHEBI:78227;
CC Evidence={ECO:0000269|PubMed:12176993};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41413;
CC Evidence={ECO:0000305|PubMed:12176993};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-(1Z-alkenyl)-sn-glycero-3-phosphocholine + H2O = 1-O-(1Z-
CC alkenyl)-sn-glycero-3-phosphate + choline + H(+);
CC Xref=Rhea:RHEA:41588, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:77283, ChEBI:CHEBI:77287;
CC Evidence={ECO:0000269|PubMed:12176993};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41589;
CC Evidence={ECO:0000305|PubMed:12176993};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + H2O =
CC 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ethanolamine + H(+);
CC Xref=Rhea:RHEA:38927, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57603, ChEBI:CHEBI:74544, ChEBI:CHEBI:74971;
CC Evidence={ECO:0000269|PubMed:12354767};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38928;
CC Evidence={ECO:0000305|PubMed:12354767};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O = 1-
CC (9Z-octadecenoyl)-sn-glycero-3-phosphate + H(+) + L-serine;
CC Xref=Rhea:RHEA:38931, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33384, ChEBI:CHEBI:74544, ChEBI:CHEBI:74617;
CC Evidence={ECO:0000269|PubMed:12354767};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38932;
CC Evidence={ECO:0000305|PubMed:12354767};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:21240271, ECO:0000269|PubMed:27075612,
CC ECO:0000269|PubMed:27268273};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:21240271,
CC ECO:0000269|PubMed:27075612, ECO:0000269|PubMed:27268273};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:21240271, ECO:0000269|PubMed:27075612,
CC ECO:0000269|PubMed:27268273};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:21240271,
CC ECO:0000269|PubMed:27075612, ECO:0000269|PubMed:27268273};
CC -!- ACTIVITY REGULATION: Inhibited by vanadate (PubMed:27268273). Inhibited
CC by micromolar levels of bile salts, such as tauroursodeoxycholate. Not
CC inhibited by taurodeoxycholate. Not inhibited by hydroxysterols, such
CC as 7-hydroxycholesterol, testosterone, dexamethasone and prednisolone
CC (PubMed:27075612). Inhibited by EDTA and EGTA (PubMed:12354767).
CC {ECO:0000269|PubMed:12354767, ECO:0000269|PubMed:27075612,
CC ECO:0000269|PubMed:27268273}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12119361,
CC ECO:0000269|PubMed:12633853, ECO:0000269|PubMed:15985467,
CC ECO:0000269|PubMed:16436050, ECO:0000269|PubMed:21240271}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q64610-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q64610-2; Sequence=VSP_024018;
CC -!- TISSUE SPECIFICITY: Abundantly expressed in cerebrum and cerebellum.
CC Localized in secretory epithelial cells in the brain and the eye
CC including choroid plexus epithelial cells, ciliary epithelial cells,
CC iris pigment epithelial cells, and retinal pigment cells.
CC {ECO:0000269|PubMed:16436050, ECO:0000269|PubMed:7961762}.
CC -!- PTM: N-glycosylation, but not furin-cleavage, plays a critical role on
CC secretion and on lysoPLD activity. {ECO:0000250|UniProtKB:Q9R1E6}.
CC -!- PTM: The interdomain disulfide bond between Cys-413 and Cys-830 is
CC essential for catalytic activity. {ECO:0000250|UniProtKB:Q9R1E6}.
CC -!- SIMILARITY: Belongs to the nucleotide pyrophosphatase/phosphodiesterase
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
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DR EMBL; D28560; BAA05910.1; -; mRNA.
DR EMBL; DQ131564; AAZ99725.1; -; mRNA.
DR EMBL; BC081747; AAH81747.1; -; mRNA.
DR PIR; A55453; A55453.
DR RefSeq; NP_476445.2; NM_057104.2.
DR PDB; 2XR9; X-ray; 2.05 A; A=36-887.
DR PDB; 2XRG; X-ray; 3.20 A; A=1-887.
DR PDB; 5DLT; X-ray; 1.60 A; A=36-887.
DR PDB; 5DLV; X-ray; 2.00 A; A/B=36-887.
DR PDB; 5DLW; X-ray; 1.80 A; A=36-887.
DR PDB; 5IJQ; X-ray; 2.05 A; A=36-887.
DR PDB; 5IJS; X-ray; 2.20 A; A=36-887.
DR PDB; 5L0B; X-ray; 2.41 A; A/B=1-887.
DR PDB; 5L0E; X-ray; 3.06 A; A/B=1-887.
DR PDB; 5L0K; X-ray; 2.73 A; A/B=51-884.
DR PDB; 5LQQ; X-ray; 2.40 A; A=36-887.
DR PDB; 5M0D; X-ray; 2.40 A; A=36-887.
DR PDB; 5M0E; X-ray; 1.95 A; A=36-887.
DR PDB; 5M0M; X-ray; 2.10 A; A=36-887.
DR PDB; 5M0S; X-ray; 2.10 A; A=36-887.
DR PDB; 5S9L; X-ray; 1.90 A; A=28-887.
DR PDB; 5S9M; X-ray; 1.80 A; A=28-887.
DR PDB; 5S9N; X-ray; 1.80 A; A=28-887.
DR PDBsum; 2XR9; -.
DR PDBsum; 2XRG; -.
DR PDBsum; 5DLT; -.
DR PDBsum; 5DLV; -.
DR PDBsum; 5DLW; -.
DR PDBsum; 5IJQ; -.
DR PDBsum; 5IJS; -.
DR PDBsum; 5L0B; -.
DR PDBsum; 5L0E; -.
DR PDBsum; 5L0K; -.
DR PDBsum; 5LQQ; -.
DR PDBsum; 5M0D; -.
DR PDBsum; 5M0E; -.
DR PDBsum; 5M0M; -.
DR PDBsum; 5M0S; -.
DR PDBsum; 5S9L; -.
DR PDBsum; 5S9M; -.
DR PDBsum; 5S9N; -.
DR AlphaFoldDB; Q64610; -.
DR SMR; Q64610; -.
DR STRING; 10116.ENSRNOP00000047118; -.
DR BindingDB; Q64610; -.
DR ChEMBL; CHEMBL3826870; -.
DR GuidetoPHARMACOLOGY; 2901; -.
DR SwissLipids; SLP:000000394; -.
DR GlyGen; Q64610; 6 sites.
DR iPTMnet; Q64610; -.
DR Ensembl; ENSRNOT00000101657; ENSRNOP00000076476; ENSRNOG00000004089. [Q64610-1]
DR GeneID; 84050; -.
DR KEGG; rno:84050; -.
DR UCSC; RGD:69298; rat. [Q64610-1]
DR CTD; 5168; -.
DR RGD; 69298; Enpp2.
DR GeneTree; ENSGT00940000155778; -.
DR InParanoid; Q64610; -.
DR OrthoDB; 999163at2759; -.
DR PhylomeDB; Q64610; -.
DR BRENDA; 3.1.4.39; 5301.
DR SABIO-RK; Q64610; -.
DR EvolutionaryTrace; Q64610; -.
DR PRO; PR:Q64610; -.
DR Proteomes; UP000002494; Chromosome 7.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0047391; F:alkylglycerophosphoethanolamine phosphodiesterase activity; IDA:RGD.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0004622; F:lysophospholipase activity; IDA:UniProtKB.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004551; F:nucleotide diphosphatase activity; IEA:InterPro.
DR GO; GO:0004528; F:phosphodiesterase I activity; IMP:RGD.
DR GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0060326; P:cell chemotaxis; IMP:RGD.
DR GO; GO:0071276; P:cellular response to cadmium ion; IEP:RGD.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IEP:RGD.
DR GO; GO:0044849; P:estrous cycle; IEP:RGD.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0001953; P:negative regulation of cell-matrix adhesion; IDA:RGD.
DR GO; GO:0034638; P:phosphatidylcholine catabolic process; IDA:UniProtKB.
DR GO; GO:0009395; P:phospholipid catabolic process; ISO:RGD.
DR GO; GO:0006644; P:phospholipid metabolic process; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:RGD.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; ISO:RGD.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; IDA:RGD.
DR GO; GO:2000394; P:positive regulation of lamellipodium morphogenesis; ISO:RGD.
DR GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; IDA:RGD.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IDA:RGD.
DR GO; GO:0045765; P:regulation of angiogenesis; IEA:InterPro.
DR GO; GO:0030334; P:regulation of cell migration; ISO:RGD.
DR GO; GO:1903165; P:response to polycyclic arene; IEP:RGD.
DR GO; GO:0030149; P:sphingolipid catabolic process; ISS:UniProtKB.
DR Gene3D; 3.40.570.10; -; 1.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR001604; DNA/RNA_non-sp_Endonuclease.
DR InterPro; IPR044929; DNA/RNA_non-sp_Endonuclease_sf.
DR InterPro; IPR029881; ENPP2.
DR InterPro; IPR020821; Extracellular_endonuc_su_A.
DR InterPro; IPR044925; His-Me_finger_sf.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR InterPro; IPR020436; SMB_chordata.
DR InterPro; IPR036024; Somatomedin_B-like_dom_sf.
DR InterPro; IPR001212; Somatomedin_B_dom.
DR PANTHER; PTHR10151:SF21; PTHR10151:SF21; 1.
DR Pfam; PF01223; Endonuclease_NS; 1.
DR Pfam; PF01663; Phosphodiest; 1.
DR Pfam; PF01033; Somatomedin_B; 2.
DR PRINTS; PR00022; SOMATOMEDINB.
DR SMART; SM00892; Endonuclease_NS; 1.
DR SMART; SM00477; NUC; 1.
DR SMART; SM00201; SO; 2.
DR SUPFAM; SSF53649; SSF53649; 1.
DR SUPFAM; SSF54060; SSF54060; 1.
DR SUPFAM; SSF90188; SSF90188; 2.
DR PROSITE; PS00524; SMB_1; 2.
DR PROSITE; PS50958; SMB_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Chemotaxis;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hydrolase; Lipid degradation;
KW Lipid metabolism; Metal-binding; Obesity; Reference proteome; Repeat;
KW Secreted; Signal; Zinc.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:15985467,
FT ECO:0000269|PubMed:16436050"
FT PROPEP 28..35
FT /note="Removed by furin"
FT /evidence="ECO:0000269|PubMed:15985467,
FT ECO:0000269|PubMed:16436050"
FT /id="PRO_0000281651"
FT CHAIN 36..887
FT /note="Ectonucleotide pyrophosphatase/phosphodiesterase
FT family member 2"
FT /id="PRO_0000188569"
FT DOMAIN 54..97
FT /note="SMB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DOMAIN 98..142
FT /note="SMB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT REGION 586..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 854..875
FT /note="Required for secretion"
FT /evidence="ECO:0000250"
FT MOTIF 126..128
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT ACT_SITE 209
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:12633853,
FT ECO:0000269|PubMed:27268273"
FT BINDING 171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:21240271,
FT ECO:0000269|PubMed:27075612, ECO:0000269|PubMed:27268273,
FT ECO:0000269|PubMed:27660691, ECO:0007744|PDB:2XR9,
FT ECO:0007744|PDB:2XRG, ECO:0007744|PDB:5DLT,
FT ECO:0007744|PDB:5DLV, ECO:0007744|PDB:5DLW,
FT ECO:0007744|PDB:5IJQ, ECO:0007744|PDB:5IJS,
FT ECO:0007744|PDB:5L0B, ECO:0007744|PDB:5L0E,
FT ECO:0007744|PDB:5L0K, ECO:0007744|PDB:5LQQ"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:21240271,
FT ECO:0000269|PubMed:27075612, ECO:0000269|PubMed:27268273,
FT ECO:0000269|PubMed:27660691, ECO:0007744|PDB:2XR9,
FT ECO:0007744|PDB:2XRG, ECO:0007744|PDB:5DLT,
FT ECO:0007744|PDB:5DLV, ECO:0007744|PDB:5DLW,
FT ECO:0007744|PDB:5IJQ, ECO:0007744|PDB:5IJS,
FT ECO:0007744|PDB:5L0B, ECO:0007744|PDB:5L0E,
FT ECO:0007744|PDB:5L0K, ECO:0007744|PDB:5LQQ"
FT BINDING 210..213
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9R1E6"
FT BINDING 230
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:27075612,
FT ECO:0007744|PDB:5DLW"
FT BINDING 243..254
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9R1E6"
FT BINDING 306
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:27075612,
FT ECO:0007744|PDB:5DLV, ECO:0007744|PDB:5DLW"
FT BINDING 311
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:21240271,
FT ECO:0000269|PubMed:27075612, ECO:0000269|PubMed:27268273,
FT ECO:0000269|PubMed:27660691, ECO:0007744|PDB:2XR9,
FT ECO:0007744|PDB:2XRG, ECO:0007744|PDB:5DLT,
FT ECO:0007744|PDB:5DLV, ECO:0007744|PDB:5DLW,
FT ECO:0007744|PDB:5IJQ, ECO:0007744|PDB:5IJS,
FT ECO:0007744|PDB:5L0B, ECO:0007744|PDB:5L0E,
FT ECO:0007744|PDB:5L0K, ECO:0007744|PDB:5LQQ"
FT BINDING 315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:21240271,
FT ECO:0000269|PubMed:27075612, ECO:0000269|PubMed:27268273,
FT ECO:0000269|PubMed:27660691, ECO:0007744|PDB:2XR9,
FT ECO:0007744|PDB:2XRG, ECO:0007744|PDB:5DLT,
FT ECO:0007744|PDB:5DLV, ECO:0007744|PDB:5DLW,
FT ECO:0007744|PDB:5IJQ, ECO:0007744|PDB:5IJS,
FT ECO:0007744|PDB:5L0B, ECO:0007744|PDB:5L0E,
FT ECO:0007744|PDB:5L0K, ECO:0007744|PDB:5LQQ"
FT BINDING 358
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:21240271,
FT ECO:0000269|PubMed:27075612, ECO:0000269|PubMed:27268273,
FT ECO:0000269|PubMed:27660691, ECO:0007744|PDB:2XRG,
FT ECO:0007744|PDB:5DLT, ECO:0007744|PDB:5DLV,
FT ECO:0007744|PDB:5IJS, ECO:0007744|PDB:5L0B,
FT ECO:0007744|PDB:5L0E, ECO:0007744|PDB:5L0K,
FT ECO:0007744|PDB:5LQQ"
FT BINDING 359
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:21240271,
FT ECO:0000269|PubMed:27075612, ECO:0000269|PubMed:27268273,
FT ECO:0000269|PubMed:27660691, ECO:0007744|PDB:2XR9,
FT ECO:0007744|PDB:2XRG, ECO:0007744|PDB:5DLT,
FT ECO:0007744|PDB:5DLV, ECO:0007744|PDB:5DLW,
FT ECO:0007744|PDB:5IJQ, ECO:0007744|PDB:5IJS,
FT ECO:0007744|PDB:5L0B, ECO:0007744|PDB:5L0E,
FT ECO:0007744|PDB:5L0K, ECO:0007744|PDB:5LQQ"
FT BINDING 474
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:21240271,
FT ECO:0000269|PubMed:27075612, ECO:0000269|PubMed:27268273,
FT ECO:0000269|PubMed:27660691, ECO:0007744|PDB:2XR9,
FT ECO:0007744|PDB:2XRG, ECO:0007744|PDB:5DLT,
FT ECO:0007744|PDB:5DLV, ECO:0007744|PDB:5DLW,
FT ECO:0007744|PDB:5IJQ, ECO:0007744|PDB:5IJS,
FT ECO:0007744|PDB:5L0B, ECO:0007744|PDB:5L0E,
FT ECO:0007744|PDB:5L0K, ECO:0007744|PDB:5LQQ"
FT BINDING 764
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:21240271,
FT ECO:0000269|PubMed:27075612, ECO:0000269|PubMed:27268273,
FT ECO:0007744|PDB:2XR9, ECO:0007744|PDB:2XRG,
FT ECO:0007744|PDB:5DLT, ECO:0007744|PDB:5DLV,
FT ECO:0007744|PDB:5DLW, ECO:0007744|PDB:5IJQ,
FT ECO:0007744|PDB:5L0K, ECO:0007744|PDB:5LQQ"
FT BINDING 766
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:21240271,
FT ECO:0000269|PubMed:27075612, ECO:0000269|PubMed:27268273,
FT ECO:0007744|PDB:2XR9, ECO:0007744|PDB:2XRG,
FT ECO:0007744|PDB:5DLT, ECO:0007744|PDB:5DLV,
FT ECO:0007744|PDB:5DLW, ECO:0007744|PDB:5IJQ,
FT ECO:0007744|PDB:5IJS, ECO:0007744|PDB:5L0K,
FT ECO:0007744|PDB:5LQQ"
FT BINDING 768
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:21240271,
FT ECO:0000269|PubMed:27075612, ECO:0000269|PubMed:27268273,
FT ECO:0007744|PDB:2XR9, ECO:0007744|PDB:2XRG,
FT ECO:0007744|PDB:5DLT, ECO:0007744|PDB:5DLV,
FT ECO:0007744|PDB:5DLW, ECO:0007744|PDB:5IJQ,
FT ECO:0007744|PDB:5IJS, ECO:0007744|PDB:5L0K,
FT ECO:0007744|PDB:5LQQ"
FT BINDING 770
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:21240271,
FT ECO:0000269|PubMed:27075612, ECO:0000269|PubMed:27268273,
FT ECO:0007744|PDB:2XR9, ECO:0007744|PDB:2XRG,
FT ECO:0007744|PDB:5DLT, ECO:0007744|PDB:5DLV,
FT ECO:0007744|PDB:5DLW, ECO:0007744|PDB:5IJQ,
FT ECO:0007744|PDB:5IJS, ECO:0007744|PDB:5L0K"
FT BINDING 772
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:21240271,
FT ECO:0000269|PubMed:27075612, ECO:0000269|PubMed:27268273,
FT ECO:0007744|PDB:2XR9, ECO:0007744|PDB:2XRG,
FT ECO:0007744|PDB:5DLT, ECO:0007744|PDB:5DLV,
FT ECO:0007744|PDB:5DLW, ECO:0007744|PDB:5IJQ,
FT ECO:0007744|PDB:5IJS, ECO:0007744|PDB:5L0K,
FT ECO:0007744|PDB:5LQQ"
FT SITE 877
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q9R1E6"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 524
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21240271"
FT CARBOHYD 610
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 831
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 58..75
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350,
FT ECO:0000269|PubMed:21240271"
FT DISULFID 62..93
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350,
FT ECO:0000269|PubMed:21240271"
FT DISULFID 73..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350,
FT ECO:0000269|PubMed:21240271"
FT DISULFID 79..85
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350,
FT ECO:0000269|PubMed:21240271"
FT DISULFID 102..119
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350,
FT ECO:0000269|PubMed:21240271"
FT DISULFID 107..137
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350,
FT ECO:0000269|PubMed:21240271"
FT DISULFID 117..130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350,
FT ECO:0000269|PubMed:21240271"
FT DISULFID 123..129
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350,
FT ECO:0000269|PubMed:21240271"
FT DISULFID 148..194
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350,
FT ECO:0000269|PubMed:21240271"
FT DISULFID 156..350
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350,
FT ECO:0000269|PubMed:21240271"
FT DISULFID 366..468
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350,
FT ECO:0000269|PubMed:21240271"
FT DISULFID 413..830
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350,
FT ECO:0000269|PubMed:21240271"
FT DISULFID 566..691
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350,
FT ECO:0000269|PubMed:21240271"
FT DISULFID 568..676
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350,
FT ECO:0000269|PubMed:21240271"
FT DISULFID 799..809
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350,
FT ECO:0000269|PubMed:21240271"
FT VAR_SEQ 591..615
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16436050"
FT /id="VSP_024018"
FT MUTAGEN 13
FT /note="I->L: No effect on secretion."
FT /evidence="ECO:0000269|PubMed:15985467"
FT MUTAGEN 16..18
FT /note="FTF->VLS: No effect on secretion."
FT /evidence="ECO:0000269|PubMed:15985467"
FT MUTAGEN 18..21
FT /note="FAIS->SVCV: No effect on secretion."
FT /evidence="ECO:0000269|PubMed:15985467"
FT MUTAGEN 21..24
FT /note="SVNI->VLTT: No effect on secretion."
FT /evidence="ECO:0000269|PubMed:15985467"
FT MUTAGEN 24..25
FT /note="IC->TI: No effect on secretion."
FT /evidence="ECO:0000269|PubMed:15985467"
FT MUTAGEN 28..30
FT /note="FTA->CIF: No effect on secretion."
FT /evidence="ECO:0000269|PubMed:15985467"
FT MUTAGEN 171
FT /note="D->N: Abolishes lysophospholipase D activity."
FT /evidence="ECO:0000269|PubMed:12633853"
FT MUTAGEN 209
FT /note="T->A: Abolishes lysophospholipase D activity."
FT /evidence="ECO:0000269|PubMed:12633853"
FT MUTAGEN 209
FT /note="T->S: 15% of wild-type lysophospholipase D
FT activity."
FT /evidence="ECO:0000269|PubMed:12633853"
FT MUTAGEN 311
FT /note="D->N: Abolishes lysophospholipase D activity."
FT /evidence="ECO:0000269|PubMed:12633853"
FT MUTAGEN 315
FT /note="H->Q: 20% of wild-type lysophospholipase D
FT activity."
FT /evidence="ECO:0000269|PubMed:12633853"
FT MUTAGEN 430
FT /note="K->A: Impaired secretion. No effect on
FT lysophospholipase activity."
FT /evidence="ECO:0000269|PubMed:21240271"
FT MUTAGEN 764..768
FT /note="DYNYD->SYAYS: Abolishes secretion. Strongly reduced
FT lysophospholipase activity."
FT /evidence="ECO:0000269|PubMed:21240271"
FT CONFLICT 97
FT /note="A -> V (in Ref. 1; BAA05910)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="C -> S (in Ref. 1; BAA05910)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="S -> P (in Ref. 1; BAA05910)"
FT /evidence="ECO:0000305"
FT CONFLICT 147..162
FT /note="DCEEIKVPECPAGFVR -> AARNQSSECLQVCP (in Ref. 1;
FT BAA05910)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="A -> V (in Ref. 1; BAA05910)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="M -> T (in Ref. 1; BAA05910)"
FT /evidence="ECO:0000305"
FT TURN 59..63
FT /evidence="ECO:0007829|PDB:5DLT"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:5DLV"
FT TURN 77..83
FT /evidence="ECO:0007829|PDB:5DLT"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:5DLT"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:5DLT"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:5DLT"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:5L0K"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:5DLT"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:5DLT"
FT HELIX 133..137
FT /evidence="ECO:0007829|PDB:5DLT"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:5DLT"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:5DLT"
FT HELIX 175..180
FT /evidence="ECO:0007829|PDB:5DLT"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:5DLT"
FT HELIX 186..194
FT /evidence="ECO:0007829|PDB:5DLT"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:5DLT"
FT HELIX 209..218
FT /evidence="ECO:0007829|PDB:5DLT"
FT HELIX 222..225
FT /evidence="ECO:0007829|PDB:5DLT"
FT STRAND 230..234
FT /evidence="ECO:0007829|PDB:5DLT"
FT TURN 235..238
FT /evidence="ECO:0007829|PDB:5DLT"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:5DLT"
FT STRAND 243..246
FT /evidence="ECO:0007829|PDB:5DLT"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:5DLT"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:5DLT"
FT HELIX 259..265
FT /evidence="ECO:0007829|PDB:5DLT"
FT HELIX 281..292
FT /evidence="ECO:0007829|PDB:5DLT"
FT TURN 296..298
FT /evidence="ECO:0007829|PDB:5DLT"
FT STRAND 301..310
FT /evidence="ECO:0007829|PDB:5DLT"
FT HELIX 311..317
FT /evidence="ECO:0007829|PDB:5DLT"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:5DLT"
FT HELIX 325..344
FT /evidence="ECO:0007829|PDB:5DLT"
FT TURN 348..350
FT /evidence="ECO:0007829|PDB:5DLT"
FT STRAND 352..358
FT /evidence="ECO:0007829|PDB:5DLT"
FT STRAND 368..371
FT /evidence="ECO:0007829|PDB:5DLT"
FT HELIX 372..374
FT /evidence="ECO:0007829|PDB:5DLT"
FT HELIX 379..381
FT /evidence="ECO:0007829|PDB:5DLT"
FT STRAND 382..385
FT /evidence="ECO:0007829|PDB:5DLT"
FT STRAND 387..395
FT /evidence="ECO:0007829|PDB:5DLT"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:5L0B"
FT HELIX 404..410
FT /evidence="ECO:0007829|PDB:5DLT"
FT STRAND 419..424
FT /evidence="ECO:0007829|PDB:5DLT"
FT HELIX 425..427
FT /evidence="ECO:0007829|PDB:5DLT"
FT HELIX 430..432
FT /evidence="ECO:0007829|PDB:5DLT"
FT STRAND 442..447
FT /evidence="ECO:0007829|PDB:5DLT"
FT STRAND 452..456
FT /evidence="ECO:0007829|PDB:5DLT"
FT HELIX 457..459
FT /evidence="ECO:0007829|PDB:5DLW"
FT STRAND 471..473
FT /evidence="ECO:0007829|PDB:5DLW"
FT HELIX 481..483
FT /evidence="ECO:0007829|PDB:5DLT"
FT STRAND 487..494
FT /evidence="ECO:0007829|PDB:5DLT"
FT STRAND 496..499
FT /evidence="ECO:0007829|PDB:5DLT"
FT HELIX 505..507
FT /evidence="ECO:0007829|PDB:5DLT"
FT HELIX 508..515
FT /evidence="ECO:0007829|PDB:5DLT"
FT TURN 527..530
FT /evidence="ECO:0007829|PDB:5DLT"
FT HELIX 531..533
FT /evidence="ECO:0007829|PDB:5DLT"
FT STRAND 534..536
FT /evidence="ECO:0007829|PDB:5DLT"
FT HELIX 559..561
FT /evidence="ECO:0007829|PDB:5DLT"
FT HELIX 577..581
FT /evidence="ECO:0007829|PDB:5DLT"
FT TURN 583..586
FT /evidence="ECO:0007829|PDB:5DLT"
FT HELIX 587..591
FT /evidence="ECO:0007829|PDB:5DLV"
FT HELIX 617..620
FT /evidence="ECO:0007829|PDB:5DLT"
FT STRAND 634..638
FT /evidence="ECO:0007829|PDB:5DLT"
FT STRAND 643..647
FT /evidence="ECO:0007829|PDB:5DLT"
FT TURN 648..651
FT /evidence="ECO:0007829|PDB:5DLT"
FT STRAND 652..660
FT /evidence="ECO:0007829|PDB:5DLT"
FT HELIX 671..673
FT /evidence="ECO:0007829|PDB:5DLT"
FT HELIX 685..687
FT /evidence="ECO:0007829|PDB:5DLT"
FT HELIX 691..696
FT /evidence="ECO:0007829|PDB:5DLT"
FT STRAND 701..706
FT /evidence="ECO:0007829|PDB:5DLT"
FT HELIX 708..710
FT /evidence="ECO:0007829|PDB:5DLT"
FT HELIX 714..717
FT /evidence="ECO:0007829|PDB:5DLT"
FT HELIX 718..721
FT /evidence="ECO:0007829|PDB:5DLT"
FT HELIX 723..725
FT /evidence="ECO:0007829|PDB:5DLT"
FT STRAND 726..729
FT /evidence="ECO:0007829|PDB:5DLT"
FT HELIX 731..742
FT /evidence="ECO:0007829|PDB:5DLT"
FT HELIX 744..752
FT /evidence="ECO:0007829|PDB:5DLT"
FT STRAND 754..762
FT /evidence="ECO:0007829|PDB:5DLT"
FT STRAND 768..770
FT /evidence="ECO:0007829|PDB:5DLT"
FT HELIX 774..776
FT /evidence="ECO:0007829|PDB:5DLT"
FT STRAND 790..801
FT /evidence="ECO:0007829|PDB:5DLT"
FT HELIX 806..808
FT /evidence="ECO:0007829|PDB:5DLT"
FT STRAND 813..821
FT /evidence="ECO:0007829|PDB:5DLT"
FT TURN 830..833
FT /evidence="ECO:0007829|PDB:5DLT"
FT HELIX 836..838
FT /evidence="ECO:0007829|PDB:5DLT"
FT HELIX 840..846
FT /evidence="ECO:0007829|PDB:5DLT"
FT HELIX 851..858
FT /evidence="ECO:0007829|PDB:5DLT"
FT STRAND 859..861
FT /evidence="ECO:0007829|PDB:5M0E"
FT STRAND 865..868
FT /evidence="ECO:0007829|PDB:5M0E"
FT HELIX 870..878
FT /evidence="ECO:0007829|PDB:5DLT"
SQ SEQUENCE 887 AA; 101576 MW; 40AD1C957F833869 CRC64;
MARQGCLGSF QVISLFTFAI SVNICLGFTA SRIKRAEWDE GPPTVLSDSP WTNTSGSCKG
RCFELQEVGP PDCRCDNLCK SYSSCCHDFD ELCLKTARGW ECTKDRCGEV RNEENACHCS
EDCLSRGDCC TNYQVVCKGE SHWVDDDCEE IKVPECPAGF VRPPLIIFSV DGFRASYMKK
GSKVMPNIEK LRSCGTHAPY MRPVYPTKTF PNLYTLATGL YPESHGIVGN SMYDPVFDAS
FHLRGREKFN HRWWGGQPLW ITATKQGVRA GTFFWSVSIP HERRILTILQ WLSLPDNERP
SVYAFYSEQP DFSGHKYGPF GPEMTNPLRE IDKTVGQLMD GLKQLRLHRC VNVIFVGDHG
MEDVTCDRTE FLSNYLTNVD DITLVPGTLG RIRAKSINNS KYDPKTIIAN LTCKKPDQHF
KPYMKQHLPK RLHYANNRRI EDIHLLVDRR WHVARKPLDV YKKPSGKCFF QGDHGFDNKV
NSMQTVFVGY GPTFKYRTKV PPFENIELYN VMCDLLGLKP APNNGTHGSL NHLLRTNTFR
PTMPDEVSRP NYPGIMYLQS EFDLGCTCDD KVEPKNKLEE LNKRLHTKGS TEAETGKFRG
SKHENKKNLN GSVEPRKERH LLYGRPAVLY RTSYDILYHT DFESGYSEIF LMPLWTSYTI
SKQAEVSSIP EHLTNCVRPD VRVSPGFSQN CLAYKNDKQM SYGFLFPPYL SSSPEAKYDA
FLVTNMVPMY PAFKRVWAYF QRVLVKKYAS ERNGVNVISG PIFDYNYDGL RDTEDEIKQY
VEGSSIPVPT HYYSIITSCL DFTQPADKCD GPLSVSSFIL PHRPDNDESC NSSEDESKWV
EELMKMHTAR VRDIEHLTGL DFYRKTSRSY SEILTLKTYL HTYESEI
