Enpp2
entrez
84050
canonical
uniprot
Q64610
canonical
ensembl
ENSRNOG00000004089
resolver
ensembl
ENSRNOG00055021831
resolver
ensembl
ENSRNOG00060003167
resolver
ensembl
ENSRNOG00065014947
resolver
ensp
ENSRNOP00000005561
resolver
ensp
ENSRNOP00000047118
resolver
ensp
ENSRNOP00000076476
resolver
ensp
ENSRNOP00000090400
resolver
ensp
ENSRNOP00000109145
resolver
enst
ENSRNOT00000005561
resolver
enst
ENSRNOT00000118544
resolver
enst
ENSRNOT00000136044
resolver
genesymbol
Enpp2
resolver
genesymbol_syn
Atx
resolver
genesymbol_syn
Npps2
resolver
uniprot
A0A8I6ADH1
resolver
uniprot
A0ABK0M387
resolver
uniprot
D3ZES5
resolver
uniprot
Q66HQ0
resolver
uniprot_entry
A0A8I6ADH1_RAT
resolver
uniprot_entry
A0ABK0M387_RAT
resolver
uniprot_entry
D3ZES5_RAT
resolver
uniprot_entry
ENPP2_RAT
resolver
uniprot_sec
Q66HQ0
resolver
activity_regulation
ACTIVITY REGULATION: 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). Inhibited by EDTA and EGTA (PubMed:12354767). {ECO:0000269|PubMed:12354767, ECO:0000269|PubMed:27075612, ECO:0000269|PubMed:27268273}.
uniprot
proteins
amino_acid_sequence
MARQGCLGSFQVISLFTFAISVNICLGFTASRIKRAEWDEGPPTVLSDSPWTNTSGSCKGRCFELQEVGPPDCRCDNLCKSYSSCCHDFDELCLKTARGWECTKDRCGEVRNEENACHCSEDCLSRGDCCTNYQVVCKGESHWVDDDCEEIKVPECPAGFVRPPLIIFSVDGFRASYMKKGSKVMPNIEKLRSCGTHAPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDASFHLRGREKFNHRWWGGQPLWITATKQGVRAGTFFWSVSIPHERRILTILQWLSLPDNERPSVYAFYSEQPDFSGHKYGPFGPEMTNPLREIDKTVGQLMDGLKQLRLHRCVNVIFVGDHGMEDVTCDRTEFLSNYLTNVDDITLVPGTLGRIRAKSINNSKYDPKTIIANLTCKKPDQHFKPYMKQHLPKRLHYANNRRIEDIHLLVDRRWHVARKPLDVYKKPSGKCFFQGDHGFDNKVNSMQTVFVGYGPTFKYRTKVPPFENIELYNVMCDLLGLKPAPNNGTHGSLNHLLRTNTFRPTMPDEVSRPNYPGIMYLQSEFDLGCTCDDKVEPKNKLEELNKRLHTKGSTEAETGKFRGSKHENKKNLNGSVEPRKERHLLYGRPAVLYRTSYDILYHTDFESGYSEIFLMPLWTSYTISKQAEVSSIPEHLTNCVRPDVRVSPGFSQNCLAYKNDKQMSYGFLFPPYLSSSPEAKYDAFLVTNMVPMYPAFKRVWAYFQRVLVKKYASERNGVNVISGPIFDYNYDGLRDTEDEIKQYVEGSSIPVPTHYYSIITSCLDFTQPADKCDGPLSVSSFILPHRPDNDESCNSSEDESKWVEELMKMHTARVRDIEHLTGLDFYRKTSRSYSEILTLKTYLHTYESEI
uniprot
proteins
ec_number
3.1.4.39
uniprot
proteins
ec_number
3.1.4.4
uniprot
proteins
function
FUNCTION: Secreted lysophospholipase D that hydrolyzes lysophospholipids to produce the signaling molecule lysophosphatidic acid (LPA) in extracellular fluids (PubMed:12354767, PubMed:12633853, PubMed:27075612, PubMed:27268273, PubMed:27660691, PubMed:29259743). Its major substrate is lysophosphatidylcholine (PubMed:12119361, PubMed:12176993, PubMed:27075612, PubMed:27268273, PubMed:27660691). Can also 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 (By similarity). Required for LPA production in activated platelets, cleaves the sn-1 lysophospholipids to generate sn-1 lysophosphatidic acids containing predominantly 18:2 and 20:4 fatty acids (By similarity). Shows a preference for the sn-1 to the sn-2 isomer of 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF) (By similarity). {ECO:0000250|UniProtKB:Q13822, ECO:0000269|PubMed:12119361, ECO:0000269|PubMed:12176993, ECO:0000269|PubMed:12354767, ECO:0000269|PubMed:12633853, ECO:0000269|PubMed:15985467, ECO:0000269|PubMed:27075612, ECO:0000269|PubMed:27268273, ECO:0000269|PubMed:27660691, ECO:0000269|PubMed:29259743}.
uniprot
proteins
mass_dalton
101576
uniprot
proteins
mutagenesis
MUTAGEN 13; /note="I->L: No effect on secretion."; /evidence="ECO:0000269|PubMed:15985467"; MUTAGEN 16..18; /note="FTF->VLS: No effect on secretion."; /evidence="ECO:0000269|PubMed:15985467"; MUTAGEN 18..21; /note="FAIS->SVCV: No effect on secretion."; /evidence="ECO:0000269|PubMed:15985467"; MUTAGEN 21..24; /note="SVNI->VLTT: No effect on secretion."; /evidence="ECO:0000269|PubMed:15985467"; MUTAGEN 24..25; /note="IC->TI: No effect on secretion."; /evidence="ECO:0000269|PubMed:15985467"; MUTAGEN 28..30; /note="FTA->CIF: No effect on secretion."; /evidence="ECO:0000269|PubMed:15985467"; MUTAGEN 171; /note="D->N: Abolishes lysophospholipase D activity."; /evidence="ECO:0000269|PubMed:12633853"; MUTAGEN 209; /note="T->A: Abolishes lysophospholipase D activity."; /evidence="ECO:0000269|PubMed:12633853"; MUTAGEN 209; /note="T->S: 15% of wild-type lysophospholipase D activity."; /evidence="ECO:0000269|PubMed:12633853"; MUTAGEN 311; /note="D->N: Abolishes lysophospholipase D activity."; /evidence="ECO:0000269|PubMed:12633853"; MUTAGEN 315; /note="H->Q: 20% of wild-type lysophospholipase D activity."; /evidence="ECO:0000269|PubMed:12633853"; MUTAGEN 430; /note="K->A: Impaired secretion. No effect on lysophospholipase activity."; /evidence="ECO:0000269|PubMed:21240271"; MUTAGEN 764..768; /note="DYNYD->SYAYS: Abolishes secretion. Strongly reduced lysophospholipase activity."; /evidence="ECO:0000269|PubMed:21240271
uniprot
proteins
post_translational_modification
PTM: N-glycosylation, but not furin-cleavage, plays a critical role on secretion and on lysoPLD activity. {ECO:0000250|UniProtKB:Q9R1E6}.; PTM: The interdomain disulfide bond between Cys-413 and Cys-830 is essential for catalytic activity. {ECO:0000250|UniProtKB:Q9R1E6}.
uniprot
proteins
protein_family
Nucleotide pyrophosphatase/phosphodiesterase family
uniprot
proteins
pubmed
12119361
uniprot
proteins
pubmed
12176993
uniprot
proteins
pubmed
12354767
uniprot
proteins
pubmed
12633853
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15985467
uniprot
proteins
pubmed
16436050
uniprot
proteins
pubmed
21240271
uniprot
proteins
pubmed
27075612
uniprot
proteins
pubmed
27268273
uniprot
proteins
pubmed
27660691
uniprot
proteins
pubmed
29259743
uniprot
proteins
pubmed
7961762
uniprot
proteins
sequence_length
887
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12119361, ECO:0000269|PubMed:12633853, ECO:0000269|PubMed:15985467, ECO:0000269|PubMed:16436050, ECO:0000269|PubMed:21240271}.
uniprot
proteins