Enpp2
entrez
18606
canonical
uniprot
Q9R1E6
canonical
ensembl
ENSMUSG00000022425
resolver
ensp
ENSMUSP00000036180
resolver
ensp
ENSMUSP00000128941
resolver
ensp
ENSMUSP00000132640
resolver
ensp
ENSMUSP00000133877
resolver
ensp
ENSMUSP00000186537
resolver
ensp
ENSMUSP00000186539
resolver
ensp
ENSMUSP00000186541
resolver
ensp
ENSMUSP00000186542
resolver
ensp
ENSMUSP00000186544
resolver
enst
ENSMUST00000173516
resolver
genesymbol
Enpp2
resolver
genesymbol_syn
Npps2
resolver
genesymbol_syn
Pdnp2
resolver
uniprot
A8UH85
resolver
uniprot
A8UH93
resolver
uniprot
B2ZP54
resolver
uniprot
G3UXY9
resolver
uniprot
Q6PDE0
resolver
uniprot
Q99LG9
resolver
uniprot_entry
ENPP2_MOUSE
resolver
uniprot_entry
G3UXY9_MOUSE
resolver
uniprot_sec
A8UH85
resolver
uniprot_sec
A8UH93
resolver
uniprot_sec
B2ZP54
resolver
uniprot_sec
Q6PDE0
resolver
uniprot_sec
Q99LG9
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by EDTA and EGTA. {ECO:0000269|PubMed:18175805}.
uniprot
proteins
amino_acid_sequence
MARQGCFGSYQVISLFTFAIGVNLCLGFTASRIKRAEWDEGPPTVLSDSPWTNTSGSCKGRCFELQEVGPPDCRCDNLCKSYSSCCHDFDELCLKTARGWECTKDRCGEVRNEENACHCSEDCLSRGDCCTNYQVVCKGESHWVDDDCEEIRVPECPAGFVRPPLIIFSVDGFRASYMKKGSKVMPNIEKLRSCGTHAPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDATFHLRGREKFNHRWWGGQPLWITATKQGVRAGTFFWSVSIPHERRILTILQWLSLPDNERPSVYAFYSEQPDFSGHKYGPFGPEMTNPLREIDKTVGQLMDGLKQLKLHRCVNVIFVGDHGMEDVTCDRTEFLSNYLTNVDDITLVPGTLGRIRPKIPNNLKYDPKAIIANLTCKKPDQHFKPYMKQHLPKRLHYANNRRIEDLHLLVERRWHVARKPLDVYKKPSGKCFFQGDHGFDNKVNSMQTVFVGYGPTFKYRTKVPPFENIELYNVMCDLLGLKPAPNNGTHGSLNHLLRTNTFRPTLPEEVSRPNYPGIMYLQSDFDLGCTCDDKVEPKNKLEELNKRLHTKGSTEERHLLYGRPAVLYRTSYDILYHTDFESGYSEIFLMPLWTSYTISKQAEVSSIPEHLTNCVRPDVRVSPGFSQNCLAYKNDKQMSYGFLFPPYLSSSPEAKYDAFLVTNMVPMYPAFKRVWTYFQRVLVKKYASERNGVNVISGPIFDYNYNGLRDIEDEIKQYVEGSSIPVPTHYYSIITSCLDFTQPADKCDGPLSVSSFILPHRPDNDESCNSSEDESKWVEELMKMHTARVRDIEHLTGLDFYRKTSRSYSEILTLKTYLHTYESEI
uniprot
proteins
disease_involvement
DISEASE: Note=May contribute to obesity (PubMed:15700135). {ECO:0000269|PubMed:15700135}.
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:17208043, PubMed:27780639, PubMed:28414242). Its major substrate is lysophosphatidylcholine (PubMed:17208043, PubMed:27780639). Can also act on sphingosylphosphorylcholine producing sphingosine-1-phosphate, a modulator of cell motility. Can hydrolyze, in vitro, bis-pNPP, to some extent pNP-TMP, and barely ATP (PubMed:18175805). 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 (By similarity). Possible involvement in cell proliferation and adipose tissue development (Probable). 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:17208043, ECO:0000269|PubMed:18175805, ECO:0000269|PubMed:21240269, ECO:0000269|PubMed:27780639, ECO:0000269|PubMed:28414242, ECO:0000305|PubMed:15700135}.
uniprot
proteins
mass_dalton
98885
uniprot
proteins
mutagenesis
MUTAGEN 12..27; /note="Missing: Complete inhibition of secretion."; /evidence="ECO:0000269|PubMed:17208043"; MUTAGEN 12..22; /note="Missing: Complete inhibition of secretion."; /evidence="ECO:0000269|PubMed:17208043"; MUTAGEN 23..27; /note="Missing: No effect on secretion."; /evidence="ECO:0000269|PubMed:17208043"; MUTAGEN 23; /note="Missing: No effect on secretion."; /evidence="ECO:0000269|PubMed:17208043"; MUTAGEN 25; /note="Missing: No effect on secretion."; /evidence="ECO:0000269|PubMed:17208043"; MUTAGEN 27..35; /note="Missing: No effect on secretion nor lysophospholipase activity."; /evidence="ECO:0000269|PubMed:17208043"; MUTAGEN 27..30; /note="Missing: No effect on secretion."; /evidence="ECO:0000269|PubMed:17208043"; MUTAGEN 27; /note="Missing: No effect on secretion."; /evidence="ECO:0000269|PubMed:17208043"; MUTAGEN 30..41; /note="Missing: No effect on secretion nor lysophospholipase activity."; /evidence="ECO:0000269|PubMed:17208043"; MUTAGEN 30..33; /note="Missing: No effect on secretion nor lysophospholipase activity."; /evidence="ECO:0000269|PubMed:17208043"; MUTAGEN 32..35; /note="Missing: No effect on secretion nor lysophospholipase activity."; /evidence="ECO:0000269|PubMed:17208043"; MUTAGEN 36..40; /note="Missing: No effect on secretion nor lysophospholipase activity."; /evidence="ECO:0000269|PubMed:17208043"; MUTAGEN 53; /note="Missing: No effect on secretion; slightly decreases lysophospholipase activity. Almost complete loss of lysophospholipase activity; when associated with N-410 del."; /evidence="ECO:0000269|PubMed:17208043"; MUTAGEN 210; /note="F->A: Reduced lysophospholipase activity."; /evidence="ECO:0000269|PubMed:21240269"; MUTAGEN 213; /note="L->A: Reduced lysophospholipase activity."; /evidence="ECO:0000269|PubMed:21240269"; MUTAGEN 230; /note="N->A: Reduced lysophospholipase activity."; /evidence="ECO:0000269|PubMed:21240269"; MUTAGEN 243; /note="L->A: Reduced lysophospholipase activity."; /evidence="ECO:0000269|PubMed:21240269"; MUTAGEN 247; /note="E->A: Reduced lysophospholipase activity."; /evidence="ECO:0000269|PubMed:21240269"; MUTAGEN 249; /note="F->A: Reduced lysophospholipase activity."; /evidence="ECO:0000269|PubMed:21240269"; MUTAGEN 410; /note="Missing: No effect on secretion; greatly inhibits lysoPLD activity. Inhibits secretion. Almost complete loss of lysoPLD activity; when associated with N-53 del."; /evidence="ECO:0000269|PubMed:17208043"; MUTAGEN 512; /note="M->A: Reduced lysophospholipase activity."; MUTAGEN 851..853; /note="LKT->AAA,RRR,SSS: No catalytic activity."; /evidence="ECO:0000269|PubMed:19329427"; MUTAGEN 851; /note="L->A: No effect."; /evidence="ECO:0000269|PubMed:19329427"; MUTAGEN 852; /note="K->A,R: Strongly reduced catalytic activity."; /evidence="ECO:0000269|PubMed:19329427"; MUTAGEN 853; /note="T->A: No effect."; /evidence="ECO:0000269|PubMed:19329427
uniprot
proteins
post_translational_modification
PTM: N-glycosylation, but not furin-cleavage, plays a critical role on secretion and on lysoPLD activity. Secretion requires simultaneous glycosylation on Asn-53 and Asn-410, while probable glycosylation of Asn-410 has a preferential role on lysoPLD activity. Not O-glycosylated. {ECO:0000269|PubMed:17208043, ECO:0000269|PubMed:21240269, ECO:0000269|PubMed:23688339}.; PTM: The interdomain disulfide bond between Cys-413 and Cys-805 is essential for catalytic activity. {ECO:0000269|PubMed:19329427}.
uniprot
proteins
protein_family
Nucleotide pyrophosphatase/phosphodiesterase family
uniprot
proteins
pubmed
10702660
uniprot
proteins
pubmed
12533192
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15700135
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17208043
uniprot
proteins
pubmed
18175805
uniprot
proteins
pubmed
19329427
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21240269
uniprot
proteins
pubmed
23027977
uniprot
proteins
pubmed
23688339
uniprot
proteins
pubmed
27780639
uniprot
proteins
pubmed
28414242
uniprot
proteins
pubmed
29259743
uniprot
proteins
sequence_length
862
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17208043, ECO:0000269|PubMed:19329427, ECO:0000269|PubMed:21240269}.
uniprot
proteins