ENPP2
entrez
5168
canonical
uniprot
Q13822
canonical
ensembl
ENSG00000136960
resolver
ensp
ENSP00000075322
resolver
ensp
ENSP00000259486
resolver
ensp
ENSP00000403315
resolver
ensp
ENSP00000428291
resolver
ensp
ENSP00000544395
resolver
ensp
ENSP00000544397
resolver
ensp
ENSP00000544400
resolver
ensp
ENSP00000645354
resolver
ensp
ENSP00000645356
resolver
enst
ENST00000427067
resolver
genesymbol
ENPP2
resolver
genesymbol_syn
ATX
resolver
genesymbol_syn
PDNP2
resolver
hgnc
HGNC:3357
resolver
uniprot
A8UHA1
resolver
uniprot
E7EUF1
resolver
uniprot
E9PHP7
resolver
uniprot
Q13827
resolver
uniprot
Q14555
resolver
uniprot
Q15117
resolver
uniprot
Q9UCQ8
resolver
uniprot
Q9UCR0
resolver
uniprot
Q9UCR1
resolver
uniprot
Q9UCR2
resolver
uniprot
Q9UCR3
resolver
uniprot
Q9UCR4
resolver
uniprot_entry
E7EUF1_HUMAN
resolver
uniprot_entry
ENPP2_HUMAN
resolver
uniprot_sec
A8UHA1
resolver
uniprot_sec
E9PHP7
resolver
uniprot_sec
Q13827
resolver
uniprot_sec
Q14555
resolver
uniprot_sec
Q15117
resolver
uniprot_sec
Q9UCQ8
resolver
uniprot_sec
Q9UCR0
resolver
uniprot_sec
Q9UCR1
resolver
uniprot_sec
Q9UCR2
resolver
uniprot_sec
Q9UCR3
resolver
uniprot_sec
Q9UCR4
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by lysophosphatidic acid (LPA) and sphingosine-1-phosphate (S1P). Inhibited by EDTA and EGTA (Probable). {ECO:0000305|PubMed:15769751, ECO:0000305|PubMed:18175805, ECO:0000305|PubMed:21240271}.
uniprot
proteins
amino_acid_sequence
MARRSSFQSCQIISLFTFAVGVNICLGFTAHRIKRAEGWEEGPPTVLSDSPWTNISGSCKGRCFELQEAGPPDCRCDNLCKSYTSCCHDFDELCLKTARGWECTKDRCGEVRNEENACHCSEDCLARGDCCTNYQVVCKGESHWVDDDCEEIKAAECPAGFVRPPLIIFSVDGFRASYMKKGSKVMPNIEKLRSCGTHSPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDATFHLRGREKFNHRWWGGQPLWITATKQGVKAGTFFWSVVIPHERRILTILQWLTLPDHERPSVYAFYSEQPDFSGHKYGPFGPEMTNPLREIDKIVGQLMDGLKQLKLHRCVNVIFVGDHGMEDVTCDRTEFLSNYLTNVDDITLVPGTLGRIRSKFSNNAKYDPKAIIANLTCKKPDQHFKPYLKQHLPKRLHYANNRRIEDIHLLVERRWHVARKPLDVYKKPSGKCFFQGDHGFDNKVNSMQTVFVGYGSTFKYKTKVPPFENIELYNVMCDLLGLKPAPNNGTHGSLNHLLRTNTFRPTMPEEVTRPNYPGIMYLQSDFDLGCTCDDKVEPKNKLDELNKRLHTKGSTEERHLLYGRPAVLYRTRYDILYHTDFESGYSEIFLMPLWTSYTVSKQAEVSSVPDHLTSCVRPDVRVSPSFSQNCLAYKNDKQMSYGFLFPPYLSSSPEAKYDAFLVTNMVPMYPAFKRVWNYFQRVLVKKYASERNGVNVISGPIFDYDYDGLHDTEDKIKQYVEGSSIPVPTHYYSIITSCLDFTQPADKCDGPLSVSSFILPHRPDNEESCNSSEDESKWVEELMKMHTARVRDIEHLTSLDFFRKTSRSYPEILTLKTYLHTYESEI
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:14500380, PubMed:15769751, PubMed:26371182, PubMed:27754931). Its major substrate is lysophosphatidylcholine (PubMed:12176993, PubMed:14500380, PubMed:27754931). Can also act on sphingosylphosphorylcholine producing sphingosine-1-phosphate, a modulator of cell motility (PubMed:14500380). Can hydrolyze, in vitro, bis-pNPP, to some extent pNP-TMP, and barely ATP (PubMed:12176993, PubMed:15769751). 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 (PubMed:11559573). Stimulates migration of melanoma cells, probably via a pertussis toxin-sensitive G protein (PubMed:1733949). May have a role in induction of parturition (PubMed:12176993). 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 (PubMed:21393252). Shows a preference for the sn-1 to the sn-2 isomer of 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF) (PubMed:21393252). {ECO:0000269|PubMed:11559573, ECO:0000269|PubMed:12176993, ECO:0000269|PubMed:12354767, ECO:0000269|PubMed:14500380, ECO:0000269|PubMed:15769751, ECO:0000269|PubMed:1733949, ECO:0000269|PubMed:21240271, ECO:0000269|PubMed:21393252, ECO:0000269|PubMed:26371182, ECO:0000269|PubMed:27754931, ECO:0000305|PubMed:15700135}.
uniprot
proteins
mass_dalton
98994
uniprot
proteins
mutagenesis
MUTAGEN 170; /note="S->E: Reduces lysophospholipase activity by about 70%."; MUTAGEN 210; /note="T->A: Loss of lysophospholipase activity and ability to hydrolyze sphingosylphosphorylcholine."; /evidence="ECO:0000269|PubMed:14500380, ECO:0000269|PubMed:21240271"; MUTAGEN 211; /note="F->Y: Reduces lysophospholipase activity by about 70%."; /evidence="ECO:0000269|PubMed:21240271"; MUTAGEN 218; /note="A->V: Reduces lysophospholipase activity by about 50%."; /evidence="ECO:0000269|PubMed:21240271"; MUTAGEN 231; /note="N->A: Strongly reduced lysophospholipase activity."; /evidence="ECO:0000269|PubMed:21240271"; MUTAGEN 307; /note="Y->Q: Reduces lysophospholipase activity by about 70%."; /evidence="ECO:0000269|PubMed:21240271"; MUTAGEN 316; /note="H->Q: Loss of ability to hydrolyze sphingosylphosphorylcholine."; /evidence="ECO:0000269|PubMed:14500380"; MUTAGEN 360; /note="H->Q: Loss of ability to hydrolyze sphingosylphosphorylcholine."; /evidence="ECO:0000269|PubMed:14500380
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-414 and Cys-806 is essential for catalytic activity. {ECO:0000250|UniProtKB:Q9R1E6}.
uniprot
proteins
protein_family
Nucleotide pyrophosphatase/phosphodiesterase family
uniprot
proteins
pubmed
11559573
uniprot
proteins
pubmed
12176993
uniprot
proteins
pubmed
12354767
uniprot
proteins
pubmed
14500380
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15700135
uniprot
proteins
pubmed
15769751
uniprot
proteins
pubmed
16421571
uniprot
proteins
pubmed
1733949
uniprot
proteins
pubmed
18175805
uniprot
proteins
pubmed
21240271
uniprot
proteins
pubmed
21393252
uniprot
proteins
pubmed
26371182
uniprot
proteins
pubmed
27754931
uniprot
proteins
pubmed
28414242
uniprot
proteins
pubmed
7982964
uniprot
proteins
pubmed
8579579
uniprot
proteins
pubmed
8586446
uniprot
proteins
sequence_length
863
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12176993, ECO:0000269|PubMed:15769751, ECO:0000269|PubMed:1733949, ECO:0000269|PubMed:26371182, ECO:0000269|PubMed:27754931}.
uniprot
proteins