ENTPD2
entrez
954
canonical
uniprot
Q9Y5L3
canonical
ensembl
ENSG00000054179
resolver
ensp
ENSP00000312494
resolver
ensp
ENSP00000347213
resolver
genesymbol
ENTPD2
resolver
genesymbol_syn
CD39L1
resolver
hgnc
HGNC:3364
resolver
uniprot
O15464
resolver
uniprot
Q5SPY6
resolver
uniprot
Q5SPY7
resolver
uniprot_entry
ENTP2_HUMAN
resolver
uniprot_sec
O15464
resolver
uniprot_sec
Q5SPY6
resolver
uniprot_sec
Q5SPY7
resolver
activity_regulation
ACTIVITY REGULATION: ATP hydrolysis activity is inhibited about 70% by 0.25 mM p-chloromercuri-phenylsulfonate (pCMPS) and >90% by 0.1% Nonidet P-40 (NP-40) (PubMed:16101300). ATP hydrolysis activity is markedly stimulated by concanavalin A, disuccinimidyl suberate (DSS) and glutaraldehyde; The stimulatory effects are greater at 55 degrees Celsius (6-10-fold) than at 37 degrees Celsius (about 2-fold) (PubMed:16101300). ATPase activity is decreased by about 50% at 55 degrees Celsius (PubMed:16101300). ATPase activity increases from 15 to 37 degrees Celsius but declines at higher temperatures (PubMed:16101300). ATPase activity is inhibited by 0.1% NP-40 at all temperatures (PubMed:16101300). {ECO:0000269|PubMed:16101300}.
uniprot
proteins
amino_acid_sequence
MAGKVRSLLPPLLLAAAGLAGLLLLCVPTRDVREPPALKYGIVLDAGSSHTSMFIYKWPADKENDTGIVGQHSSCDVPGGGISSYADNPSGASQSLVGCLEQALQDVPKERHAGTPLYLGATAGMRLLNLTNPEASTSVLMAVTHTLTQYPFDFRGARILSGQEEGVFGWVTANYLLENFIKYGWVGRWFRPRKGTLGAMDLGGASTQITFETTSPAEDRASEVQLHLYGQHYRVYTHSFLCYGRDQVLQRLLASALQTHGFHPCWPRGFSTQVLLGDVYQSPCTMAQRPQNFNSSARVSLSGSSDPHLCRDLVSGLFSFSSCPFSRCSFNGVFQPPVAGNFVAFSAFFYTVDFLRTSMGLPVATLQQLEAAAVNVCNQTWAQLQARVPGQRARLADYCAGAMFVQQLLSRGYGFDERAFGGVIFQKKAADTAVGWALGYMLNLTNLIPADPPGLRKGTDFSSWVVLLLLFASALLAALVLLLRQVHSAKLPSTI
uniprot
proteins
ec_number
3.6.1.5
uniprot
proteins
function
FUNCTION: Catalyzes the hydrolysis of nucleoside triphosphates (NTPs) and diphosphates (NDPs), with a marked preference for triphosphonucleosides over diphosphonucleosides (PubMed:10510450, PubMed:12888562, PubMed:16101300, PubMed:18404504). The enzyme sequentially removes phosphate groups in two successive steps, converting NTPs to nucleoside monophosphates (NMPs) via NDP intermediates (PubMed:10510450, PubMed:12888562, PubMed:16101300, PubMed:18404504). This activity contributes to the regulation of extracellular nucleotides levels (PubMed:10510450, PubMed:12888562, PubMed:16101300, PubMed:18404504). ATP hydrolysis is characterized by fast ADP accumulation and delayed AMP formation, reflecting limited ADP hydrolase activity (By similarity). Hydrolyzes ADP and UDP only to a marginal extent, and does not hydrolyze AMP (PubMed:10510450, PubMed:12888562, PubMed:16101300, PubMed:18404504). All nucleoside 5'-diphosphates are hydrolyzed at rates lower than those of their corresponding triphosphates (By similarity). {ECO:0000250|UniProtKB:O35795, ECO:0000269|PubMed:10510450, ECO:0000269|PubMed:12888562, ECO:0000269|PubMed:16101300, ECO:0000269|PubMed:18404504}.; FUNCTION: [Isoform gamma]: Catalytically inactive. {ECO:0000269|PubMed:12888562}.; FUNCTION: [Isoform Short]: Catalytically inactive. {ECO:0000269|PubMed:12888562}.
uniprot
proteins
mass_dalton
53665
uniprot
proteins
mutagenesis
MUTAGEN 399; /note="C->S: Abolishes ecto-ATPase activity, accumulates intracellularly."; /evidence="ECO:0000269|PubMed:12888562"; MUTAGEN 443; /note="N->D: 7% of wild-type ATPase activity, accumulates intracellularly."; /evidence="ECO:0000269|PubMed:12888562
uniprot
proteins
protein_family
GDA1/CD39 NTPase family
uniprot
proteins
pubmed
10510450
uniprot
proteins
pubmed
12888562
uniprot
proteins
pubmed
15164053
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16101300
uniprot
proteins
pubmed
18404504
uniprot
proteins
pubmed
9271669
uniprot
proteins
sequence_length
495
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform Long]: Cell membrane {ECO:0000269|PubMed:12888562}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform Short]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12888562}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform gamma]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12888562}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 8..28; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 463..483; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins