Entpd2
entrez
64467
canonical
uniprot
O35795
canonical
ensembl
ENSRNOG00000013102
resolver
ensp
ENSRNOP00000017829
resolver
ensp
ENSRNOP00000086303
resolver
enst
ENSRNOT00000017829
resolver
genesymbol
Entpd2
resolver
genesymbol_syn
Cd39l1
resolver
genesymbol_syn
Npdc1
resolver
uniprot
F1M7N2
resolver
uniprot
Q5RJP4
resolver
uniprot
Q9JHY5
resolver
uniprot
Q9WVE7
resolver
uniprot_entry
ENTP2_RAT
resolver
uniprot_entry
F1M7N2_RAT
resolver
uniprot_entry
Q5RJP4_RAT
resolver
uniprot_sec
Q9JHY5
resolver
uniprot_sec
Q9WVE7
resolver
activity_regulation
ACTIVITY REGULATION: ATPase activityis inhibited by only 55% by Evans Blue, at a concentration of 100 mm (PubMed:10231370). Suramin (100 mm) inhibits ATPase activity by 45% (PubMed:10231370, PubMed:15362980). Inhibited by PPADS (100 muM) (PubMed:15362980). {ECO:0000269|PubMed:10231370, ECO:0000269|PubMed:15362980}.
uniprot
proteins
amino_acid_sequence
MAGKLVSLVPPLLLAAAGLTGLLLLCVPTQDVREPPALKYGIVLDAGSSHTSMFVYKWPADKENDTGIVGQHSSCDVQGGGISSYANDPSKAGQSLVRCLEQALRDVPRDRHASTPLYLGATAGMRPFNLTSPEATARVLEAVTQTLTQYPFDFRGARILSGQDEGVFGWVTANYLLENFIKYGWVGRWIRPRKGTLGAMDLGGASTQITFETTSPSEDPGNEVHLRLYGQHYRVYTHSFLCYGRDQILLRLLASALQIHRFHPCWPKGYSTQVLLQEVYQSPCTMGQRPRAFNGSAIVSLSGTSNATLCRDLVSRLFNISSCPFSQCSFNGVFQPPVAGNFIAFSAFYYTVDFLTTVMGLPVGTLKQLEEATEITCNQTWTELQARVPGQKTRLADYCAVAMFIHQLLSRGYHFDERSFREVVFQKKAADTAVGWALGYMLNLTNLIPADLPGLRKGTHFSSWVALLLLFTVLILAALVLLLRQVRSAKSPGAL
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:10231370, PubMed:11229804, PubMed:15362980, PubMed:23830739, PubMed:9364474). The enzyme sequentially removes phosphate groups in two successive steps, converting NTPs to nucleoside monophosphates (NMPs) via NDP intermediates (PubMed:10231370, PubMed:11229804, PubMed:15362980, PubMed:23830739, PubMed:9364474). This activity contributes to the regulation of extracellular nucleotides levels (PubMed:10231370, PubMed:11229804, PubMed:15362980, PubMed:23830739, PubMed:9364474). ATP hydrolysis is characterized by fast ADP accumulation and delayed AMP formation, reflecting limited ADP hydrolase activity (PubMed:10231370, PubMed:15362980). Hydrolyzes ADP and UDP only to a marginal extent, and does not hydrolyze AMP (PubMed:9364474). All nucleoside 5'-diphosphates are hydrolyzed at rates lower than those of their corresponding triphosphates (PubMed:15362980). {ECO:0000269|PubMed:10231370, ECO:0000269|PubMed:11229804, ECO:0000269|PubMed:15362980, ECO:0000269|PubMed:23830739, ECO:0000269|PubMed:9364474}.
uniprot
proteins
mass_dalton
54390
uniprot
proteins
protein_family
GDA1/CD39 NTPase family
uniprot
proteins
pubmed
10231370
uniprot
proteins
pubmed
10581401
uniprot
proteins
pubmed
11229804
uniprot
proteins
pubmed
15362980
uniprot
proteins
pubmed
18458329
uniprot
proteins
pubmed
23830739
uniprot
proteins
pubmed
24090084
uniprot
proteins
pubmed
9364474
uniprot
proteins
sequence_length
495
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:15362980}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:15362980}; Multi-pass membrane protein {ECO:0000255}. Note=Also accumulated intracellularly. {ECO:0000269|PubMed:15362980}.
uniprot
proteins
transmembrane_region
TRANSMEM 5..25; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 463..483; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins