ID   A0A3Q1BQE2_AMPOC        Unreviewed;       509 AA.
AC   A0A3Q1BQE2;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Ectonucleoside triphosphate diphosphohydrolase 2-like {ECO:0000313|Ensembl:ENSAOCP00000016822.1};
GN   Name=ENTPD2 {ECO:0000313|Ensembl:ENSAOCP00000016822.1};
OS   Amphiprion ocellaris (Clown anemonefish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000016822.1, ECO:0000313|Proteomes:UP000257160};
RN   [1] {ECO:0000313|Ensembl:ENSAOCP00000016822.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC       {ECO:0000256|ARBA:ARBA00009283}.
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DR   AlphaFoldDB; A0A3Q1BQE2; -.
DR   STRING; 80972.ENSAOCP00000016822; -.
DR   Ensembl; ENSAOCT00000032453.1; ENSAOCP00000016822.1; ENSAOCG00000021841.1.
DR   GeneTree; ENSGT01100000263542; -.
DR   OMA; NEECRYQ; -.
DR   Proteomes; UP000257160; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR   Gene3D; 3.30.420.40; -; 1.
DR   Gene3D; 3.30.420.150; Exopolyphosphatase. Domain 2; 1.
DR   InterPro; IPR000407; GDA1_CD39_NTPase.
DR   PANTHER; PTHR11782; ADENOSINE/GUANOSINE DIPHOSPHATASE; 1.
DR   PANTHER; PTHR11782:SF33; ECTONUCLEOSIDE TRIPHOSPHATE DIPHOSPHOHYDROLASE 2; 1.
DR   Pfam; PF01150; GDA1_CD39; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000257160};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..509
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018720294"
FT   TRANSMEM        471..493
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   ACT_SITE        165
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT   BINDING         209..213
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ   SEQUENCE   509 AA;  56218 MW;  00957BE43AB1D94A CRC64;
     MAQRSAHLVV PIALLLFGLV AILLLTIPAE DVQEPPGFMY GIVLDAGSSH TALYIYKWPA
     DKQNGTGVVT QHSECHVKGG GISSYVGQQG AAGQSLEVCL DQAVKDIPKD RHRLTPVYLG
     ATAGMRLLHI SSPDQSVQIL QEVGHKIHSY PFNYQGAAIL SGQEEGAYGW VTVPELTAQE
     SFNQQKSYGF EGRWFSPSRP TVGALDFGGA STQITFATEE KIEDKHVMKL RLYGHEYSLY
     THSFLCYGQD QFLKRLMAHI IKSQGYSDSV THPCFPADVS RVLKFNGIFD SPCTAKYKPS
     SYDPQASLTV HGSGNYQHCL GNVSELFSFS GCKFSQCSFD DVFQPNVTGG FMAFSAFYYI
     HSFLQRVTGV TVRTPTELDE TAKEVCSMSF NEMMLRAPDL KSRLLNYCAA SVFMEILLLR
     GYGFNDASFQ RISFQKKAGD ASVGWALGYM LSLSNMLPAE RMELRKALTP GAWGTLIFLF
     VLLLAAVLVF ILFRVCDVRK KKGSSESNI
//