ID A0A2Y9NFL6_DELLE Unreviewed; 681 AA.
AC A0A2Y9NFL6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Ectonucleoside triphosphate diphosphohydrolase 8 {ECO:0000256|ARBA:ARBA00039598};
DE EC=3.6.1.5 {ECO:0000256|ARBA:ARBA00012148};
GN Name=ENTPD8 {ECO:0000313|RefSeq:XP_022433739.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022433739.1};
RN [1] {ECO:0000313|RefSeq:XP_022433739.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022433739.1};
RG RefSeq;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + 2 H2O = a ribonucleoside
CC 5'-phosphate + 2 H(+) + 2 phosphate; Xref=Rhea:RHEA:36795,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.5;
CC Evidence={ECO:0000256|ARBA:ARBA00000211};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC {ECO:0000256|ARBA:ARBA00009283, ECO:0000256|RuleBase:RU003833}.
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DR RefSeq; XP_022433739.1; XM_022578031.2.
DR AlphaFoldDB; A0A2Y9NFL6; -.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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:SF31; ECTONUCLEOSIDE TRIPHOSPHATE DIPHOSPHOHYDROLASE 8; 1.
DR Pfam; PF01150; GDA1_CD39; 2.
DR PROSITE; PS01238; GDA1_CD39_NTPASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000256|RuleBase:RU003833};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR600407-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483}.
FT REGION 448..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 200
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 240..244
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 681 AA; 71978 MW; 212CF57132969DAE CRC64;
MGLTWRERAF TALLGAAAVS GLTTLILFLV EATNVLLPAD TKFGIVFDAG SSHTSLLVYQ
WPANKENDTG VVSQALACRA KAPGAPDVAS LQPLPRTSRG LSPVCLKSPS SVSWPGISSY
ASDPAQAGES LQGCLEEALA LIPKAKHQQT PMFLGATGGM RLLSRKNSSQ AEDVFAAVSQ
ALSRSPVAFW GAELLAGQDE GALGWVTINY VLGLLVQYSF SGEWIQPLEG TLVGALDMGG
ASTQITFVPG GPILDTTTQA TFRLYGTEHS VYTHSYLCFG HDQMLNRLLA GLVQSSPSLL
VRHPCYHSGY RGTLALAPLY GSPCVQAAAP RDLGQNLTVE GTGNPGACVA AIRGLFNFSS
CDGRGDCAFD RVYQPPVRGQ FYAFSNFYHT FHFLNLTSRP PLATANATIW EFCQRPWKLV
GGCGPPAPHL GPSSLGCRLH RAGTPSQAVW PGGWGAPGRR LRGTPRRGAS LGGPGGQEAS
WGSWPPGPPG GGELARAGRP AARLLCLGPV HPHAPARGLR VQPGDLGRHR VPQAGRWHRH
RLDAGLHAEP DRPDPSRGAR PVAGTELWRL GGRSRLFGAD PHGHSRGHCG AALAPGLGWL
PPGAGRQRPE LARAFLSPNP KGSPCGLWPH GHMAPFCRWG HSGHGGCAVA PTMAFRCQRP
SGFPMLHEGW AIATPAALRA V
//