ID A0A2K6RU02_RHIRO Unreviewed; 458 AA.
AC A0A2K6RU02;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
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|Ensembl:ENSRROP00000044508.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000044508.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000044508.1}
RP IDENTIFICATION.
RG Ensembl;
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 AlphaFoldDB; A0A2K6RU02; -.
DR STRING; 61622.ENSRROP00000044508; -.
DR Ensembl; ENSRROT00000069025.1; ENSRROP00000044508.1; ENSRROG00000045217.1.
DR GeneTree; ENSGT01100000263542; -.
DR Proteomes; UP000233200; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017110; F:nucleoside diphosphate phosphatase activity; IEA:Ensembl.
DR GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:Ensembl.
DR GO; GO:0009133; P:nucleoside diphosphate biosynthetic process; IEA:Ensembl.
DR GO; GO:0009124; P:nucleoside monophosphate biosynthetic process; IEA:Ensembl.
DR Gene3D; 3.30.420.40; -; 2.
DR Gene3D; 3.30.420.150; Exopolyphosphatase. Domain 2; 2.
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|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000233200};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 431..456
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 168
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 208..212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 458 AA; 49546 MW; 809B60D168EBDD83 CRC64;
MGLSRKEQVF LAILGASGVS GLTALILLLV EATSVLLPTD IKFGIVFDAG SSHTSLFLYQ
WPADKENGTG VVSQALACQV EGPGISSYTS NPAQAGESLQ GCLEEALVLI PEAQHRKTPM
FLGATAGMRL LRQKNSSQAR DIFAAVTQVL GRSPVDFWGA ELLAGQDEGA FGWITVNYGL
GTLVKYSFTG EWIQPPEETL VGALDMGGAS TQITFVPGGP ILDKSTQADF RLYGSNYSVY
THSYLCFGRD QMLSRLLVGL VQSRPAALLR HPCYLSGYQT TLALAPLYES PCVHTTPPLS
LPQNLTVEGT GNPGACVSAI RELFNFSSCQ GQEDCAFDGI YQPPLQGKFY VETSYPGQDR
WLPDYCASGL YILTLLHEGY RFSEETWPSL EFRKQAGGVD IGWTLGYMLN LTGMIPADAP
AQLWAVSYGV WVAKVVFMVL TLVAVVGAAL VQLFWLQD
//
