ID A0A2Y9EIW3_PHYMC Unreviewed; 494 AA.
AC A0A2Y9EIW3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
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_007103703.2};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_007103703.2};
RN [1] {ECO:0000313|RefSeq:XP_007103703.2}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007103703.2};
RG RefSeq;
RL Submitted (NOV-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_007103703.2; XM_007103641.4.
DR AlphaFoldDB; A0A2Y9EIW3; -.
DR STRING; 9755.ENSPCTP00005024446; -.
DR Ensembl; ENSPCTT00005026940; ENSPCTP00005024446; ENSPCTG00005017402.
DR KEGG; pcad:102981071; -.
DR InParanoid; A0A2Y9EIW3; -.
DR OrthoDB; 180318at2759; -.
DR Proteomes; UP000248484; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:SF31; ECTONUCLEOSIDE TRIPHOSPHATE DIPHOSPHOHYDROLASE 8; 1.
DR Pfam; PF01150; GDA1_CD39; 1.
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:UP000248484};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 465..492
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 494 AA; 53200 MW; 7B54EB76229B0803 CRC64;
MGLTWKERAF TALLGAAAVS GLTTLILFLV EATNVLLPAD TKFGIVFDAG SSHTSLFVYQ
WLANKENDTG VVSQALACQA KGPGISSYAS DPAQAGESLQ GCLEEALALI PKAKHQQTPM
FLGATAGMRL LSQKNSSQAE DVFAAVSRVL SQSPADFWGA ELLAGQDEGA LGWVTINYVL
GLLVKYSFSG EWIRPLEGTL VGALDMGGAS TQITFVPGGP ILDTTTQVTF CLYGTEHSVY
THSYLCFGRD QMLNRLLAGL VQSSPGLLVR HPCYHSGYRG TLALAPLYGS PCVQAAAPRD
LGRNLTVEGT GNPGACVAAI RGLFNFSSCE GRGDCAFDRV YQPPVRGQFY AFSNFYHTFH
FLNLTSRPPL ATANATVWEF CQRPWKLVEA SSPGQDHRLR DYCASGLYIL TLLLEGYGFS
QETWGGIEFR KQAGGTDIGW TLGYMLNLTS LIPAEAPAQW RAQSYGVWVA GVVFLVLTLV
AILGATAVQL WLRD
//