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Database: UniProt
Entry: G3WE81_SARHA
LinkDB: G3WE81_SARHA
Original site: G3WE81_SARHA 
ID   G3WE81_SARHA            Unreviewed;       495 AA.
AC   G3WE81;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 61.
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:ENSSHAP00000013736.1};
OS   Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX   NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000013736.1, ECO:0000313|Proteomes:UP000007648};
RN   [1] {ECO:0000313|Ensembl:ENSSHAP00000013736.1, ECO:0000313|Proteomes:UP000007648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA   Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA   Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA   Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA   Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA   Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA   Jones M.E., Schuster S.C.;
RT   "Genetic diversity and population structure of the endangered marsupial
RT   Sarcophilus harrisii (Tasmanian devil).";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN   [2] {ECO:0000313|Ensembl:ENSSHAP00000013736.1}
RP   IDENTIFICATION.
RG   Ensembl;
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_003757580.1; XM_003757532.1.
DR   AlphaFoldDB; G3WE81; -.
DR   STRING; 9305.ENSSHAP00000013736; -.
DR   Ensembl; ENSSHAT00000013849.2; ENSSHAP00000013736.1; ENSSHAG00000011745.2.
DR   GeneID; 100919726; -.
DR   KEGG; shr:100919726; -.
DR   CTD; 377841; -.
DR   eggNOG; KOG1386; Eukaryota.
DR   GeneTree; ENSGT01100000263542; -.
DR   HOGENOM; CLU_010246_2_3_1; -.
DR   InParanoid; G3WE81; -.
DR   OMA; TVNTTIW; -.
DR   OrthoDB; 180318at2759; -.
DR   TreeFam; TF332859; -.
DR   Proteomes; UP000007648; Unassembled WGS sequence.
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   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:UP000007648};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..30
FT                   /note="Helical"
FT                   /evidence="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   495 AA;  55454 MW;  AA892EDE02E7B48C CRC64;
     MGISYRNVVF SIFLGATIIA GIIALIVFLV GGSDIVLSPE TKYGMVFDAG SSHTSLYVYK
     WPANKENDTG IVSQALFCNV EGPGISHYVN DPVKAGESLR ACMEKALTLI PEDRHQETPT
     FLGATAGMRL LREKNSSQAD RIFEEISKIL AQFPVNFQGA QILTGKDEGS FGWITVNYIL
     GTLVKYSFSG EWIQPPMAEM VGALDLGGAS TQISFLPLDP IADPSTQGTF RLYGFNYSIY
     THSYLCYGQN QMQKRLLAHL VQIRPSEVVR NPCYHGGYED MTSLADLYDT PCVQNSQNFG
     PMQNIRVEGT GNPEACYSAI YSLFNFSTCQ GQKDCAFDGI YQPQEHGQFY AFSGFYYTFH
     FLNLTDGQSL YTVNRTIWEF CQKPWKQVEA SYPGQKQRLP TYCTNAMYIL ILLTKGYKFD
     DATWDNIHFR RQAAGTDIGW SLGYMLNMTN MIPAEAPVIQ MTESYGVWIA GIFFIVLAIL
     MSIISGVIYY FWSPD
//
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