ID ENTP8_CHICK Reviewed; 493 AA. AC O93295; Q90X66; DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 27-MAR-2024, entry version 119. DE RecName: Full=Ectonucleoside triphosphate diphosphohydrolase 8; DE Short=E-NTPDase 8; DE Short=NTPDase 8; DE Short=NTPDase8; DE EC=3.6.1.5; DE AltName: Full=Liver ecto-ATP diphosphohydrolase; GN Name=ENTPD8; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 1-21 AND 150-156. RC TISSUE=Oviduct; RX PubMed=9632655; DOI=10.1074/jbc.273.26.16043; RA Nagy A.K., Knowles A.F., Nagami G.T.; RT "Molecular cloning of the chicken oviduct ecto-ATP-diphosphohydrolase."; RL J. Biol. Chem. 273:16043-16049(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME ACTIVITY, BIOPHYSICOCHEMICAL RP PROPERTIES, AND SUBCELLULAR LOCATION. RC TISSUE=Liver; RX PubMed=11985621; DOI=10.1046/j.1432-1033.2002.02898.x; RA Knowles A.F., Nagy A.K., Strobel R.S., Wu-Weis M.; RT "Purification, characterization, cloning, and expression of the chicken RT liver ecto-ATP-diphosphohydrolase."; RL Eur. J. Biochem. 269:2373-2382(2002). RN [3] RP PROTEIN SEQUENCE OF 1-17. RC TISSUE=Stomach; RX PubMed=9295305; DOI=10.1074/jbc.272.38.23645; RA Lewis-Carl S., Kirley T.L.; RT "Immunolocalization of the ecto-ATPase and ecto-apyrase in chicken gizzard RT and stomach. Purification and N-terminal sequence of the stomach ecto- RT apyrase."; RL J. Biol. Chem. 272:23645-23652(1997). RN [4] RP FUNCTION. RX PubMed=16101300; DOI=10.1021/bi050019k; RA Mukasa T., Lee Y., Knowles A.F.; RT "Either the carboxyl- or the amino-terminal region of the human ecto-ATPase RT (E-NTPDase 2) confers detergent and temperature sensitivity to the chicken RT ecto-ATP-diphosphohydrolase (E-NTPDase 8)."; RL Biochemistry 44:11160-11170(2005). CC -!- FUNCTION: Canalicular ectonucleoside NTPDase responsible for the main CC hepatic NTPDase activity. Ectonucleoside ATPases catalyze the CC hydrolysis of gamma- and beta-phosphate residues of nucleotides, CC playing a central role in concentration of extracellular nucleotides. CC {ECO:0000269|PubMed:11985621, ECO:0000269|PubMed:16101300}. 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:0000269|PubMed:11985621}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Ca(2+) or Mg(2+). Has lower efficiency with Mg(2+). {ECO:0000250}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.51 mM for ATP {ECO:0000269|PubMed:11985621}; CC KM=5.3 mM for ADP {ECO:0000269|PubMed:11985621}; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11985621}; CC Multi-pass membrane protein {ECO:0000269|PubMed:11985621}. CC -!- PTM: N-glycosylated. CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF041355; AAC26491.1; -; mRNA. DR EMBL; AF426405; AAL25086.1; -; mRNA. DR RefSeq; NP_989578.2; NM_204247.2. DR AlphaFoldDB; O93295; -. DR SMR; O93295; -. DR STRING; 9031.ENSGALP00000014500; -. DR GlyCosmos; O93295; 12 sites, No reported glycans. DR PaxDb; 9031-ENSGALP00000014500; -. DR GeneID; 374095; -. DR KEGG; gga:374095; -. DR CTD; 377841; -. DR VEuPathDB; HostDB:geneid_374095; -. DR eggNOG; KOG1386; Eukaryota. DR InParanoid; O93295; -. DR PhylomeDB; O93295; -. DR BRENDA; 3.6.1.5; 1306. DR SABIO-RK; O93295; -. DR PRO; PR:O93295; -. DR Proteomes; UP000000539; Unassembled WGS sequence. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0004050; F:apyrase activity; IEA:UniProtKB-EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004382; F:GDP phosphatase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0045134; F:UDP phosphatase activity; IBA:GO_Central. DR GO; GO:0009134; P:nucleoside diphosphate catabolic process; IBA:GO_Central. 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 1: Evidence at protein level; KW ATP-binding; Calcium; Cell membrane; Direct protein sequencing; KW Disulfide bond; Glycoprotein; Hydrolase; Magnesium; Membrane; KW Metal-binding; Nucleotide-binding; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1..493 FT /note="Ectonucleoside triphosphate diphosphohydrolase 8" FT /id="PRO_0000209905" FT TOPO_DOM 1..7 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 8..28 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 29..463 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 464..486 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 487..493 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT ACT_SITE 166 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:O35795" FT CARBOHYD 65 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 79 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 133 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 223 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 234 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 267 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 324 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 330 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 361 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 372 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 382 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 445 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 76..100 FT /evidence="ECO:0000250" FT DISULFID 244..291 FT /evidence="ECO:0000250" FT DISULFID 327..333 FT /evidence="ECO:0000250" FT DISULFID 379..401 FT /evidence="ECO:0000250" FT CONFLICT 16 FT /note="C -> W (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 21 FT /note="I -> G (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 278..280 FT /note="RRI -> QEN (in Ref. 2; AAL25086)" FT /evidence="ECO:0000305" FT CONFLICT 316 FT /note="P -> R (in Ref. 2; AAL25086)" FT /evidence="ECO:0000305" FT CONFLICT 325 FT /note="L -> F (in Ref. 2; AAL25086)" FT /evidence="ECO:0000305" FT CONFLICT 461..462 FT /note="HE -> QQ (in Ref. 2; AAL25086)" FT /evidence="ECO:0000305" SQ SEQUENCE 493 AA; 54035 MW; F14FF4C3AA2F3603 CRC64; MEYKGKVVAG LLTATCVFSI IALILSAVDV KDVFLPPGTK YGLVFDAGST HTALYVYQWP ADKENGTGIV SQVESCTVNG SGISSYADDP AGAGASLKPC LDKAMAVIPV EQQWQTPTYL GATAGMRLLR EQNSTKAEQV FAEVSKAIRE FPVDFRGAQI LTGNEEGSFG WITVNYLLET LIKFSFAGKW EHPQNTEVLG ALDLGGASTQ ITFQPGVTIE DKNTSVLFRL YGTNYSLYTH SYLCYGQIQA SKRLMAALHQ DGSYVQNISH PCYPKGYRRI ITIAEIYDSP CVPTPSMLSP AQILTVTGTG NPAACPTAIL KLFNLTCGAN RTCGFDGVYQ PPVRGQFFAF AGFYYTFSFL NLTGQQSLSH VNATVWDFCN KNWSELVETF PQNKEHLHTY CVVGLYILTL LVDGYKFDEH TWSNIHFSQK AGNADIGWTL GFMLNLTNMI PTEALEHVKG HEPSLWAGAI SFIVLAIVAG LVAILLQCFW KSK //