ENTP8_CHICK
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 03-AUG-2022, entry version 113.
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 PaxDb; O93295; -.
DR GeneID; 374095; -.
DR KEGG; gga:374095; -.
DR CTD; 377841; -.
DR VEuPathDB; HostDB:geneid_374095; -.
DR eggNOG; KOG1386; Eukaryota.
DR InParanoid; O93295; -.
DR OrthoDB; 1337265at2759; -.
DR PhylomeDB; O93295; -.
DR BRENDA; 3.6.1.5; 1306.
DR SABIO-RK; O93295; -.
DR PRO; PR:O93295; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0102490; F:8-oxo-dGTP phosphohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0102485; F:dATP phosphohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0102486; F:dCTP phosphohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0102491; F:dGTP phosphohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0102488; F:dTTP phosphohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0102487; F:dUTP phosphohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0102489; F:GTP phosphohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0004382; F:guanosine-diphosphatase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017110; F:nucleoside-diphosphatase activity; IBA:GO_Central.
DR GO; GO:0045134; F:uridine-diphosphatase activity; IBA:GO_Central.
DR GO; GO:0009134; P:nucleoside diphosphate catabolic process; IBA:GO_Central.
DR InterPro; IPR000407; GDA1_CD39_NTPase.
DR PANTHER; PTHR11782; PTHR11782; 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
