ENTP1_BOVIN
ID ENTP1_BOVIN Reviewed; 513 AA.
AC O18956;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Ectonucleoside triphosphate diphosphohydrolase 1;
DE Short=NTPDase 1;
DE EC=3.6.1.5;
DE AltName: Full=Ecto-ATP diphosphohydrolase 1;
DE Short=Ecto-ATPDase 1;
DE Short=Ecto-ATPase 1;
DE AltName: Full=Ecto-apyrase;
DE AltName: Full=Lymphoid cell activation antigen;
DE AltName: CD_antigen=CD39;
GN Name=ENTPD1; Synonyms=CD39;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Aortic endothelium;
RA Chang A.S., Garcia R.L., Chang S.M., Schilling W.P.;
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 97-103; 123-133; 136-140; 145-168 AND 459-471.
RC TISSUE=Aorta;
RX PubMed=8955160; DOI=10.1074/jbc.271.51.33116;
RA Kaczmarek E., Koziak K., Sevigny J., Siegel J.B., Anrather J.,
RA Beaudoin A.R., Bach F.H., Robson S.C.;
RT "Identification and characterization of CD39/vascular ATP
RT diphosphohydrolase.";
RL J. Biol. Chem. 271:33116-33122(1996).
CC -!- FUNCTION: In the nervous system, could hydrolyze ATP and other
CC nucleotides to regulate purinergic neurotransmission. Could also be
CC implicated in the prevention of platelet aggregation by hydrolyzing
CC platelet-activating ADP to AMP. Hydrolyzes ATP and ADP equally well.
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
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DR EMBL; AF005940; AAB62382.1; -; mRNA.
DR RefSeq; NP_776961.1; NM_174536.2.
DR AlphaFoldDB; O18956; -.
DR SMR; O18956; -.
DR STRING; 9913.ENSBTAP00000045026; -.
DR BindingDB; O18956; -.
DR ChEMBL; CHEMBL2766; -.
DR PaxDb; O18956; -.
DR PRIDE; O18956; -.
DR GeneID; 282223; -.
DR KEGG; bta:282223; -.
DR CTD; 953; -.
DR eggNOG; KOG1386; Eukaryota.
DR InParanoid; O18956; -.
DR OrthoDB; 1337265at2759; -.
DR SABIO-RK; O18956; -.
DR PRO; PR:O18956; -.
DR Proteomes; UP000009136; 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: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; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Hydrolase; Magnesium; Membrane; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..513
FT /note="Ectonucleoside triphosphate diphosphohydrolase 1"
FT /id="PRO_0000209901"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..481
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 482..502
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 503..513
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 174
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O35795"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 460
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 255..300
FT /evidence="ECO:0000250|UniProtKB:P97687"
FT DISULFID 281..327
FT /evidence="ECO:0000250|UniProtKB:P97687"
FT DISULFID 340..345
FT /evidence="ECO:0000250|UniProtKB:P97687"
FT DISULFID 393..416
FT /evidence="ECO:0000250|UniProtKB:P97687"
FT CONFLICT 97
FT /note="K -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 101..103
FT /note="INV -> CGF (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 464
FT /note="K -> V (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 513 AA; 58114 MW; 20FE98F27B6D2F96 CRC64;
MEDRRESELK VFCSKNILSI LGFSCIIAVI ALLALGLTQN KALPENVKFG IVLDAGSSHT
SLYIYRWPAE KENDTGVVTQ IEESNVKGPG ISGFAKKVNE INVYLTACME RAQKVIPSIQ
HMETPVYLGA TAGMRLLRME NKQMADKILA AVASSISEYP FDFQGARIIS GQEEGAYGWI
TVNYLLGKFT QKLSWFNLKP SKDDTQETYG ALDLGGASTQ ITFVPQNETT ESPNNNLYFR
LYGKNYSVYT HSFLCYGKDQ ALLQKLALGL QGTNGIIHEP CFHSRYMRKI KMSVLNEGFC
TKRHELNSSF YPLVDIEIRG AGNFQRCRQS IIQLFNTSYC PYSSCSFNGV FLPPLHGQFG
AFSAFYYVME FLNLTSEESV SVEQLTEKLE EFCAQRWEEV QKNFGEVKEK YLSEYCFSGT
YILVLLLNGY HFTAESWKNI HFMNKVRSTD VGWTLGYMLN LTNKIPAEEP MSPPLPHSTY
VFLMVLFSLI LLAVIIVGIV VFHKPSYFWK DMV
