ENTP1_PIG
ID ENTP1_PIG Reviewed; 510 AA.
AC Q9MYU4;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 114.
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;
DE Contains:
DE RecName: Full=Ectonucleoside triphosphate diphosphohydrolase 1 27 kDa subunit;
DE Contains:
DE RecName: Full=Ectonucleoside triphosphate diphosphohydrolase 1 54 kDa subunit;
GN Name=ENTPD1; Synonyms=CD39;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Aortic endothelium;
RX PubMed=10866813; DOI=10.1046/j.1432-1327.2000.01462.x;
RA Lemmens R., Vanduffel L., Kittel A., Beaudoin A.R., Benrezzak O.,
RA Sevigny J.;
RT "Distribution, cloning, and characterization of porcine nucleoside
RT triphosphate diphosphohydrolase-1.";
RL Eur. J. Biochem. 267:4106-4114(2000).
RN [2]
RP PROTEIN SEQUENCE OF 202-220.
RC TISSUE=Pancreas;
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 -!- TISSUE SPECIFICITY: Highest expression found in vascular endothelium,
CC smooth muscle, spleen and lung.
CC -!- PTM: Cleaved into two polypeptides that seem to stay together by
CC noncovalent interactions.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
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DR EMBL; AJ133746; CAB95871.1; -; mRNA.
DR RefSeq; NP_999318.1; NM_214153.1.
DR AlphaFoldDB; Q9MYU4; -.
DR SMR; Q9MYU4; -.
DR STRING; 9823.ENSSSCP00000011184; -.
DR PaxDb; Q9MYU4; -.
DR PeptideAtlas; Q9MYU4; -.
DR GeneID; 397298; -.
DR KEGG; ssc:397298; -.
DR CTD; 953; -.
DR eggNOG; KOG1386; Eukaryota.
DR InParanoid; Q9MYU4; -.
DR OrthoDB; 1337265at2759; -.
DR BRENDA; 3.6.1.5; 6170.
DR SABIO-RK; Q9MYU4; -.
DR ChiTaRS; ENTPD1; pig.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
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 InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR PANTHER; PTHR11782; PTHR11782; 1.
DR Pfam; PF01150; GDA1_CD39; 1.
DR SUPFAM; SSF56327; SSF56327; 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..510
FT /note="Ectonucleoside triphosphate diphosphohydrolase 1"
FT /id="PRO_0000019905"
FT CHAIN 1..201
FT /note="Ectonucleoside triphosphate diphosphohydrolase 1 27
FT kDa subunit"
FT /id="PRO_0000019906"
FT CHAIN 202..510
FT /note="Ectonucleoside triphosphate diphosphohydrolase 1 54
FT kDa subunit"
FT /id="PRO_0000019907"
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..477
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 478..498
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 499..510
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 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 84..108
FT /evidence="ECO:0000250|UniProtKB:P97687"
FT DISULFID 255..300
FT /evidence="ECO:0000250|UniProtKB:P97687"
FT DISULFID 281..324
FT /evidence="ECO:0000250|UniProtKB:P97687"
FT DISULFID 337..342
FT /evidence="ECO:0000250|UniProtKB:P97687"
FT DISULFID 390..413
FT /evidence="ECO:0000250|UniProtKB:P97687"
FT CONFLICT 203
FT /note="G -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 510 AA; 57757 MW; 82F86869040D7735 CRC64;
MEDRRESELK TFCSKNILVI LGFSSIIAVI ALLALGLTQN KPLPENVKFG IVLDAGSSHT
SLYIYKWPAE KENDTGVVSQ VEECKLKGPG ISEFAKKLGE IDIYLEACME RARTVVPKSQ
HAETPVYLGA TAGMRLLRMK NENLASKILS TVAESITRYP FDFQGARIIT GQEEGAYGWI
TINYLLDKFI QKSGWFNLKP RKGDTQETYG ALDLGGASTQ ITFVPQNQVL ESPENTLHFR
LYGKNYSVYT HSFLCYGKDQ ALLQKLTKDL KNTNGTIHEP CFHSGYQRRM NVSHLYEAPC
TRRFLTSLPF PELEIQGTGD FQKCQQSIRP LFNTSYCPYS RCSFDGVFLP LPQGDFAAFS
AFYYVMGFLN LTSEEGSFQS KVTSTLEAFC SRPWAELQMY FGDVKEKYLS EYCFSGTYIL
TLLLSGYHFT AETWKNIHFM GKVQSTSVGW TLGYMLNLTN MIPSEEPSST RLSHSTYVFL
MVLFSLILVI VVIIGLFVCH RPSYFWKDMV
