ENTP1_RAT
ID ENTP1_RAT Reviewed; 511 AA.
AC P97687;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 130.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, COFACTOR,
RP GLYCOSYLATION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Hippocampus;
RX PubMed=9221928; DOI=10.1016/s0169-328x(97)00066-1;
RA Wang T.-F., Rosenberg P.A., Guidotti G.;
RT "Characterization of brain ecto-apyrase: evidence for only one ecto-apyrase
RT (CD39) gene.";
RL Brain Res. Mol. Brain Res. 47:295-302(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Cochlea;
RX PubMed=10581401; DOI=10.1016/s0169-328x(99)00244-2;
RA Vlajkovic S.M., Housley G.D., Greenwood D., Thorne P.R.;
RT "Evidence for alternative splicing of ecto-ATPase associated with
RT termination of purinergic transmission.";
RL Brain Res. Mol. Brain Res. 73:85-92(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 432-511.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=9364474; DOI=10.1016/s0028-3908(97)00115-9;
RA Kegel B., Braun N., Heine P., Maliszewski C.R., Zimmermann H.;
RT "An ecto-ATPase and an ecto-ATP diphosphohydrolase are expressed in rat
RT brain.";
RL Neuropharmacology 36:1189-1200(1997).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 38-477, AND DISULFIDE BONDS.
RX PubMed=22100451; DOI=10.1016/j.jmb.2011.10.050;
RA Zebisch M., Krauss M., Schafer P., Strater N.;
RT "Crystallographic evidence for a domain motion in rat nucleoside
RT triphosphate diphosphohydrolase (NTPDase) 1.";
RL J. Mol. Biol. 415:288-306(2012).
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 {ECO:0000269|PubMed:9221928}.
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:9221928};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:9221928};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:9221928};
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in primary neurons and astrocytes,
CC kidney, liver, muscle, thymus, lung and spleen.
CC {ECO:0000269|PubMed:9221928}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:9221928}.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
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DR EMBL; U81295; AAC53195.1; -; mRNA.
DR EMBL; Y15685; CAA75730.1; -; mRNA.
DR PDB; 3ZX0; X-ray; 2.50 A; A/B/C/D=38-189, A/B/C/D=207-477.
DR PDB; 3ZX2; X-ray; 1.81 A; A/B/C/D=38-189, A/B/C/D=207-477.
DR PDB; 3ZX3; X-ray; 1.70 A; A/B/C/D=38-189, A/B/C/D=207-477.
DR PDBsum; 3ZX0; -.
DR PDBsum; 3ZX2; -.
DR PDBsum; 3ZX3; -.
DR AlphaFoldDB; P97687; -.
DR SMR; P97687; -.
DR STRING; 10116.ENSRNOP00000051602; -.
DR BindingDB; P97687; -.
DR ChEMBL; CHEMBL2767; -.
DR GuidetoPHARMACOLOGY; 2888; -.
DR GlyGen; P97687; 7 sites.
DR iPTMnet; P97687; -.
DR PhosphoSitePlus; P97687; -.
DR PaxDb; P97687; -.
DR PRIDE; P97687; -.
DR RGD; 69265; Entpd1.
DR eggNOG; KOG1386; Eukaryota.
DR InParanoid; P97687; -.
DR PhylomeDB; P97687; -.
DR BRENDA; 3.6.1.5; 5301.
DR BRENDA; 3.6.1.6; 5301.
DR Reactome; R-RNO-8850843; Phosphate bond hydrolysis by NTPDase proteins.
DR SABIO-RK; P97687; -.
DR PRO; PR:P97687; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005604; C:basement membrane; ISO:RGD.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0097060; C:synaptic membrane; IDA:RGD.
DR GO; GO:0008021; C:synaptic vesicle; IDA:RGD.
DR GO; GO:0102490; F:8-oxo-dGTP phosphohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0043262; F:adenosine-diphosphatase activity; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:RGD.
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:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0017110; F:nucleoside-diphosphatase activity; ISO:RGD.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; ISO:RGD.
DR GO; GO:0045134; F:uridine-diphosphatase activity; IBA:GO_Central.
DR GO; GO:0046032; P:ADP catabolic process; ISO:RGD.
DR GO; GO:0071275; P:cellular response to aluminum ion; IEP:RGD.
DR GO; GO:0035457; P:cellular response to interferon-alpha; IEP:RGD.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:2001170; P:negative regulation of ATP biosynthetic process; IMP:RGD.
DR GO; GO:0033602; P:negative regulation of dopamine secretion; IMP:RGD.
DR GO; GO:0009134; P:nucleoside diphosphate catabolic process; IBA:GO_Central.
DR GO; GO:0030168; P:platelet activation; ISO:RGD.
DR GO; GO:0009181; P:purine ribonucleoside diphosphate catabolic process; ISO:RGD.
DR GO; GO:0033198; P:response to ATP; IEP:RGD.
DR GO; GO:0010996; P:response to auditory stimulus; IEP:RGD.
DR GO; GO:0031000; P:response to caffeine; IEP:RGD.
DR GO; GO:0010332; P:response to gamma radiation; IEP:RGD.
DR GO; GO:0035456; P:response to interferon-beta; IEP:RGD.
DR GO; GO:1903576; P:response to L-arginine; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0043278; P:response to morphine; IEP:RGD.
DR GO; GO:0010238; P:response to proline; IEP:RGD.
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 3D-structure; ATP-binding; Calcium; Disulfide bond; Glycoprotein;
KW Hydrolase; Magnesium; Membrane; Nucleotide-binding; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..511
FT /note="Ectonucleoside triphosphate diphosphohydrolase 1"
FT /id="PRO_0000209904"
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..478
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 479..499
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 500..511
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 46..171
FT /note="N-terminal lobe"
FT REGION 205..441
FT /note="C-terminal lobe"
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 226
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 374
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 84..108
FT /evidence="ECO:0000269|PubMed:22100451"
FT DISULFID 254..300
FT /evidence="ECO:0000269|PubMed:22100451"
FT DISULFID 281..324
FT /evidence="ECO:0000269|PubMed:22100451"
FT DISULFID 337..342
FT /evidence="ECO:0000269|PubMed:22100451"
FT DISULFID 391..414
FT /evidence="ECO:0000269|PubMed:22100451"
FT CONFLICT 332
FT /note="F -> L (in Ref. 2)"
FT /evidence="ECO:0000305"
FT STRAND 47..55
FT /evidence="ECO:0007829|PDB:3ZX3"
FT STRAND 60..68
FT /evidence="ECO:0007829|PDB:3ZX3"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:3ZX3"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:3ZX3"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:3ZX3"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:3ZX3"
FT HELIX 101..115
FT /evidence="ECO:0007829|PDB:3ZX3"
FT HELIX 118..121
FT /evidence="ECO:0007829|PDB:3ZX3"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:3ZX3"
FT HELIX 132..140
FT /evidence="ECO:0007829|PDB:3ZX3"
FT HELIX 142..157
FT /evidence="ECO:0007829|PDB:3ZX3"
FT STRAND 159..168
FT /evidence="ECO:0007829|PDB:3ZX3"
FT HELIX 171..185
FT /evidence="ECO:0007829|PDB:3ZX3"
FT TURN 186..189
FT /evidence="ECO:0007829|PDB:3ZX3"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:3ZX3"
FT STRAND 215..222
FT /evidence="ECO:0007829|PDB:3ZX3"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:3ZX3"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:3ZX3"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:3ZX3"
FT STRAND 243..253
FT /evidence="ECO:0007829|PDB:3ZX3"
FT HELIX 257..268
FT /evidence="ECO:0007829|PDB:3ZX3"
FT STRAND 273..279
FT /evidence="ECO:0007829|PDB:3ZX3"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:3ZX3"
FT HELIX 292..295
FT /evidence="ECO:0007829|PDB:3ZX3"
FT HELIX 299..304
FT /evidence="ECO:0007829|PDB:3ZX3"
FT STRAND 311..317
FT /evidence="ECO:0007829|PDB:3ZX3"
FT HELIX 321..329
FT /evidence="ECO:0007829|PDB:3ZX3"
FT STRAND 338..344
FT /evidence="ECO:0007829|PDB:3ZX3"
FT STRAND 356..360
FT /evidence="ECO:0007829|PDB:3ZX3"
FT HELIX 361..372
FT /evidence="ECO:0007829|PDB:3ZX3"
FT HELIX 380..391
FT /evidence="ECO:0007829|PDB:3ZX3"
FT HELIX 395..401
FT /evidence="ECO:0007829|PDB:3ZX3"
FT HELIX 407..410
FT /evidence="ECO:0007829|PDB:3ZX3"
FT HELIX 413..425
FT /evidence="ECO:0007829|PDB:3ZX3"
FT HELIX 432..437
FT /evidence="ECO:0007829|PDB:3ZX3"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:3ZX3"
FT STRAND 442..444
FT /evidence="ECO:0007829|PDB:3ZX3"
FT STRAND 447..451
FT /evidence="ECO:0007829|PDB:3ZX2"
FT HELIX 452..459
FT /evidence="ECO:0007829|PDB:3ZX3"
SQ SEQUENCE 511 AA; 57408 MW; 4CC123D3E644C193 CRC64;
MEDIKDSKVK RFCSKNILII LGFSSVLAVI ALIAVGLTHN KPLPENVKYG IVLDAGSSHT
NLYIYKWPAE KENDTGVVQL LEECQVKGPG ISKYAQKTDE IAAYLAECMK MSTERIPASK
QHQTPVYLGA TAGMRLLRME SKQSADEVLA AVSRSLKSYP FDFQGAKIIT GQEEGAYGWI
TINYLLGRFT QEQSWLNFIS DSQKQATFGA LDLGGSSTQV TFVPLNQTLE APETSLQFRL
YGTDYTVYTH SFLCYGKDQA LWQKLAQDIQ VSSGGILKDP CFYPGYKKVV NVSELYGTPC
TKRFEKKLPF NQFQVQGTGD YEQCHQSILK FFNNSHCPYS QCAFNGVFLP PLQGSFGAFS
AFYFVMDFFK KMANDSVSSQ EKMTEITKNF CSKPWEEVKA SYPTVKEKYL SEYCFSGTYI
LSLLLQGYNF TGTSWDQIHF MGKIKDSNAG WTLGYMLNLT NMIPAEQPLS PPLPHSTYIS
LMVLFSLVLV AMVITGLFIF SKPSYFWKEA V
