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Ectonucleoside triphosphate diphosphohydrolase 1 (NTPDase 1) (EC 3.6.1.5) (Ecto-ATP diphosphohydrolase 1) (Ecto-ATPDase 1) (Ecto-ATPase 1) (Ecto-apyrase) (Lymphoid cell activation antigen) (CD antigen CD39)

 ENTP1_RAT               Reviewed;         511 AA.
P97687;
20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
22-NOV-2017, entry version 118.
RecName: Full=Ectonucleoside triphosphate diphosphohydrolase 1;
Short=NTPDase 1;
EC=3.6.1.5;
AltName: Full=Ecto-ATP diphosphohydrolase 1;
Short=Ecto-ATPDase 1;
Short=Ecto-ATPase 1;
AltName: Full=Ecto-apyrase;
AltName: Full=Lymphoid cell activation antigen;
AltName: CD_antigen=CD39;
Name=Entpd1; Synonyms=Cd39;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, COFACTOR,
GLYCOSYLATION, AND TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley; TISSUE=Brain, and Hippocampus;
PubMed=9221928; DOI=10.1016/S0169-328X(97)00066-1;
Wang T.-F., Rosenberg P.A., Guidotti G.;
"Characterization of brain ecto-apyrase: evidence for only one ecto-
apyrase (CD39) gene.";
Brain Res. Mol. Brain Res. 47:295-302(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Wistar; TISSUE=Cochlea;
PubMed=10581401; DOI=10.1016/S0169-328X(99)00244-2;
Vlajkovic S.M., Housley G.D., Greenwood D., Thorne P.R.;
"Evidence for alternative splicing of ecto-ATPase associated with
termination of purinergic transmission.";
Brain Res. Mol. Brain Res. 73:85-92(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 432-511.
STRAIN=Sprague-Dawley; TISSUE=Brain;
PubMed=9364474; DOI=10.1016/S0028-3908(97)00115-9;
Kegel B., Braun N., Heine P., Maliszewski C.R., Zimmermann H.;
"An ecto-ATPase and an ecto-ATP diphosphohydrolase are expressed in
rat brain.";
Neuropharmacology 36:1189-1200(1997).
[4]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 38-477, AND DISULFIDE BONDS.
PubMed=22100451; DOI=10.1016/j.jmb.2011.10.050;
Zebisch M., Krauss M., Schafer P., Strater N.;
"Crystallographic evidence for a domain motion in rat nucleoside
triphosphate diphosphohydrolase (NTPDase) 1.";
J. Mol. Biol. 415:288-306(2012).
-!- FUNCTION: In the nervous system, could hydrolyze ATP and other
nucleotides to regulate purinergic neurotransmission. Could also
be implicated in the prevention of platelet aggregation by
hydrolyzing platelet-activating ADP to AMP. Hydrolyzes ATP and ADP
equally well. {ECO:0000269|PubMed:9221928}.
-!- CATALYTIC ACTIVITY: A nucleoside 5'-triphosphate + 2 H(2)O = a
nucleoside 5'-phosphate + 2 phosphate.
{ECO:0000269|PubMed:9221928}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:9221928};
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:9221928};
-!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: Expressed in primary neurons and astrocytes,
kidney, liver, muscle, thymus, lung and spleen.
{ECO:0000269|PubMed:9221928}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:9221928}.
-!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U81295; AAC53195.1; -; mRNA.
EMBL; Y15685; CAA75730.1; -; mRNA.
UniGene; Rn.17491; -.
PDB; 3ZX0; X-ray; 2.50 A; A/B/C/D=38-189, A/B/C/D=207-477.
PDB; 3ZX2; X-ray; 1.81 A; A/B/C/D=38-189, A/B/C/D=207-477.
PDB; 3ZX3; X-ray; 1.70 A; A/B/C/D=38-189, A/B/C/D=207-477.
PDBsum; 3ZX0; -.
PDBsum; 3ZX2; -.
PDBsum; 3ZX3; -.
ProteinModelPortal; P97687; -.
SMR; P97687; -.
STRING; 10116.ENSRNOP00000051602; -.
BindingDB; P97687; -.
ChEMBL; CHEMBL2767; -.
GuidetoPHARMACOLOGY; 2888; -.
iPTMnet; P97687; -.
PhosphoSitePlus; P97687; -.
PaxDb; P97687; -.
PRIDE; P97687; -.
RGD; 69265; Entpd1.
eggNOG; KOG1386; Eukaryota.
eggNOG; COG5371; LUCA.
HOVERGEN; HBG018982; -.
InParanoid; P97687; -.
PhylomeDB; P97687; -.
BRENDA; 3.6.1.5; 5301.
BRENDA; 3.6.1.6; 5301.
PRO; PR:P97687; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005605; C:basal lamina; ISO:RGD.
GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
GO; GO:0009986; C:cell surface; IDA:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; ISO:RGD.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0014069; C:postsynaptic density; IDA:RGD.
GO; GO:0097060; C:synaptic membrane; IDA:RGD.
GO; GO:0008021; C:synaptic vesicle; IDA:RGD.
GO; GO:0102490; F:8-oxo-dGTP phosphohydrolase activity; IEA:UniProtKB-EC.
GO; GO:0043262; F:adenosine-diphosphatase activity; IDA:RGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; IDA:RGD.
GO; GO:0102485; F:dATP phosphohydrolase activity; IEA:UniProtKB-EC.
GO; GO:0102486; F:dCTP phosphohydrolase activity; IEA:UniProtKB-EC.
GO; GO:0102491; F:dGTP phosphohydrolase activity; IEA:UniProtKB-EC.
GO; GO:0102488; F:dTTP phosphohydrolase activity; IEA:UniProtKB-EC.
GO; GO:0102487; F:dUTP phosphohydrolase activity; IEA:UniProtKB-EC.
GO; GO:0102489; F:GTP phosphohydrolase activity; IEA:UniProtKB-EC.
GO; GO:0042802; F:identical protein binding; IDA:RGD.
GO; GO:0017110; F:nucleoside-diphosphatase activity; ISO:RGD.
GO; GO:0017111; F:nucleoside-triphosphatase activity; ISO:RGD.
GO; GO:0071275; P:cellular response to aluminum ion; IEP:RGD.
GO; GO:0035457; P:cellular response to interferon-alpha; IEP:RGD.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:RGD.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; ISO:RGD.
GO; GO:2001170; P:negative regulation of ATP biosynthetic process; IMP:RGD.
GO; GO:0033602; P:negative regulation of dopamine secretion; IMP:RGD.
GO; GO:0030168; P:platelet activation; ISO:RGD.
GO; GO:0051260; P:protein homooligomerization; IDA:RGD.
GO; GO:0009181; P:purine ribonucleoside diphosphate catabolic process; ISO:RGD.
GO; GO:0033198; P:response to ATP; IEP:RGD.
GO; GO:0010996; P:response to auditory stimulus; IEP:RGD.
GO; GO:0031000; P:response to caffeine; IEP:RGD.
GO; GO:0010332; P:response to gamma radiation; IEP:RGD.
GO; GO:0035456; P:response to interferon-beta; IEP:RGD.
GO; GO:1903576; P:response to L-arginine; IEP:RGD.
GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
GO; GO:0043278; P:response to morphine; IEP:RGD.
GO; GO:0010238; P:response to proline; IEP:RGD.
InterPro; IPR000407; GDA1_CD39_NTPase.
PANTHER; PTHR11782; PTHR11782; 1.
Pfam; PF01150; GDA1_CD39; 1.
PROSITE; PS01238; GDA1_CD39_NTPASE; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Calcium; Complete proteome; Disulfide bond;
Glycoprotein; Hydrolase; Magnesium; Membrane; Nucleotide-binding;
Reference proteome; Transmembrane; Transmembrane helix.
CHAIN 1 511 Ectonucleoside triphosphate
diphosphohydrolase 1.
/FTId=PRO_0000209904.
TOPO_DOM 1 16 Cytoplasmic. {ECO:0000255}.
TRANSMEM 17 37 Helical. {ECO:0000255}.
TOPO_DOM 38 478 Extracellular. {ECO:0000255}.
TRANSMEM 479 499 Helical. {ECO:0000255}.
TOPO_DOM 500 511 Cytoplasmic. {ECO:0000255}.
REGION 46 171 N-terminal lobe.
REGION 205 441 C-terminal lobe.
ACT_SITE 174 174 Proton acceptor. {ECO:0000250}.
CARBOHYD 73 73 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 226 226 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 291 291 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 333 333 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 374 374 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 429 429 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 458 458 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 84 108 {ECO:0000269|PubMed:22100451}.
DISULFID 254 300 {ECO:0000269|PubMed:22100451}.
DISULFID 281 324 {ECO:0000269|PubMed:22100451}.
DISULFID 337 342 {ECO:0000269|PubMed:22100451}.
DISULFID 391 414 {ECO:0000269|PubMed:22100451}.
CONFLICT 332 332 F -> L (in Ref. 2). {ECO:0000305}.
STRAND 47 55 {ECO:0000244|PDB:3ZX3}.
STRAND 60 68 {ECO:0000244|PDB:3ZX3}.
STRAND 79 85 {ECO:0000244|PDB:3ZX3}.
STRAND 87 89 {ECO:0000244|PDB:3ZX3}.
HELIX 91 94 {ECO:0000244|PDB:3ZX3}.
HELIX 98 100 {ECO:0000244|PDB:3ZX3}.
HELIX 101 115 {ECO:0000244|PDB:3ZX3}.
HELIX 118 121 {ECO:0000244|PDB:3ZX3}.
STRAND 125 130 {ECO:0000244|PDB:3ZX3}.
HELIX 132 140 {ECO:0000244|PDB:3ZX3}.
HELIX 142 157 {ECO:0000244|PDB:3ZX3}.
STRAND 159 168 {ECO:0000244|PDB:3ZX3}.
HELIX 171 185 {ECO:0000244|PDB:3ZX3}.
TURN 186 189 {ECO:0000244|PDB:3ZX3}.
STRAND 209 213 {ECO:0000244|PDB:3ZX3}.
STRAND 215 222 {ECO:0000244|PDB:3ZX3}.
STRAND 229 231 {ECO:0000244|PDB:3ZX3}.
HELIX 232 234 {ECO:0000244|PDB:3ZX3}.
STRAND 235 240 {ECO:0000244|PDB:3ZX3}.
STRAND 243 253 {ECO:0000244|PDB:3ZX3}.
HELIX 257 268 {ECO:0000244|PDB:3ZX3}.
STRAND 273 279 {ECO:0000244|PDB:3ZX3}.
STRAND 287 291 {ECO:0000244|PDB:3ZX3}.
HELIX 292 295 {ECO:0000244|PDB:3ZX3}.
HELIX 299 304 {ECO:0000244|PDB:3ZX3}.
STRAND 311 317 {ECO:0000244|PDB:3ZX3}.
HELIX 321 329 {ECO:0000244|PDB:3ZX3}.
STRAND 338 344 {ECO:0000244|PDB:3ZX3}.
STRAND 356 360 {ECO:0000244|PDB:3ZX3}.
HELIX 361 372 {ECO:0000244|PDB:3ZX3}.
HELIX 380 391 {ECO:0000244|PDB:3ZX3}.
HELIX 395 401 {ECO:0000244|PDB:3ZX3}.
HELIX 407 410 {ECO:0000244|PDB:3ZX3}.
HELIX 413 425 {ECO:0000244|PDB:3ZX3}.
HELIX 432 437 {ECO:0000244|PDB:3ZX3}.
STRAND 438 440 {ECO:0000244|PDB:3ZX3}.
STRAND 442 444 {ECO:0000244|PDB:3ZX3}.
STRAND 447 451 {ECO:0000244|PDB:3ZX2}.
HELIX 452 459 {ECO:0000244|PDB:3ZX3}.
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


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