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Ectonucleoside triphosphate diphosphohydrolase 2 (NTPDase 2) (EC 3.6.1.-) (CD39 antigen-like 1) (Ecto-ATP diphosphohydrolase 2) (Ecto-ATPDase 2) (Ecto-ATPase 2)

 ENTP2_RAT               Reviewed;         495 AA.
O35795; Q9JHY5; Q9WVE7;
29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
22-NOV-2017, entry version 119.
RecName: Full=Ectonucleoside triphosphate diphosphohydrolase 2;
Short=NTPDase 2;
EC=3.6.1.-;
AltName: Full=CD39 antigen-like 1;
AltName: Full=Ecto-ATP diphosphohydrolase 2;
Short=Ecto-ATPDase 2;
Short=Ecto-ATPase 2;
Name=Entpd2; Synonyms=Cd39l1;
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] (ISOFORM 1), AND CHARACTERIZATION.
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=Sprague-Dawley; TISSUE=Sertoli cell;
PubMed=11229804;
Lu Q., Porter L.D., Cui X., Sanborn B.M.;
"Ecto-ATPase mRNA is regulated by FSH in Sertoli cells.";
J. Androl. 22:289-301(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 379-495 (ISOFORM 2).
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).
[4]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 28-461 ALONE AND IN COMPLEX
WITH ATP ANALOGS AND CALCIUM, ACTIVE SITE, AND DISULFIDE BONDS.
PubMed=18458329; DOI=10.1073/pnas.0802535105;
Zebisch M., Strater N.;
"Structural insight into signal conversion and inactivation by
NTPDase2 in purinergic signaling.";
Proc. Natl. Acad. Sci. U.S.A. 105:6882-6887(2008).
-!- FUNCTION: In the nervous system, could hydrolyze ATP and other
nucleotides to regulate purinergic neurotransmission. Hydrolyzes
ADP only to a marginal extent.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane {ECO:0000250};
Multi-pass membrane protein {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O35795-1; Sequence=Displayed;
Name=2;
IsoId=O35795-2; Sequence=VSP_003613;
-!- TISSUE SPECIFICITY: Expressed in brain, heart, vas deferens,
kidney, skeletal muscle, thymus, lung and spleen. Weak expression
in liver.
-!- INDUCTION: By FSH in Sertoli cells but not in peritubular cells;
by cAMP in both type of cells.
-!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; Y11835; CAA72533.1; -; mRNA.
EMBL; AF276940; AAF87740.1; -; mRNA.
EMBL; AF129103; AAD42303.1; -; mRNA.
RefSeq; NP_742027.1; NM_172030.1.
UniGene; Rn.8276; -.
PDB; 3CJ1; X-ray; 1.70 A; A=29-461.
PDB; 3CJ7; X-ray; 1.80 A; A=29-461.
PDB; 3CJ9; X-ray; 1.80 A; A=29-461.
PDB; 3CJA; X-ray; 2.10 A; A=29-461.
PDB; 4BQZ; X-ray; 2.05 A; A=28-462.
PDB; 4BR0; X-ray; 2.05 A; A=28-462.
PDB; 4BR2; X-ray; 2.00 A; A=28-462.
PDB; 4BR5; X-ray; 1.75 A; A=28-462.
PDB; 4CD1; X-ray; 2.00 A; A=28-462.
PDB; 4CD3; X-ray; 2.19 A; A=28-461.
PDBsum; 3CJ1; -.
PDBsum; 3CJ7; -.
PDBsum; 3CJ9; -.
PDBsum; 3CJA; -.
PDBsum; 4BQZ; -.
PDBsum; 4BR0; -.
PDBsum; 4BR2; -.
PDBsum; 4BR5; -.
PDBsum; 4CD1; -.
PDBsum; 4CD3; -.
ProteinModelPortal; O35795; -.
SMR; O35795; -.
STRING; 10116.ENSRNOP00000017829; -.
BindingDB; O35795; -.
ChEMBL; CHEMBL3300; -.
iPTMnet; O35795; -.
PhosphoSitePlus; O35795; -.
UniCarbKB; O35795; -.
PaxDb; O35795; -.
PRIDE; O35795; -.
GeneID; 64467; -.
KEGG; rno:64467; -.
UCSC; RGD:69266; rat. [O35795-1]
CTD; 954; -.
RGD; 69266; Entpd2.
eggNOG; KOG1386; Eukaryota.
eggNOG; COG5371; LUCA.
HOGENOM; HOG000059572; -.
HOVERGEN; HBG018982; -.
InParanoid; O35795; -.
KO; K01509; -.
PhylomeDB; O35795; -.
BRENDA; 3.6.1.5; 5301.
EvolutionaryTrace; O35795; -.
PRO; PR:O35795; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005605; C:basal lamina; ISO:RGD.
GO; GO:0044297; C:cell body; IDA:RGD.
GO; GO:0031253; C:cell projection membrane; IDA:RGD.
GO; GO:0009986; C:cell surface; IDA:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
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: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:0035457; P:cellular response to interferon-alpha; IEP:RGD.
GO; GO:0071354; P:cellular response to interleukin-6; IMP: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: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:0010996; P:response to auditory stimulus; 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; Alternative splicing; ATP-binding; Calcium;
Cell membrane; Complete proteome; Disulfide bond; Glycoprotein;
Hydrolase; Magnesium; Membrane; Nucleotide-binding;
Reference proteome; Transmembrane; Transmembrane helix.
CHAIN 1 495 Ectonucleoside triphosphate
diphosphohydrolase 2.
/FTId=PRO_0000209908.
TOPO_DOM 1 4 Cytoplasmic. {ECO:0000255}.
TRANSMEM 5 25 Helical. {ECO:0000255}.
TOPO_DOM 26 462 Extracellular. {ECO:0000255}.
TRANSMEM 463 483 Helical. {ECO:0000255}.
TOPO_DOM 484 495 Cytoplasmic. {ECO:0000255}.
NP_BIND 204 208 ATP.
ACT_SITE 165 165 Proton acceptor.
{ECO:0000269|PubMed:18458329}.
CARBOHYD 64 64 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 129 129 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 294 294 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 306 306 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 319 319 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 378 378 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 443 443 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 75 99 {ECO:0000269|PubMed:18458329}.
DISULFID 242 284 {ECO:0000269|PubMed:18458329}.
DISULFID 265 310 {ECO:0000269|PubMed:18458329}.
DISULFID 323 328 {ECO:0000269|PubMed:18458329}.
DISULFID 377 399 {ECO:0000269|PubMed:18458329}.
VAR_SEQ 486 495 VRSAKSPGAL -> DVRSQPVTQGEVHSEWDFCSDLQGPGN
FLSGPLERQAPEPTGWESVPCLLVKTFVIKDFS (in
isoform 2).
{ECO:0000303|PubMed:10581401}.
/FTId=VSP_003613.
CONFLICT 20 20 T -> A (in Ref. 2; AAF87740).
{ECO:0000305}.
CONFLICT 127 128 PF -> LL (in Ref. 2; AAF87740).
{ECO:0000305}.
CONFLICT 339 339 A -> T (in Ref. 2; AAF87740).
{ECO:0000305}.
CONFLICT 444 444 L -> F (in Ref. 2; AAF87740).
{ECO:0000305}.
STRAND 38 46 {ECO:0000244|PDB:3CJ1}.
STRAND 51 59 {ECO:0000244|PDB:3CJ1}.
HELIX 60 62 {ECO:0000244|PDB:3CJ7}.
STRAND 70 76 {ECO:0000244|PDB:3CJ1}.
STRAND 78 80 {ECO:0000244|PDB:3CJ1}.
HELIX 82 85 {ECO:0000244|PDB:3CJ1}.
HELIX 90 95 {ECO:0000244|PDB:3CJ1}.
HELIX 97 106 {ECO:0000244|PDB:3CJ1}.
HELIX 109 114 {ECO:0000244|PDB:3CJ1}.
STRAND 116 121 {ECO:0000244|PDB:3CJ1}.
HELIX 123 131 {ECO:0000244|PDB:3CJ1}.
HELIX 133 147 {ECO:0000244|PDB:3CJ1}.
STRAND 150 159 {ECO:0000244|PDB:3CJ1}.
HELIX 162 176 {ECO:0000244|PDB:3CJ1}.
TURN 177 180 {ECO:0000244|PDB:3CJ1}.
STRAND 198 202 {ECO:0000244|PDB:3CJ1}.
STRAND 204 212 {ECO:0000244|PDB:3CJ1}.
HELIX 220 222 {ECO:0000244|PDB:3CJ1}.
STRAND 223 228 {ECO:0000244|PDB:3CJ1}.
STRAND 231 241 {ECO:0000244|PDB:3CJ1}.
HELIX 245 259 {ECO:0000244|PDB:3CJ1}.
STRAND 261 263 {ECO:0000244|PDB:3CJ1}.
STRAND 271 275 {ECO:0000244|PDB:3CJ1}.
HELIX 276 280 {ECO:0000244|PDB:3CJ1}.
TURN 283 287 {ECO:0000244|PDB:3CJ1}.
STRAND 298 303 {ECO:0000244|PDB:3CJ1}.
HELIX 307 315 {ECO:0000244|PDB:3CJ1}.
STRAND 324 330 {ECO:0000244|PDB:3CJ1}.
STRAND 342 346 {ECO:0000244|PDB:3CJ1}.
HELIX 347 357 {ECO:0000244|PDB:3CJ1}.
HELIX 366 378 {ECO:0000244|PDB:3CJ1}.
HELIX 381 385 {ECO:0000244|PDB:3CJ1}.
HELIX 395 397 {ECO:0000244|PDB:3CJ1}.
HELIX 398 410 {ECO:0000244|PDB:3CJ1}.
TURN 411 413 {ECO:0000244|PDB:4CD1}.
HELIX 417 420 {ECO:0000244|PDB:3CJ1}.
STRAND 423 425 {ECO:0000244|PDB:3CJ1}.
STRAND 427 429 {ECO:0000244|PDB:3CJ1}.
HELIX 437 444 {ECO:0000244|PDB:3CJ1}.
HELIX 453 458 {ECO:0000244|PDB:3CJ1}.
SEQUENCE 495 AA; 54390 MW; 237B999F1BEB8E00 CRC64;
MAGKLVSLVP PLLLAAAGLT GLLLLCVPTQ DVREPPALKY GIVLDAGSSH TSMFVYKWPA
DKENDTGIVG QHSSCDVQGG GISSYANDPS KAGQSLVRCL EQALRDVPRD RHASTPLYLG
ATAGMRPFNL TSPEATARVL EAVTQTLTQY PFDFRGARIL SGQDEGVFGW VTANYLLENF
IKYGWVGRWI RPRKGTLGAM DLGGASTQIT FETTSPSEDP GNEVHLRLYG QHYRVYTHSF
LCYGRDQILL RLLASALQIH RFHPCWPKGY STQVLLQEVY QSPCTMGQRP RAFNGSAIVS
LSGTSNATLC RDLVSRLFNI SSCPFSQCSF NGVFQPPVAG NFIAFSAFYY TVDFLTTVMG
LPVGTLKQLE EATEITCNQT WTELQARVPG QKTRLADYCA VAMFIHQLLS RGYHFDERSF
REVVFQKKAA DTAVGWALGY MLNLTNLIPA DLPGLRKGTH FSSWVALLLL FTVLILAALV
LLLRQVRSAK SPGAL


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