ID   ENTP2_RAT               Reviewed;         495 AA.
AC   O35795; Q9JHY5; Q9WVE7;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   08-NOV-2023, entry version 143.
DE   RecName: Full=Ectonucleoside triphosphate diphosphohydrolase 2;
DE            Short=NTPDase 2;
DE            EC=3.6.1.-;
DE   AltName: Full=CD39 antigen-like 1;
DE   AltName: Full=Ecto-ATP diphosphohydrolase 2;
DE            Short=Ecto-ATPDase 2;
DE            Short=Ecto-ATPase 2;
GN   Name=Entpd2; Synonyms=Cd39l1;
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] (ISOFORM 1), AND CHARACTERIZATION.
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   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=Sprague-Dawley; TISSUE=Sertoli cell;
RX   PubMed=11229804;
RA   Lu Q., Porter L.D., Cui X., Sanborn B.M.;
RT   "Ecto-ATPase mRNA is regulated by FSH in Sertoli cells.";
RL   J. Androl. 22:289-301(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 379-495 (ISOFORM 2).
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   [4]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-64, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=24090084; DOI=10.1021/pr400783j;
RA   Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA   Graham M.E., Packer N.H., Cordwell S.J.;
RT   "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT   heterogeneity.";
RL   J. Proteome Res. 12:5791-5800(2013).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 28-461 ALONE AND IN COMPLEX WITH
RP   ATP ANALOGS AND CALCIUM, ACTIVE SITE, AND DISULFIDE BONDS.
RX   PubMed=18458329; DOI=10.1073/pnas.0802535105;
RA   Zebisch M., Strater N.;
RT   "Structural insight into signal conversion and inactivation by NTPDase2 in
RT   purinergic signaling.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:6882-6887(2008).
CC   -!- FUNCTION: In the nervous system, could hydrolyze ATP and other
CC       nucleotides to regulate purinergic neurotransmission. Hydrolyzes ADP
CC       only to a marginal extent.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000250}; Multi-
CC       pass membrane protein {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O35795-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O35795-2; Sequence=VSP_003613;
CC   -!- TISSUE SPECIFICITY: Expressed in brain, heart, vas deferens, kidney,
CC       skeletal muscle, thymus, lung and spleen. Weak expression in liver.
CC   -!- INDUCTION: By FSH in Sertoli cells but not in peritubular cells; by
CC       cAMP in both type of cells.
CC   -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
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DR   EMBL; Y11835; CAA72533.1; -; mRNA.
DR   EMBL; AF276940; AAF87740.1; -; mRNA.
DR   EMBL; AF129103; AAD42303.1; -; mRNA.
DR   RefSeq; NP_742027.1; NM_172030.1.
DR   PDB; 3CJ1; X-ray; 1.70 A; A=29-461.
DR   PDB; 3CJ7; X-ray; 1.80 A; A=29-461.
DR   PDB; 3CJ9; X-ray; 1.80 A; A=29-461.
DR   PDB; 3CJA; X-ray; 2.10 A; A=29-461.
DR   PDB; 4BQZ; X-ray; 2.05 A; A=28-462.
DR   PDB; 4BR0; X-ray; 2.05 A; A=28-462.
DR   PDB; 4BR2; X-ray; 2.00 A; A=28-462.
DR   PDB; 4BR5; X-ray; 1.75 A; A=28-462.
DR   PDB; 4CD1; X-ray; 2.00 A; A=28-462.
DR   PDB; 4CD3; X-ray; 2.19 A; A=28-461.
DR   PDBsum; 3CJ1; -.
DR   PDBsum; 3CJ7; -.
DR   PDBsum; 3CJ9; -.
DR   PDBsum; 3CJA; -.
DR   PDBsum; 4BQZ; -.
DR   PDBsum; 4BR0; -.
DR   PDBsum; 4BR2; -.
DR   PDBsum; 4BR5; -.
DR   PDBsum; 4CD1; -.
DR   PDBsum; 4CD3; -.
DR   AlphaFoldDB; O35795; -.
DR   SMR; O35795; -.
DR   STRING; 10116.ENSRNOP00000017829; -.
DR   BindingDB; O35795; -.
DR   ChEMBL; CHEMBL3300; -.
DR   DrugCentral; O35795; -.
DR   GlyCosmos; O35795; 7 sites, 2 glycans.
DR   GlyGen; O35795; 7 sites, 2 N-linked glycans (1 site).
DR   iPTMnet; O35795; -.
DR   PhosphoSitePlus; O35795; -.
DR   SwissPalm; O35795; -.
DR   PaxDb; 10116-ENSRNOP00000017829; -.
DR   GeneID; 64467; -.
DR   KEGG; rno:64467; -.
DR   UCSC; RGD:69266; rat. [O35795-1]
DR   AGR; RGD:69266; -.
DR   CTD; 954; -.
DR   RGD; 69266; Entpd2.
DR   eggNOG; KOG1386; Eukaryota.
DR   InParanoid; O35795; -.
DR   OrthoDB; 180318at2759; -.
DR   PhylomeDB; O35795; -.
DR   BRENDA; 3.6.1.5; 5301.
DR   Reactome; R-RNO-8850843; Phosphate bond hydrolysis by NTPDase proteins.
DR   EvolutionaryTrace; O35795; -.
DR   PRO; PR:O35795; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005604; C:basement membrane; ISO:RGD.
DR   GO; GO:0044297; C:cell body; IDA:RGD.
DR   GO; GO:0031253; C:cell projection membrane; IDA:RGD.
DR   GO; GO:0009986; C:cell surface; IDA:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0043262; F:ADP phosphatase 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:0004382; F:GDP phosphatase activity; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR   GO; GO:0017110; F:nucleoside diphosphate phosphatase activity; ISO:RGD.
DR   GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; ISO:RGD.
DR   GO; GO:0045134; F:UDP phosphatase activity; IBA:GO_Central.
DR   GO; GO:0035457; P:cellular response to interferon-alpha; IEP:RGD.
DR   GO; GO:0071354; P:cellular response to interleukin-6; IMP: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: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:0010996; P:response to auditory stimulus; IEP:RGD.
DR   CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR   Gene3D; 3.30.420.40; -; 1.
DR   Gene3D; 3.30.420.150; Exopolyphosphatase. Domain 2; 1.
DR   InterPro; IPR000407; GDA1_CD39_NTPase.
DR   PANTHER; PTHR11782; ADENOSINE/GUANOSINE DIPHOSPHATASE; 1.
DR   PANTHER; PTHR11782:SF33; ECTONUCLEOSIDE TRIPHOSPHATE DIPHOSPHOHYDROLASE 2; 1.
DR   Pfam; PF01150; GDA1_CD39; 1.
DR   PROSITE; PS01238; GDA1_CD39_NTPASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ATP-binding; Calcium; Cell membrane;
KW   Disulfide bond; Glycoprotein; Hydrolase; Magnesium; Membrane;
KW   Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..495
FT                   /note="Ectonucleoside triphosphate diphosphohydrolase 2"
FT                   /id="PRO_0000209908"
FT   TOPO_DOM        1..4
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        26..462
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        463..483
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        484..495
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        165
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000269|PubMed:18458329"
FT   BINDING         204..208
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:18458329"
FT   CARBOHYD        64
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0007744|PubMed:24090084"
FT   CARBOHYD        129
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        294
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        306
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        319
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        378
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        443
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        75..99
FT                   /evidence="ECO:0000269|PubMed:18458329"
FT   DISULFID        242..284
FT                   /evidence="ECO:0000269|PubMed:18458329"
FT   DISULFID        265..310
FT                   /evidence="ECO:0000269|PubMed:18458329"
FT   DISULFID        323..328
FT                   /evidence="ECO:0000269|PubMed:18458329"
FT   DISULFID        377..399
FT                   /evidence="ECO:0000269|PubMed:18458329"
FT   VAR_SEQ         486..495
FT                   /note="VRSAKSPGAL -> DVRSQPVTQGEVHSEWDFCSDLQGPGNFLSGPLERQAP
FT                   EPTGWESVPCLLVKTFVIKDFS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10581401"
FT                   /id="VSP_003613"
FT   CONFLICT        20
FT                   /note="T -> A (in Ref. 2; AAF87740)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        127..128
FT                   /note="PF -> LL (in Ref. 2; AAF87740)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        339
FT                   /note="A -> T (in Ref. 2; AAF87740)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        444
FT                   /note="L -> F (in Ref. 2; AAF87740)"
FT                   /evidence="ECO:0000305"
FT   STRAND          38..46
FT                   /evidence="ECO:0007829|PDB:3CJ1"
FT   STRAND          51..59
FT                   /evidence="ECO:0007829|PDB:3CJ1"
FT   HELIX           60..62
FT                   /evidence="ECO:0007829|PDB:3CJ7"
FT   STRAND          70..76
FT                   /evidence="ECO:0007829|PDB:3CJ1"
FT   STRAND          78..80
FT                   /evidence="ECO:0007829|PDB:3CJ1"
FT   HELIX           82..85
FT                   /evidence="ECO:0007829|PDB:3CJ1"
FT   HELIX           90..95
FT                   /evidence="ECO:0007829|PDB:3CJ1"
FT   HELIX           97..106
FT                   /evidence="ECO:0007829|PDB:3CJ1"
FT   HELIX           109..114
FT                   /evidence="ECO:0007829|PDB:3CJ1"
FT   STRAND          116..121
FT                   /evidence="ECO:0007829|PDB:3CJ1"
FT   HELIX           123..131
FT                   /evidence="ECO:0007829|PDB:3CJ1"
FT   HELIX           133..147
FT                   /evidence="ECO:0007829|PDB:3CJ1"
FT   STRAND          150..159
FT                   /evidence="ECO:0007829|PDB:3CJ1"
FT   HELIX           162..176
FT                   /evidence="ECO:0007829|PDB:3CJ1"
FT   TURN            177..180
FT                   /evidence="ECO:0007829|PDB:3CJ1"
FT   STRAND          198..202
FT                   /evidence="ECO:0007829|PDB:3CJ1"
FT   STRAND          204..212
FT                   /evidence="ECO:0007829|PDB:3CJ1"
FT   HELIX           220..222
FT                   /evidence="ECO:0007829|PDB:3CJ1"
FT   STRAND          223..228
FT                   /evidence="ECO:0007829|PDB:3CJ1"
FT   STRAND          231..241
FT                   /evidence="ECO:0007829|PDB:3CJ1"
FT   HELIX           245..259
FT                   /evidence="ECO:0007829|PDB:3CJ1"
FT   STRAND          261..263
FT                   /evidence="ECO:0007829|PDB:3CJ1"
FT   STRAND          271..275
FT                   /evidence="ECO:0007829|PDB:3CJ1"
FT   HELIX           276..280
FT                   /evidence="ECO:0007829|PDB:3CJ1"
FT   TURN            283..287
FT                   /evidence="ECO:0007829|PDB:3CJ1"
FT   STRAND          298..303
FT                   /evidence="ECO:0007829|PDB:3CJ1"
FT   HELIX           307..315
FT                   /evidence="ECO:0007829|PDB:3CJ1"
FT   STRAND          324..330
FT                   /evidence="ECO:0007829|PDB:3CJ1"
FT   STRAND          342..346
FT                   /evidence="ECO:0007829|PDB:3CJ1"
FT   HELIX           347..357
FT                   /evidence="ECO:0007829|PDB:3CJ1"
FT   HELIX           366..378
FT                   /evidence="ECO:0007829|PDB:3CJ1"
FT   HELIX           381..385
FT                   /evidence="ECO:0007829|PDB:3CJ1"
FT   HELIX           395..397
FT                   /evidence="ECO:0007829|PDB:3CJ1"
FT   HELIX           398..410
FT                   /evidence="ECO:0007829|PDB:3CJ1"
FT   TURN            411..413
FT                   /evidence="ECO:0007829|PDB:4CD1"
FT   HELIX           417..420
FT                   /evidence="ECO:0007829|PDB:3CJ1"
FT   STRAND          423..425
FT                   /evidence="ECO:0007829|PDB:3CJ1"
FT   STRAND          427..429
FT                   /evidence="ECO:0007829|PDB:3CJ1"
FT   HELIX           437..444
FT                   /evidence="ECO:0007829|PDB:3CJ1"
FT   HELIX           453..458
FT                   /evidence="ECO:0007829|PDB:3CJ1"
SQ   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
//