ENTP2_RAT
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 03-AUG-2022, entry version 137.
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 GlyGen; O35795; 7 sites, 2 N-linked glycans (1 site).
DR iPTMnet; O35795; -.
DR PhosphoSitePlus; O35795; -.
DR PaxDb; O35795; -.
DR PRIDE; O35795; -.
DR GeneID; 64467; -.
DR KEGG; rno:64467; -.
DR UCSC; RGD:69266; rat. [O35795-1]
DR CTD; 954; -.
DR RGD; 69266; Entpd2.
DR eggNOG; KOG1386; Eukaryota.
DR InParanoid; O35795; -.
DR OrthoDB; 1337265at2759; -.
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: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; IDA:RGD.
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: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: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 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; 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
