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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_CHICK             Reviewed;         495 AA.
P79784;
29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
10-MAY-2017, entry version 106.
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;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-22; 69-74;
84-91; 108; 121; 145-151; 155-177; 209-218; 252-259; 274-285; 338-353;
375-381; 384-390; 449-457 AND 460-480.
TISSUE=Gizzard, and Skeletal muscle;
PubMed=8995405; DOI=10.1074/jbc.272.2.1076;
Kirley T.L.;
"Complementary DNA cloning and sequencing of the chicken muscle ecto-
ATPase. Homology with the lymphoid cell activation antigen CD39.";
J. Biol. Chem. 272:1076-1081(1997).
[2]
PROTEIN SEQUENCE OF 2-13 AND 155-177, AND CHARACTERIZATION.
PubMed=7989647; DOI=10.1016/0165-022X(94)90057-4;
Stout J.G., Kirley T.L.;
"Purification and characterization of the ecto-Mg-ATPase of chicken
gizzard smooth muscle.";
J. Biochem. Biophys. Methods 29:61-75(1994).
-!- FUNCTION: In the nervous system, could hydrolyze ATP and other
nucleotides to regulate purinergic neurotransmission. Hydrolyzes
ADP only to a marginal extent (By similarity). {ECO:0000250}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
protein {ECO:0000305}.
-!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U74467; AAC60071.1; -; mRNA.
UniGene; Gga.44860; -.
ProteinModelPortal; P79784; -.
SMR; P79784; -.
STRING; 9031.ENSGALP00000014728; -.
PaxDb; P79784; -.
eggNOG; KOG1386; Eukaryota.
eggNOG; COG5371; LUCA.
HOGENOM; HOG000059572; -.
HOVERGEN; HBG018982; -.
InParanoid; P79784; -.
PhylomeDB; P79784; -.
Proteomes; UP000000539; Unplaced.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:AgBase.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; IDA:AgBase.
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;
ATP-binding; Calcium; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; Hydrolase; Magnesium; Membrane;
Nucleotide-binding; Reference proteome; Transmembrane;
Transmembrane helix.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:7989647,
ECO:0000269|PubMed:8995405}.
CHAIN 2 495 Ectonucleoside triphosphate
diphosphohydrolase 2.
/FTId=PRO_0000209909.
TOPO_DOM 2 4 Cytoplasmic. {ECO:0000255}.
TRANSMEM 5 25 Helical. {ECO:0000255}.
TOPO_DOM 26 465 Extracellular. {ECO:0000255}.
TRANSMEM 466 486 Helical. {ECO:0000255}.
TOPO_DOM 487 495 Cytoplasmic. {ECO:0000255}.
NP_BIND 201 205 ATP. {ECO:0000250}.
COMPBIAS 9 14 Poly-Leu.
ACT_SITE 162 162 Proton acceptor. {ECO:0000250}.
CARBOHYD 62 62 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 297 297 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 418 418 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 444 444 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 73 97 {ECO:0000250}.
DISULFID 239 286 {ECO:0000250}.
DISULFID 267 311 {ECO:0000250}.
DISULFID 324 329 {ECO:0000250}.
DISULFID 378 400 {ECO:0000250}.
CONFLICT 12 12 L -> LL (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 175 177 ENF -> GNK (in Ref. 2; AA sequence).
{ECO:0000305}.
SEQUENCE 495 AA; 54534 MW; 0C472AF15482A9DF CRC64;
MARRAAAVLL LLALGCLLGI LLLCLGSGDA RGPPSFKYGI VLDAGSSHTA VFIYKWPADK
ENDTGVVSEH SMCDVEGPGI SSYSSKPPAA GKSLEHCLSQ AMRDVPKEKH ADTPLYLGAT
AGMRLLTIAD PPSQTCLSAV MATLKSYPFD FGGAKILSGE EEGVFGWITA NYLLENFIKR
GWLGEWIQSK KKTLGAMDFG GASTQITFET SDAIEDPKNE VMLKLYGQPY KVYTHSFLCY
GRDQVLKRLL SKVLQAENYQ ETVANPCWPT GYRKSLSLSS IYDSPCTEKE RPGLPLNTTV
VVSGTGNGNL CAVHVNKLFD FTSCSFSHCS FDGVFQPEVS GNFIAFSAFF YTVDFIRTVM
ERPVHSPSDL KDAAETICAT SWNELYQKAP RLEKRLPDYC ATSTFVYLLI TKGYNFNNRS
FPSIAFQKKA GETSIGWALG YMLNLTNMIP AQEPASHRSM LYNYWVILIL LFVITTLTAL
LTAVYLLRRS KSSTI


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