ENTP2_CHICK
ID ENTP2_CHICK Reviewed; 495 AA.
AC P79784;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 121.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-22; 69-74; 84-91;
RP 108; 121; 145-151; 155-177; 209-218; 252-259; 274-285; 338-353; 375-381;
RP 384-390; 449-457 AND 460-480.
RC TISSUE=Gizzard, and Skeletal muscle;
RX PubMed=8995405; DOI=10.1074/jbc.272.2.1076;
RA Kirley T.L.;
RT "Complementary DNA cloning and sequencing of the chicken muscle ecto-
RT ATPase. Homology with the lymphoid cell activation antigen CD39.";
RL J. Biol. Chem. 272:1076-1081(1997).
RN [2]
RP PROTEIN SEQUENCE OF 2-13 AND 155-177, AND CHARACTERIZATION.
RX PubMed=7989647; DOI=10.1016/0165-022x(94)90057-4;
RA Stout J.G., Kirley T.L.;
RT "Purification and characterization of the ecto-Mg-ATPase of chicken gizzard
RT smooth muscle.";
RL J. Biochem. Biophys. Methods 29:61-75(1994).
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 (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
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DR EMBL; U74467; AAC60071.1; -; mRNA.
DR AlphaFoldDB; P79784; -.
DR SMR; P79784; -.
DR STRING; 9031.ENSGALP00000014728; -.
DR PaxDb; P79784; -.
DR VEuPathDB; HostDB:geneid_395797; -.
DR eggNOG; KOG1386; Eukaryota.
DR InParanoid; P79784; -.
DR PhylomeDB; P79784; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:AgBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004382; F:guanosine-diphosphatase activity; IBA:GO_Central.
DR GO; GO:0017110; F:nucleoside-diphosphatase activity; IBA:GO_Central.
DR GO; GO:0045134; F:uridine-diphosphatase activity; IBA:GO_Central.
DR GO; GO:0009134; P:nucleoside diphosphate catabolic process; IBA:GO_Central.
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 ATP-binding; Calcium; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Hydrolase; Magnesium; Membrane; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7989647,
FT ECO:0000269|PubMed:8995405"
FT CHAIN 2..495
FT /note="Ectonucleoside triphosphate diphosphohydrolase 2"
FT /id="PRO_0000209909"
FT TOPO_DOM 2..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..465
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 466..486
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 487..495
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 162
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O35795"
FT BINDING 201..205
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O35795"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 73..97
FT /evidence="ECO:0000250|UniProtKB:O35795"
FT DISULFID 239..286
FT /evidence="ECO:0000250|UniProtKB:O35795"
FT DISULFID 267..311
FT /evidence="ECO:0000250|UniProtKB:O35795"
FT DISULFID 324..329
FT /evidence="ECO:0000250|UniProtKB:O35795"
FT DISULFID 378..400
FT /evidence="ECO:0000250|UniProtKB:O35795"
FT CONFLICT 12
FT /note="L -> LL (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 175..177
FT /note="ENF -> GNK (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ 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
