ID A7YWN0_BOVIN Unreviewed; 495 AA.
AC A7YWN0;
DT 23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 23-OCT-2007, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE SubName: Full=ENTPD2 protein {ECO:0000313|EMBL:AAI34660.1};
GN Name=ENTPD2 {ECO:0000313|EMBL:AAI34660.1};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|EMBL:AAI34660.1};
RN [1] {ECO:0000313|EMBL:AAI34660.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=L1 Hereford {ECO:0000313|EMBL:AAI34660.1};
RC TISSUE=Fetal skin {ECO:0000313|EMBL:AAI34660.1};
RA Moore S., Alexander L., Brownstein M., Guan L., Lobo S., Meng Y.,
RA Tanaguchi M., Wang Z., Yu J., Prange C., Schreiber K., Shenmen C.,
RA Wagner L., Bala M., Barbazuk S., Barber S., Babakaiff R., Beland J.,
RA Chun E., Del Rio L., Gibson S., Hanson R., Kirkpatrick R., Liu J.,
RA Matsuo C., Mayo M., Santos R.R., Stott J., Tsai M., Wong D., Siddiqui A.,
RA Holt R., Jones S.J., Marra M.A.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC {ECO:0000256|ARBA:ARBA00009283, ECO:0000256|RuleBase:RU003833}.
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DR EMBL; BC134659; AAI34660.1; -; mRNA.
DR RefSeq; NP_001099118.1; NM_001105648.1.
DR AlphaFoldDB; A7YWN0; -.
DR SMR; A7YWN0; -.
DR GeneID; 100126045; -.
DR KEGG; bta:100126045; -.
DR CTD; 954; -.
DR OrthoDB; 180318at2759; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Hydrolase {ECO:0000256|RuleBase:RU003833};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 461..483
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 165
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 204..208
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 495 AA; 53897 MW; D6F2CA9F3D1F686F CRC64;
MAGKALSLLP PLLLAAAGLA GLLLLCVPTR DIREPPALKY GIVLDAGSSH TSMFIYKWPA
DKENDTGIVG QHSSCDAQGG GISSYADNPS GAGQSLVECL NQALRDVPKE RHAGTPLYLG
ATAGMRLLNL TSPEASANVL AAVTQTLTQY PFDFRGARIL SGQDEGVFGW VTANYLLENF
IKYGWVGRWF RPRKGTLGAM DLGGASTQIT FETTSPTEDP ANEVQLRLYG QRYRVYTHSF
LCYGRDQVLR RLLARALQTH GSHPCWPRGY STHVMLWDVY ELPCTAAQRP QAFNRSARVS
LAGSSDPALC RSLVSQLFNS SSCHFSRCSF NGVFQPPVAG KFIAFSAFFY TMDFLRTVMG
LPVATLQQLE GAVVTLCNQT WSELQARAPD DRARLPDYCA GAMFVQQLLS RGYGFDERSF
GGVTFQKKAG DTAVGWALGY MLNLTNLIPA DPPGLRKGTD FSSWVVLLLL FAAMLLAAFA
LLLHQARSTK SASTI
//
