ID A0A3P8YJH0_ESOLU Unreviewed; 472 AA.
AC A0A3P8YJH0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Ectonucleoside triphosphate diphosphohydrolase 2b {ECO:0000313|Ensembl:ENSELUP00000016678.2};
GN Name=ENTPD2 {ECO:0000313|Ensembl:ENSELUP00000016678.2};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000016678.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000016678.2, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000016678.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC {ECO:0000256|ARBA:ARBA00009283, ECO:0000256|RuleBase:RU003833}.
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DR AlphaFoldDB; A0A3P8YJH0; -.
DR Ensembl; ENSELUT00000039863.2; ENSELUP00000016678.2; ENSELUG00000016455.2.
DR GeneTree; ENSGT01100000263542; -.
DR OrthoDB; 180318at2759; -.
DR Proteomes; UP000265140; LG14.
DR Bgee; ENSELUG00000016455; Expressed in nose and 12 other cell types or tissues.
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 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000265140};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..29
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 472 AA; 51950 MW; BF18ED8B249DAB23 CRC64;
MAKQYFHVFL AFALLLFGIV SILLLTIPIG DLTAPPEFMY GIVLDAGSSH TSMYIYKWPA
DKQNDTGVVT QHSECHPKGG GISSYAGQQG AAGKSLEDCL NQAMQDIPRA RHELTPVYLG
ATAGMRLLNI SSPEHSAQVL QEVGQKIKSY PFKYQGAAIL SGQDEGAYGW VTVNYLLENF
IKYGFMGRWL SPGRPTVGAL DFGGASIQIT FVTKDEVEDA KDRKKLRLYG HDYSLYTHSF
LCFGRDQVLK RLLASLVKAQ GHTGSVFHPC FPAGYSTTIK METLFDSPCT VAQKPSSGYN
PQAALSVVGS GDYDHCLGNI TELFSFSSCP FSKCSFNQVF QPNVSGHFMA FSSFFHVHQF
LLSATGIDVT TPAQLEKATR AICNMSINQT LALVPDQRPR LQDFCAASLF TKVLLTRGYR
FDEKSFPHIS FQNKVSFIDG NICFLSPSFT PHVSIIIHVT QSHVSVVQAL YS
//
