ID H0W990_CAVPO Unreviewed; 530 AA.
AC H0W990;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Ectonucleoside triphosphate diphosphohydrolase 3 {ECO:0000313|Ensembl:ENSCPOP00000019548.2};
GN Name=ENTPD3 {ECO:0000313|Ensembl:ENSCPOP00000019548.2};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000019548.2, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000019548.2}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000019548.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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; AAKN02012232; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003476907.2; XM_003476859.3.
DR AlphaFoldDB; H0W990; -.
DR STRING; 10141.ENSCPOP00000019548; -.
DR Ensembl; ENSCPOT00000025093.2; ENSCPOP00000019548.2; ENSCPOG00000026506.2.
DR GeneID; 100733912; -.
DR KEGG; cpoc:100733912; -.
DR CTD; 956; -.
DR VEuPathDB; HostDB:ENSCPOG00000026506; -.
DR eggNOG; KOG1386; Eukaryota.
DR GeneTree; ENSGT01100000263542; -.
DR HOGENOM; CLU_010246_2_3_1; -.
DR InParanoid; H0W990; -.
DR OMA; GNAISDM; -.
DR OrthoDB; 180318at2759; -.
DR TreeFam; TF332859; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000026506; Expressed in adrenal gland and 9 other cell types or tissues.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0017110; F:nucleoside diphosphate phosphatase activity; IEA:Ensembl.
DR GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:Ensembl.
DR GO; GO:0009134; P:nucleoside diphosphate catabolic process; IEA:Ensembl.
DR GO; GO:0009143; P:nucleoside triphosphate catabolic process; IEA:Ensembl.
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:SF38; ECTONUCLEOSIDE TRIPHOSPHATE DIPHOSPHOHYDROLASE 3; 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:UP000005447};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 487..509
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 183
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 223..227
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 530 AA; 58251 MW; CD0CFA72D8ABC3BD CRC64;
MLAAGTRRPH AHAGLQTLSR TPAIVVSLAV LLLSVMVLTT LTLVQTRHSQ VIPPGLKYGI
VLDAGSSRTT VYVYQWPAEK ENNTGVVSQT FKCSVRGPGI SSYGDNPQDA PTAFEDCMQR
VQQQVPVSLH RSTRVYLGAT AGMRLLRLQN ETAAEEILAS IQSYFRSQPF DFRGAQIISG
QEEGVYGWIT ANYIQGNFLE KDLWHTWVHP HGAGTTGALD LGGASTQIAF AVGDTGMQNA
SDVVQVALYG YTYVLYTHSF QCYGRNEAEK RFLALLLQNS SAATQVTNPC YPRGYRVTIP
MGQVFDSLCT VQQKPASYDP LHSVIFKGTG DPGLCRETMA SIFDFSACRG QEDCSFDGVY
QPKVQGPFVA FAGFYYTASA LNLSGSFPLA TFNASTWHFC SHTWAELPIL LPKFDEVYAR
SYCFSANYIY HLLVHGYKFT HETWPQIQFE KEVGNSSIGW SLGYMLSLTN QIPAVSALVR
LSIPPPAFMG LLAFFTASTL LSLAFLAFLC SAARTEKRSE HALEHAVDAD
//