ID A0A2I0LMD1_COLLI Unreviewed; 493 AA.
AC A0A2I0LMD1;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Ectonucleoside triphosphate diphosphohydrolase 8 {ECO:0000256|ARBA:ARBA00039598};
DE EC=3.6.1.5 {ECO:0000256|ARBA:ARBA00012148};
GN ORFNames=A306_00014239 {ECO:0000313|EMBL:PKK18584.1};
OS Columba livia (Rock dove).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX NCBI_TaxID=8932 {ECO:0000313|EMBL:PKK18584.1, ECO:0000313|Proteomes:UP000053872};
RN [1] {ECO:0000313|EMBL:PKK18584.1, ECO:0000313|Proteomes:UP000053872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Blood {ECO:0000313|EMBL:PKK18584.1};
RX PubMed=23371554; DOI=10.1126/science.1230422;
RA Shapiro M.D., Kronenberg Z., Li C., Domyan E.T., Pan H., Campbell M.,
RA Tan H., Huff C.D., Hu H., Vickrey A.I., Nielsen S.C., Stringham S.A.,
RA Hu H., Willerslev E., Gilbert M.T., Yandell M., Zhang G., Wang J.;
RT "Genomic diversity and evolution of the head crest in the rock pigeon.";
RL Science 339:1063-1067(2013).
RN [2] {ECO:0000313|EMBL:PKK18584.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Blood {ECO:0000313|EMBL:PKK18584.1};
RA Holt C., Campbell M., Edelman N., Keays D., Kapusta A., Domyan E., Suh A.,
RA Carleton J., Warren W., Yandell M., Gilbert M.T., Shapiro M.D.;
RT "Improved genome assembly and annotation for the rock pigeon (Columba
RT livia).";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + 2 H2O = a ribonucleoside
CC 5'-phosphate + 2 H(+) + 2 phosphate; Xref=Rhea:RHEA:36795,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.5;
CC Evidence={ECO:0000256|ARBA:ARBA00000211};
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC {ECO:0000256|ARBA:ARBA00009283, ECO:0000256|RuleBase:RU003833}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PKK18584.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AKCR02000194; PKK18582.1; -; Genomic_DNA.
DR EMBL; AKCR02000194; PKK18583.1; -; Genomic_DNA.
DR EMBL; AKCR02000194; PKK18584.1; -; Genomic_DNA.
DR RefSeq; XP_005511845.1; XM_005511788.1.
DR RefSeq; XP_005511846.1; XM_005511789.1.
DR RefSeq; XP_005511847.1; XM_005511790.1.
DR AlphaFoldDB; A0A2I0LMD1; -.
DR STRING; 8932.A0A2I0LMD1; -.
DR GeneID; 102096210; -.
DR KEGG; clv:102096210; -.
DR CTD; 377841; -.
DR InParanoid; A0A2I0LMD1; -.
DR OrthoDB; 180318at2759; -.
DR Proteomes; UP000053872; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; 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:SF31; ECTONUCLEOSIDE TRIPHOSPHATE DIPHOSPHOHYDROLASE 8; 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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000256|RuleBase:RU003833, ECO:0000313|EMBL:PKK18584.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000053872};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 465..490
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 166
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 206..210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 493 AA; 53940 MW; 2BB7074313F75767 CRC64;
MDYKAKAVAG LLAATCVFSI IALILSVVQV KNVFLPPSTK YGLVFDAGST HTALYIYQWP
GDKENGTGIV SQVEACAVSG PGISSYADDP AGAGASLKPC LDKAMEIVPA EQQRDTPTYL
GATAGMRLLR EQNSTKADQV FAEITKAIGE YPVDFRGARI LTGNEEGSFG WITVNYLLET
LVKFSFAEKW EHPQDTEVLG ALDLGGASTQ ITFQPGVTIE DKNTSVSFRL YGTNYSLYTH
SYLCYGQTQA LKMLLAALHQ GNLSSQHISH PCYPSEYQEN VTTAELYNSP CVHAPNTSSP
AQVLTVTGTG DPVACSIAVQ KLFNISCGAN RTCGFNGVYQ PPVRGQFFAF AGFYYTFHFL
NLTSQQSLND VKLTVQDFCK RPWAELVETF PQQKGNLHTY CSVAIYILTL LFDGYKFDEH
TWSSIQFRRQ AANTDIGWTL GFMLNFTNTI PTEALEHVKG HQPSLWAGAV SFIVLAIVAG
LVAAVLQCFW KTK
//
