ID G7P4R7_MACFA Unreviewed; 453 AA.
AC G7P4R7;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=bis(5'-adenosyl)-triphosphatase {ECO:0000256|ARBA:ARBA00012377};
DE EC=3.6.1.29 {ECO:0000256|ARBA:ARBA00012377};
DE AltName: Full=AP3A hydrolase {ECO:0000256|ARBA:ARBA00031824};
DE AltName: Full=Ectonucleotide pyrophosphatase/phosphodiesterase family member 4 {ECO:0000256|ARBA:ARBA00031114};
GN Name=ENPP4 {ECO:0000313|Ensembl:ENSMFAP00000026151.2};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000026151.2, ECO:0000313|Proteomes:UP000233100};
RN [1] {ECO:0000313|Ensembl:ENSMFAP00000026151.2, ECO:0000313|Proteomes:UP000233100}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMFAP00000026151.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Hydrolyzes extracellular Ap3A into AMP and ADP, and Ap4A into
CC AMP and ATP. Ap3A and Ap4A are diadenosine polyphosphates thought to
CC induce proliferation of vascular smooth muscle cells. Acts as a
CC procoagulant, mediating platelet aggregation at the site of nascent
CC thrombus via release of ADP from Ap3A and activation of ADP receptors.
CC {ECO:0000256|ARBA:ARBA00025036}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + P(1),P(3)-bis(5'-adenosyl) triphosphate = ADP + AMP + 2
CC H(+); Xref=Rhea:RHEA:13893, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58529, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216;
CC EC=3.6.1.29; Evidence={ECO:0000256|ARBA:ARBA00001475};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the nucleotide pyrophosphatase/phosphodiesterase
CC family. {ECO:0000256|ARBA:ARBA00010594}.
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DR AlphaFoldDB; G7P4R7; -.
DR SMR; G7P4R7; -.
DR STRING; 9541.ENSMFAP00000026151; -.
DR Ensembl; ENSMFAT00000029827.2; ENSMFAP00000026151.2; ENSMFAG00000044542.2.
DR VEuPathDB; HostDB:ENSMFAG00000044542; -.
DR eggNOG; KOG2645; Eukaryota.
DR GeneTree; ENSGT00940000158831; -.
DR OrthoDB; 1366859at2759; -.
DR Proteomes; UP000233100; Chromosome 4.
DR Bgee; ENSMFAG00000044542; Expressed in heart and 13 other cell types or tissues.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0047710; F:bis(5'-adenosyl)-triphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR GO; GO:0030194; P:positive regulation of blood coagulation; IEA:Ensembl.
DR GO; GO:0046130; P:purine ribonucleoside catabolic process; IEA:Ensembl.
DR CDD; cd16018; Enpp; 1.
DR Gene3D; 3.30.1360.180; -; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR PANTHER; PTHR10151:SF79; BIS(5'-ADENOSYL)-TRIPHOSPHATASE ENPP4; 1.
DR PANTHER; PTHR10151; ECTONUCLEOTIDE PYROPHOSPHATASE/PHOSPHODIESTERASE; 1.
DR Pfam; PF01663; Phosphodiest; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Blood coagulation {ECO:0000256|ARBA:ARBA00023084};
KW Hemostasis {ECO:0000256|ARBA:ARBA00022696};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000233100};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..453
FT /note="bis(5'-adenosyl)-triphosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014304005"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 453 AA; 51539 MW; C9F6AF7225FB5DBD CRC64;
MKLLVILLFS GLITGCRSDS SSSLPPKLLL VSFDGFRADY LKNYEFPHLQ NFIKEGVLVE
HVKNVFITKT FPNHYSIVTG LYEESHGIVA NSMYDAVTKK HFSDSNDKDP FWWNEAVPIW
VTNQLQENRS SAAAMWPGTD VPIHNTTSSY FMNYNSSVSF EERLNNITMW LNNSNPPVTF
ATLYWEEPDA SGHKYGPEDK ENMSRVLKKI DDLIGDLVQK LKMLGLWENL NVIITSDHGM
TQCSQDRLIN LDVCIDHSYY TLIDLSPVAA ILPKINRTEV YNKLKNCNSH MNVYLKEDIP
NRFYYQHNDR IQPIILVANE GWTIVLNKSS QKLGDHGYDN SLPSMHPFLA AHGPAFHKGY
KHSTINIVDI YPMMCHILGL KPHPNNGTFG HTKCLLVDQW CINLPEAIAI VVGSLLVLTT
LTCLIIIMQN RLSVPRPFSR LQLQEDDDDP LIG
//
