ID M3YM48_MUSPF Unreviewed; 453 AA.
AC M3YM48;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
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:ENSMPUP00000012405.1,
GN ECO:0000313|RefSeq:XP_004739828.1, ECO:0000313|RefSeq:XP_004739829.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000012405.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000012405.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_004739828.1, ECO:0000313|RefSeq:XP_004739829.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_004739828.1,
RC ECO:0000313|RefSeq:XP_004739829.1};
RG RefSeq;
RL Submitted (NOV-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 EMBL; AEYP01006014; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004739828.1; XM_004739771.3.
DR RefSeq; XP_004739829.1; XM_004739772.3.
DR STRING; 9669.ENSMPUP00000012405; -.
DR Ensembl; ENSMPUT00000012606.1; ENSMPUP00000012405.1; ENSMPUG00000012499.1.
DR GeneID; 101679013; -.
DR KEGG; mpuf:101679013; -.
DR CTD; 22875; -.
DR eggNOG; KOG2645; Eukaryota.
DR GeneTree; ENSGT00940000158831; -.
DR HOGENOM; CLU_017594_1_2_1; -.
DR OMA; INSVDIY; -.
DR OrthoDB; 1366859at2759; -.
DR Proteomes; UP000000715; Unplaced.
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.
PE 3: Inferred from homology;
KW Blood coagulation {ECO:0000256|ARBA:ARBA00023084};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hemostasis {ECO:0000256|ARBA:ARBA00022696};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000000715};
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_5041158880"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 453 AA; 51482 MW; A87F3E49C1CA82AF CRC64;
MKLLVILLFS GLITCCGGNS SHSLPSKLLL VSFDGFRADY LQNYEFPHLQ NFIKEGVLVE
HVKNVFITKT FPNHYSIVTG LYEESHGIVA NSMYDVITKK HFSDFDDKDP FWWNEAVPIW
VTNQLQENRS SAAAMWPGTD VPIHNTTPSY FMNYSSSVSF EERLNNITMW LMNSNPPVTF
ATLYWEEPDA SGHKYGPEDK ENMYRVLKEV DDLIGELVHR LKVLGLWENL NVIITSDHGM
TQCSKDKLIN LDLCIDRSSY TLVDLTPVAA VLPKINTTEV YNKLKVCNPH MNVYLKEDIP
ARFHYQHNDR IQPIILVADE GWTIVLNKSL PKLGDHGYDN SLSSMHPFLA AHGPAFHKGY
KHSTINSVDI YPMMCHILGL KPHPNNGTFG HTKCLLVDQW CINLPEAIGI VIGALLVLTT
LTCLIIIMQN RLSVPRPFSR LQLQEDDDDP LIE
//
