ID R4GNJ8_PONAB Unreviewed; 453 AA.
AC R4GNJ8; A0A2J8Y4Z7;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
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:ENSPPYP00000018644};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000018644, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000018644, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPPYP00000018644}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAY-2013) 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 RefSeq; XP_009240203.1; XM_009241928.1.
DR AlphaFoldDB; R4GNJ8; -.
DR Ensembl; ENSPPYT00000019383; ENSPPYP00000018644; ENSPPYG00000016666.
DR GeneID; 100172690; -.
DR CTD; 22875; -.
DR GeneTree; ENSGT00940000158831; -.
DR HOGENOM; CLU_017594_1_2_1; -.
DR InParanoid; R4GNJ8; -.
DR OrthoDB; 1366859at2759; -.
DR Proteomes; UP000001595; Chromosome 6.
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 Hemostasis {ECO:0000256|ARBA:ARBA00022696};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001595};
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..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..453
FT /note="bis(5'-adenosyl)-triphosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014593326"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 453 AA; 51628 MW; 86402F6D3AFFA163 CRC64;
MKLLVILLFS GLITGFRSDS SSSLPPKLLL VSFDGFRADY LNNYEFPHLQ NFIKEGVLVE
HVKNVFITKT FPNHYSIVTG LYEESHGIVA NSMYDAVTKK HFSDSNDKDP FWWNEAVPIW
VTNQLQENRS SAAAMWPGTD VPIHNTISSY FMNYNSSVSF EERLNNITMW LNNSNPPVTF
ATLYWEEPDA SGHKYGPEDK ENMSRVLKKI DDLIGDLVQK LKMLGLWENL NVIITSDHGM
TQCSQDRLIN LDVCIDHSYY TLIDLSPVAA ILPKINRTEV YNRLKNCSSH MNVYLKEDIP
NRFYYQHNDR IQPIILVADE GWTIVLNESS QKLGDHGYDN SLPSMHPFLA AHGPAFHKGY
KHSTINIVDI YPMMCHILGL KPHPNNGTFG HTKCLLVDQW CINLPEAIAI VIGSLLVLTM
LTCLIIIMQN RLSVPRPFSR LQLQEDDDDP LIG
//
