ID A0A093NQ20_PYGAD Unreviewed; 452 AA.
AC A0A093NQ20;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
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 ORFNames=AS28_01579 {ECO:0000313|EMBL:KFW64080.1};
OS Pygoscelis adeliae (Adelie penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae; Pygoscelis.
OX NCBI_TaxID=9238 {ECO:0000313|EMBL:KFW64080.1, ECO:0000313|Proteomes:UP000054081};
RN [1] {ECO:0000313|EMBL:KFW64080.1, ECO:0000313|Proteomes:UP000054081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS28 {ECO:0000313|EMBL:KFW64080.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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; KL224801; KFW64080.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093NQ20; -.
DR STRING; 9238.A0A093NQ20; -.
DR Proteomes; UP000054081; Unassembled WGS sequence.
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 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:UP000054081};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..452
FT /note="bis(5'-adenosyl)-triphosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001889073"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 452 AA; 51069 MW; 772226B3AE48C39F CRC64;
MNSMLTLFFS GVVACCAHST GDSVSRLLLV SFDGFRADYL ETYKLPHLQE FIEDGVLVKQ
VTNAFITKTF PNHYTIVTGL YEESHGIVAN DMYDADAKKK FSQFNDSDPF WWNEAVPIWV
TNQQQGNGAS AAAMWPGTDV KINDTTPHFF MKYNFSVTFE ERVEKIVAWL NSSNPVVSFA
TLYWEEPDAS GHKYGPDDTE NMRKVLEEVD NHIGFLMNKL KALGLWDTIN IIITSDHGMA
ACSAKKLIIL DGCIGRNNYT LIDKSPVAAV LPRQNKRDVY NLLKKCSSHM KIYLKEEIPD
RFHYRHNKRI QPIILVADEG WTIVQNESLS KLGDHGYDNA LPSMHPFLAA RGPAFHRGYK
QSTMNNVDIY PMMCHILGLT PQPHNGTFSN TKCLLADQWC INLPEAIGIV VGAFMILTTF
TCIIIISKNR VAPPRPFSRL QLQYDDDDPL IG
//
