ID   Q5ZKC4_CHICK            Unreviewed;       331 AA.
AC   Q5ZKC4;
DT   23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, entry version 90.
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=RCJMB04_11m23 {ECO:0000313|EMBL:CAG31819.1};
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031 {ECO:0000313|EMBL:CAG31819.1};
RN   [1] {ECO:0000313|EMBL:CAG31819.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CB {ECO:0000313|EMBL:CAG31819.1};
RC   TISSUE=Bursa {ECO:0000313|EMBL:CAG31819.1};
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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}.
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; AJ720160; CAG31819.1; -; mRNA.
DR   AlphaFoldDB; Q5ZKC4; -.
DR   VEuPathDB; HostDB:geneid_422055; -.
DR   PhylomeDB; Q5ZKC4; -.
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   2: Evidence at transcript level;
KW   Blood coagulation {ECO:0000256|ARBA:ARBA00023084};
KW   Hemostasis {ECO:0000256|ARBA:ARBA00022696};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..331
FT                   /note="bis(5'-adenosyl)-triphosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004265220"
SQ   SEQUENCE   331 AA;  38040 MW;  834305786546C7C7 CRC64;
     MNLQIVLFVS AILSCCARSG SSAPRLLLVS FDGFRADYLE TYSLPHLQEL IEDGVLVKQV
     TNAFITKTFP NHYSIVTGLY EESHGIVAND MYDPDAKKKF SQFNDSDPFW WNEAVPIWVT
     NQQQRNGTSA AAMWPGTDVR INNTTPQFFM KYNFSVTFEE RVEKIIRWLN SSDPVVNFAT
     LYWEEPDASG HKYGPDDTEN MRRVLEQVDQ HVGFLTGKLK ASGLWDTINV IITSDHGMAQ
     GSPKKLIVLD NCIGRGNYTL IDRSPVAAVL PKNNKEYVYN LLKQCDDRHM KVYLKEEIPD
     RFHYRHNKRI QPIILIADEG WTMYRMRPSQ S
//