ID V8NF30_OPHHA Unreviewed; 461 AA.
AC V8NF30;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
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|EMBL:ETE60172.1};
GN ORFNames=L345_14083 {ECO:0000313|EMBL:ETE60172.1};
OS Ophiophagus hannah (King cobra) (Naja hannah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE60172.1, ECO:0000313|Proteomes:UP000018936};
RN [1] {ECO:0000313|EMBL:ETE60172.1, ECO:0000313|Proteomes:UP000018936}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Blood {ECO:0000313|EMBL:ETE60172.1};
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETE60172.1}.
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DR EMBL; AZIM01004888; ETE60172.1; -; Genomic_DNA.
DR AlphaFoldDB; V8NF30; -.
DR Proteomes; UP000018936; 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:0090729; F:toxin activity; IEA:UniProtKB-KW.
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:UP000018936};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..461
FT /note="bis(5'-adenosyl)-triphosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004770857"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 461 AA; 52944 MW; FD91B68F9B342B72 CRC64;
MHVEILSRML FLVIVLLFNG IISYSDGKSV SKSVPRLLLV SFDGFRADYL KKYELPHLQD
FIKAGVLVEH VTNAFITKTF PNHYSIVTGL YEESHGIVAN EMFDNDTKKK FSQFNDTDSF
WWDEAIPIWV SNEWQENKTS ASAMWPGTDV KIHDTLPHFF MKYNYSVSFS ERVEKIIEWL
NSSNPLVTFA TLYWEEPDAS GHKYGPEDTK NMTKVLHEVD KHIGLLVEKL KVSKLWEEIN
VIITSDHGMA QCSQERLIKL DRCVNSSNYK LIDRSPVAAI LPNNVTHVYD LMKNCSPNMK
VYLKEEIPER YHYHHNKRIQ PIILVADEGW TIVQNGSLPR LGDHGYDDTL PSMQPFLAAH
GPAFRKNYRL NSIRTIDIYP MMCHILGLKS QPNNGTLSNS KCLLVDQWCI NVPEAIGIVI
GVFMILTILM CLIIITKNRT PPLRPFSRLQ LQEDDDDPLI G
//
