ENPP4_DANRE
ID ENPP4_DANRE Reviewed; 459 AA.
AC Q566N0;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Bis(5'-adenosyl)-triphosphatase enpp4;
DE EC=3.6.1.29;
DE AltName: Full=AP3A hydrolase;
DE Short=AP3Aase;
DE AltName: Full=Ectonucleotide pyrophosphatase/phosphodiesterase family member 4;
DE Short=E-NPP 4;
DE Short=NPP-4;
DE Flags: Precursor;
GN Name=enpp4; ORFNames=zgc:113299;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2005) 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 (By similarity). {ECO:0000250}.
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;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein.
CC -!- SIMILARITY: Belongs to the nucleotide pyrophosphatase/phosphodiesterase
CC family. {ECO:0000305}.
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DR EMBL; BC093443; AAH93443.1; -; mRNA.
DR RefSeq; NP_001017887.1; NM_001017887.1.
DR AlphaFoldDB; Q566N0; -.
DR SMR; Q566N0; -.
DR STRING; 7955.ENSDARP00000076322; -.
DR PaxDb; Q566N0; -.
DR Ensembl; ENSDART00000004043; ENSDARP00000004660; ENSDARG00000006877.
DR Ensembl; ENSDART00000179751; ENSDARP00000147669; ENSDARG00000110396.
DR GeneID; 550586; -.
DR KEGG; dre:550586; -.
DR CTD; 22875; -.
DR ZFIN; ZDB-GENE-050417-444; enpp4.
DR eggNOG; KOG2645; Eukaryota.
DR GeneTree; ENSGT00940000158831; -.
DR HOGENOM; CLU_017594_1_2_1; -.
DR InParanoid; Q566N0; -.
DR OMA; FTCIIII; -.
DR OrthoDB; 999163at2759; -.
DR PhylomeDB; Q566N0; -.
DR TreeFam; TF330032; -.
DR Reactome; R-DRE-6798695; Neutrophil degranulation.
DR PRO; PR:Q566N0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 17.
DR Bgee; ENSDARG00000006877; Expressed in blastula and 17 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR GO; GO:0030194; P:positive regulation of blood coagulation; IEA:InterPro.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR029879; ENPP4.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR PANTHER; PTHR10151:SF79; PTHR10151:SF79; 1.
DR Pfam; PF01663; Phosphodiest; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
PE 2: Evidence at transcript level;
KW Blood coagulation; Cell membrane; Disulfide bond; Glycoprotein; Hemostasis;
KW Hydrolase; Membrane; Metal-binding; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Zinc.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..459
FT /note="Bis(5'-adenosyl)-triphosphatase enpp4"
FT /id="PRO_0000324798"
FT TOPO_DOM 20..408
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 430..459
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 76
FT /note="AMP-threonine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 40
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 242
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 340
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 258..291
FT /evidence="ECO:0000250"
FT DISULFID 398..405
FT /evidence="ECO:0000250"
SQ SEQUENCE 459 AA; 51603 MW; 59CE6D7B9B23C011 CRC64;
MQISAYLCAL IACCGLTLSA PTANNKSSSE APPLLLVSFD GFRADYLNKY SFPNLEKFFS
DGVLVHELTN VFTTKTFPNH YSLVTGLYAE SHGMLASIMY DPVAKKHFSI KNDSDPFWWD
EATPIWVSVE ESGYHAASAM WPGSDVNIQN HTLKYTFKYD SRVSFKERLG NITQWMTTDK
SLKFASLYWE EPDFSGHTYG PDNTTEMARV LKEVDGHVGY LMEELDRMEL WGKINVIITS
DHGMAQCSEE RIIRLDDCVS PSSYTLVDLT PVAAIIPLED KTTVYNNLSS CHVHLKAYMK
NDVPDRLHYK NNERIQPIIL VADEGWTIVK NGRLPRLGDH GYDNTLPSMH PFLAAHGPAF
RKGYKMSSFN SVDLYPLMCH LIGIPPKANN GSFAHVRCTL VNEQCGELAL AVGLVMGVLI
ILTTFTCLFK LMKNRNVSSP RPFARLELDD DGDDEPLLE
