ENPP4_PONAB
ID ENPP4_PONAB Reviewed; 452 AA.
AC Q5RAC0;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 83.
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;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR859098; CAH91290.1; -; mRNA.
DR RefSeq; NP_001125764.1; NM_001132292.1.
DR AlphaFoldDB; Q5RAC0; -.
DR SMR; Q5RAC0; -.
DR STRING; 9601.ENSPPYP00000018644; -.
DR Ensembl; ENSPPYT00000019383; ENSPPYP00000018644; ENSPPYG00000016666.
DR GeneID; 100172690; -.
DR KEGG; pon:100172690; -.
DR CTD; 22875; -.
DR eggNOG; KOG2645; Eukaryota.
DR InParanoid; Q5RAC0; -.
DR Proteomes; UP000001595; Chromosome 6.
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:Ensembl.
DR GO; GO:0046130; P:purine ribonucleoside catabolic process; IEA:Ensembl.
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..15
FT /evidence="ECO:0000255"
FT CHAIN 16..452
FT /note="Bis(5'-adenosyl)-triphosphatase ENPP4"
FT /id="PRO_0000324797"
FT TOPO_DOM 16..406
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..452
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 70
FT /note="AMP-threonine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 34
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
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 237
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 335
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 254..287
FT /evidence="ECO:0000250"
FT DISULFID 393..400
FT /evidence="ECO:0000250"
SQ SEQUENCE 452 AA; 51561 MW; 8996A3F1AAE1CCCA 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 QKCDHGYDNS LPSMHPFLAA HGPAFHKGYK
HSTINIVDIY PMMCHILGLK PHPNNGTFGH TKCLLVDQWC INLPEAIAIV IGSLLVLTML
TCLIIIMQNR LSVPRPFSRL QLQEDDDDPL IG
