ENTP5_BOVIN
ID ENTP5_BOVIN Reviewed; 432 AA.
AC E1BPW0;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Ectonucleoside triphosphate diphosphohydrolase 5 {ECO:0000250|UniProtKB:Q9WUZ9};
DE Short=NTPDase 5;
DE EC=3.6.1.6 {ECO:0000250|UniProtKB:Q9WUZ9};
DE AltName: Full=Guanosine-diphosphatase ENTPD5;
DE Short=GDPase ENTPD5;
DE AltName: Full=Uridine-diphosphatase ENTPD5;
DE Short=UDPase ENTPD5;
DE Flags: Precursor;
GN Name=ENTPD5;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
CC -!- FUNCTION: Hydrolyzes nucleoside diphosphates with a preference for GDP,
CC IDP and UDP compared to ADP and CDP (By similarity). In the lumen of
CC the endoplasmic reticulum, hydrolyzes UDP that acts as an end-product
CC feedback inhibitor of the UDP-Glc:glycoprotein glucosyltransferases.
CC UMP can be transported back by an UDP-sugar antiporter to the cytosol
CC where it is consumed to regenerate UDP-glucose. Therefore, it
CC positively regulates protein reglucosylation by clearing UDP from the
CC ER lumen and by promoting the regeneration of UDP-glucose. Protein
CC reglucosylation is essential to proper glycoprotein folding and quality
CC control in the ER (By similarity). {ECO:0000250|UniProtKB:O75356,
CC ECO:0000250|UniProtKB:Q9WUZ9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-diphosphate + H2O = a ribonucleoside 5'-
CC phosphate + H(+) + phosphate; Xref=Rhea:RHEA:36799,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:58043; EC=3.6.1.6;
CC Evidence={ECO:0000250|UniProtKB:O75356};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36800;
CC Evidence={ECO:0000250|UniProtKB:O75356};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP + H2O = GMP + H(+) + phosphate; Xref=Rhea:RHEA:22156,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58115, ChEBI:CHEBI:58189; EC=3.6.1.6;
CC Evidence={ECO:0000250|UniProtKB:O75356};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22157;
CC Evidence={ECO:0000250|UniProtKB:O75356};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + UDP = H(+) + phosphate + UMP; Xref=Rhea:RHEA:64876,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57865, ChEBI:CHEBI:58223; EC=3.6.1.6;
CC Evidence={ECO:0000250|UniProtKB:O75356};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64877;
CC Evidence={ECO:0000250|UniProtKB:O75356};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + IDP = H(+) + IMP + phosphate; Xref=Rhea:RHEA:35207,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58053, ChEBI:CHEBI:58280; EC=3.6.1.6;
CC Evidence={ECO:0000250|UniProtKB:O75356};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35208;
CC Evidence={ECO:0000250|UniProtKB:O75356};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CDP + H2O = CMP + H(+) + phosphate; Xref=Rhea:RHEA:64880,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58069, ChEBI:CHEBI:60377; EC=3.6.1.6;
CC Evidence={ECO:0000250|UniProtKB:O75356};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64881;
CC Evidence={ECO:0000250|UniProtKB:O75356};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP + H2O = AMP + H(+) + phosphate; Xref=Rhea:RHEA:61436,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=3.6.1.6;
CC Evidence={ECO:0000250|UniProtKB:O75356};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61437;
CC Evidence={ECO:0000250|UniProtKB:O75356};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:O75356};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O75356};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q9WUZ9}.
CC -!- SUBUNIT: Monomer; active form. Homodimer; disulfide-linked. Homodimers
CC are enzymatically inactive. {ECO:0000250|UniProtKB:O75356}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q9WUZ9}. Secreted
CC {ECO:0000250|UniProtKB:O75356}.
CC -!- PTM: N-glycosylated; high-mannose type. {ECO:0000250|UniProtKB:Q9WUZ9}.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
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DR EMBL; AAFC03056279; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; E1BPW0; -.
DR SMR; E1BPW0; -.
DR STRING; 9913.ENSBTAP00000027098; -.
DR PaxDb; E1BPW0; -.
DR PeptideAtlas; E1BPW0; -.
DR eggNOG; KOG1385; Eukaryota.
DR HOGENOM; CLU_010246_0_2_1; -.
DR InParanoid; E1BPW0; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043262; F:adenosine-diphosphatase activity; IEA:RHEA.
DR GO; GO:0036384; F:cytidine-diphosphatase activity; IEA:RHEA.
DR GO; GO:0004382; F:guanosine-diphosphatase activity; ISS:UniProtKB.
DR GO; GO:1990003; F:inosine-diphosphatase activity; IEA:RHEA.
DR GO; GO:0045134; F:uridine-diphosphatase activity; ISS:UniProtKB.
DR GO; GO:0051084; P:'de novo' post-translational protein folding; ISS:UniProtKB.
DR GO; GO:0006487; P:protein N-linked glycosylation; ISS:UniProtKB.
DR GO; GO:0006256; P:UDP catabolic process; ISS:UniProtKB.
DR GO; GO:0006011; P:UDP-glucose metabolic process; ISS:UniProtKB.
DR InterPro; IPR000407; GDA1_CD39_NTPase.
DR PANTHER; PTHR11782; PTHR11782; 1.
DR Pfam; PF01150; GDA1_CD39; 1.
DR PROSITE; PS01238; GDA1_CD39_NTPASE; 1.
PE 3: Inferred from homology;
KW Calcium; Disulfide bond; Endoplasmic reticulum; Glycoprotein; Hydrolase;
KW Magnesium; Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..432
FT /note="Ectonucleoside triphosphate diphosphohydrolase 5"
FT /id="PRO_0000404541"
FT ACT_SITE 175
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9WUZ9"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 275..307
FT /evidence="ECO:0000250"
FT DISULFID 367..381
FT /evidence="ECO:0000250"
SQ SEQUENCE 432 AA; 47888 MW; 524FB2B1BBAD88DF CRC64;
MALYQGAAFF MLVASCVCST VFHREQQTWF EGVFLSSMCP VNVSAGTLYG IMFDAGSTGT
RIHVYTFVQK VPDNTGQLPV LEGEIFDSVK PGLSAFVDQP KQGAETVQEL LEVAKDSIPP
SHWKRTPVVL KATAGLRLLP EEKAEALLFE VKEIFKKSPF LVPDDSVSIM DGSYEGILAW
VTVNFLTGQL HGHNQETVGT LDLGGASTQI TFLPQFEKTL EQTPRDYLTS FEMFNSTYKL
YTHSYLGFGL KAARLATLGA LETAGIDGYT FRSACLPRWL EAEWIFGGVK YQYGGNQEAG
EVGFEPCYAE VLRVVQGKLH QPDEVQRGSF YAFSYYYDRA VDTDMIDYEK GGVLKVEDFE
RKAREVCDNL ENFTSGSPFL CMDLSYITAL LKDGFGFASS TVLQLTKKVN NIETGWALGA
TFHLLQSLGI SH
