ENTP5_MESAU
ID ENTP5_MESAU Reviewed; 469 AA.
AC Q9QYC8; Q9QYC9;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=ER-UDPase;
DE AltName: Full=Guanosine-diphosphatase ENTPD5;
DE Short=GDPase ENTPD5;
DE AltName: Full=Nucleoside diphosphatase;
DE AltName: Full=Proto-oncogene cph {ECO:0000303|PubMed:9989819};
DE AltName: Full=Uridine-diphosphatase ENTPD5;
DE Short=UDPase ENTPD5;
DE Flags: Precursor;
GN Name=ENTPD5; Synonyms=CD39L4, CPH;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND MISCELLANEOUS.
RX PubMed=9989819; DOI=10.1038/sj.onc.1202324;
RA Velasco J.A., Avila M.A., Notario V.;
RT "The product of the cph oncogene is a truncated, nucleotide-binding protein
RT that enhances cellular survival to stress.";
RL Oncogene 18:689-701(1999).
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 -!- TISSUE SPECIFICITY: Expressed in fetal cells and most adult tissues.
CC {ECO:0000269|PubMed:9989819}.
CC -!- PTM: N-glycosylated; high-mannose type. {ECO:0000250|UniProtKB:Q9WUZ9}.
CC -!- MISCELLANEOUS: ENTPD5 has transforming capacity and tumorigenic
CC potential. {ECO:0000305|PubMed:9989819}.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
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DR EMBL; AF084568; AAF22931.1; ALT_TERM; mRNA.
DR EMBL; AF084569; AAF22932.1; -; mRNA.
DR RefSeq; NP_001268880.1; NM_001281951.1.
DR AlphaFoldDB; Q9QYC8; -.
DR SMR; Q9QYC8; -.
DR STRING; 10036.XP_005086446.1; -.
DR GeneID; 101836947; -.
DR CTD; 957; -.
DR eggNOG; KOG1385; Eukaryota.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000189706; 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 2: Evidence at transcript level;
KW Calcium; Disulfide bond; Endoplasmic reticulum; Glycoprotein; Hydrolase;
KW Magnesium; Proto-oncogene; Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..469
FT /note="Ectonucleoside triphosphate diphosphohydrolase 5"
FT /id="PRO_0000019909"
FT ACT_SITE 172
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9WUZ9"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 272..303
FT /evidence="ECO:0000250"
FT DISULFID 363..377
FT /evidence="ECO:0000250"
SQ SEQUENCE 469 AA; 52126 MW; 03D8A23E0C73474B CRC64;
MATPWGAVFF LLMIACAGST VFYREQQTWF EGVFLSSMCP ANVSASTFYG IMFDAGSTGT
RIHVYTFVQK AAGQLPFLEG EIFDSVKPGL SAFADQPKQG AQTVHALLEV AKDSIPRSHW
KRTPVVLKAT AGLRLLPEQK AQALLLEVEE IFKMSPFLVP DDSVSIMDGS YEGILAWVTV
NFLTGQLHGH SQETMGTLDL GGASTQITFL PQFSKTLEQT PRDYLTSFEM FNSTFKLYTH
SYLGFGLKAA RLATLGALET EGTDGHTFRS ACLPRWLEAE WIFGGVKYQY GGNQEGEMGF
EPCYAEVLRV VQGKLHQPEE IRGSSFYAFS YYYDRAADTH LIDYEKGGVL KVEDFERKAR
EVCDNLESFT SGSPFLCMDL SYITALLKDG FGFADGTLLQ LTKKVNNIET GWPGGHLSPA
AVSGHLQLRL SVPLETCTSE LLFTGRRGLG HFLQLRWRKP GLKPIDWLY
