ENTP5_RAT
ID ENTP5_RAT Reviewed; 427 AA.
AC Q6P6S9;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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; BC062044; AAH62044.1; -; mRNA.
DR RefSeq; NP_955426.1; NM_199394.1.
DR AlphaFoldDB; Q6P6S9; -.
DR SMR; Q6P6S9; -.
DR STRING; 10116.ENSRNOP00000041026; -.
DR GlyGen; Q6P6S9; 1 site.
DR PaxDb; Q6P6S9; -.
DR PRIDE; Q6P6S9; -.
DR GeneID; 314312; -.
DR KEGG; rno:314312; -.
DR UCSC; RGD:735219; rat.
DR CTD; 957; -.
DR RGD; 735219; Entpd5.
DR eggNOG; KOG1385; Eukaryota.
DR InParanoid; Q6P6S9; -.
DR OrthoDB; 1337265at2759; -.
DR PhylomeDB; Q6P6S9; -.
DR Reactome; R-RNO-8850843; Phosphate bond hydrolysis by NTPDase proteins.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q6P6S9; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0043262; F:adenosine-diphosphatase activity; ISO:RGD.
DR GO; GO:0036384; F:cytidine-diphosphatase activity; ISO:RGD.
DR GO; GO:0004382; F:guanosine-diphosphatase activity; ISS:UniProtKB.
DR GO; GO:1990003; F:inosine-diphosphatase activity; ISO:RGD.
DR GO; GO:0017110; F:nucleoside-diphosphatase activity; ISO:RGD.
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:0046034; P:ATP metabolic process; ISO:RGD.
DR GO; GO:0009134; P:nucleoside diphosphate catabolic process; IBA:GO_Central.
DR GO; GO:0045821; P:positive regulation of glycolytic process; ISO:RGD.
DR GO; GO:0006487; P:protein N-linked glycosylation; ISS:UniProtKB.
DR GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; ISO:RGD.
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; Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..427
FT /note="Ectonucleoside triphosphate diphosphohydrolase 5"
FT /id="PRO_0000404542"
FT ACT_SITE 171
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9WUZ9"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 271..302
FT /evidence="ECO:0000250"
FT DISULFID 362..376
FT /evidence="ECO:0000250"
SQ SEQUENCE 427 AA; 47373 MW; 6CBBC44D96A60211 CRC64;
MATSWASVFL LIIAYVGGTV FYREQQTWFE GVFLSSMCPV NVSAGTFYGI MFDAGSTGTR
IHVYTFVQRT SGQLPFLEGE IFDSVKPGLS AFVDQPKQGA ETVQELLEVA KDSIPRSHWK
RTPVVLKATA GLRLLPEQKA QTLLLEVEEI FKNSPFLVPD DSVSIMDGSY EGILAWVTVN
FLTGQLHGRG QETVGTLDLG GASTQITFLP QLEKTLEQTP KGYLASFEMF NSTFKLYTHS
YLGFGLKAAR LATLGALEAE GTDGHTFRSA CLPRWLEAEW IFGGVKYQYG GNQEGEMGFE
PCYAEVRRVV QGKLHQPEEI RGSSFYAFSY YYDRAAETHL IDYEKGGVLK VEDFERKARE
VCDNLESFSS GSPFLCMDLS YITALLKDGF GFEDGTLLQL TKKVNNIETG WALGATFHLL
QSLGITS
