ENTP5_AILME
ID ENTP5_AILME Reviewed; 433 AA.
AC D2GZV9;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 03-AUG-2022, entry version 41.
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; ORFNames=PANDA_002660;
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
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; GL192398; EFB27007.1; -; Genomic_DNA.
DR AlphaFoldDB; D2GZV9; -.
DR SMR; D2GZV9; -.
DR STRING; 9646.ENSAMEP00000019291; -.
DR eggNOG; KOG1385; Eukaryota.
DR InParanoid; D2GZV9; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
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..433
FT /note="Ectonucleoside triphosphate diphosphohydrolase 5"
FT /id="PRO_0000404540"
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..308
FT /evidence="ECO:0000250"
FT DISULFID 368..382
FT /evidence="ECO:0000250"
SQ SEQUENCE 433 AA; 48066 MW; 0715F6B3424FA18F CRC64;
MATTWGAAFF MLVASCVCST VFHRDQQTWF EGVFLSSMCP INVSASTLYG IMFDAGSTGT
RIHIYTFVQK IPGQLPILEG EIFESVKPGL SAFVDQPKQG AETVEELLEV AKDSVPRSHW
KRTPVVLKAT AGLRLLPEQK AEALLFEVRE IFRKSPFLVP DDSVSIMDGS YEGILAWVTV
NFLTGQLHGH SQKTVGTLDL GGASTQITFL PQFEKTLEQT PRGYLTSFEM FNSTYKLYTH
SYLGFGLKAA RLATLGALET EGIDGHTFRS ACLPRWLEAE WIFGGVKYQY GGNKEGNEGS
GEVGFEPCYA EVLRVVQGKL HQPDEVRKSS FYAFSYYYDR AADTDMIDYE TGGVLKVEDF
ERKAREVCDN LEKFTSGSPF LCMDLSYITA LLKDGFGFAD STILQLSKKV NNIETGWALG
ATFHLLQSLG ISH
