V5NTD_GLOBB
ID V5NTD_GLOBB Reviewed; 54 AA.
AC P0DJJ5;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 1.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=Snake venom 5'-nucleotidase;
DE Short=5'-NT;
DE EC=3.1.3.5 {ECO:0000269|PubMed:18384831};
DE AltName: Full=Ecto-5'-nucleotidase {ECO:0000303|PubMed:18384831};
DE Flags: Fragments;
OS Gloydius blomhoffii blomhoffii (Japanese mamushi) (Agkistrodon blomhoffii
OS blomhoffii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius.
OX NCBI_TaxID=417378;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND
RP SUBUNIT.
RC TISSUE=Venom;
RX PubMed=18384831; DOI=10.1016/j.toxicon.2008.02.003;
RA Ogawa Y., Kanai-Azuma M., Akimoto Y., Kawakami H., Yanoshita R.;
RT "Exosome-like vesicles in Gloydius blomhoffii blomhoffii venom.";
RL Toxicon 51:984-993(2008).
RN [2]
RP REVIEW.
RX PubMed=20186872; DOI=10.1002/cbf.1637;
RA Dhananjaya B.L., D'Souza C.J.;
RT "The pharmacological role of nucleotidases in snake venoms.";
RL Cell Biochem. Funct. 28:171-177(2010).
CC -!- FUNCTION: Hydrolyzes nucleotides into nucleosides (PubMed:18384831).
CC Snake venom 5'-nucleotidases are widely distributed among venomous
CC snake taxa, but there is a lack of information about their biological
CC activities. They have been shown to inhibit platelet aggregation. This
CC effect may be due to the liberation of inhibitory AMP or adenosine by
CC its action on ADP released upon initiation of aggregation. Venom 5'-
CC nucleotidases are also known to synergistically act in vivo with other
CC toxins like ADPases, phospholipases, and disintegrins to exert a more
CC pronounced anti-coagulant effect. {ECO:0000269|PubMed:18384831,
CC ECO:0000305|PubMed:20186872}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside +
CC phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043; EC=3.1.3.5;
CC Evidence={ECO:0000269|PubMed:18384831};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:18384831}; Lipid-
CC anchor, GPI-anchor {ECO:0000250|UniProtKB:P21589}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:18384831}.
CC -!- PTM: Venom 5'-nucleotidases (or a part thereof) may be released into
CC the venom via exosome-like vesicles. They may be attached via a GPI
CC anchor to the membrane of these vesicles. Soluble forms of 5'-
CC nucleotidase might be released by cleavage of the ectodomain in the
CC exosome-like vesicles or venom gland cells.
CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family. {ECO:0000305}.
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DR AlphaFoldDB; P0DJJ5; -.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0106411; F:XMP 5'-nucleosidase activity; IEA:UniProtKB-EC.
DR InterPro; IPR006146; 5'-Nucleotdase_CS.
DR PROSITE; PS00785; 5_NUCLEOTIDASE_1; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; GPI-anchor; Hydrolase;
KW Lipoprotein; Membrane; Metal-binding; Nucleotide-binding; Zinc.
FT CHAIN <1..>54
FT /note="Snake venom 5'-nucleotidase"
FT /evidence="ECO:0000305|PubMed:18384831"
FT /id="PRO_0000418207"
FT BINDING 11
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A0A2I4HXH5"
FT BINDING 13
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A0A2I4HXH5"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT NON_CONS 17..18
FT /evidence="ECO:0000305|PubMed:18384831"
FT NON_CONS 25..26
FT /evidence="ECO:0000305|PubMed:18384831"
FT NON_CONS 41..42
FT /evidence="ECO:0000305|PubMed:18384831"
FT NON_TER 1
FT /evidence="ECO:0000305|PubMed:18384831"
FT NON_TER 54
FT /evidence="ECO:0000305|PubMed:18384831"
SQ SEQUENCE 54 AA; 6012 MW; 0E67C1C1A34A95C7 CRC64;
SFELTILHTN DVHARVEIIN VGSEKSDDGR QVPVVQAYAF GIQLHNYSSQ EIGK
