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Venom phosphodiesterase 2 (Ectonucleotide pyrophosphatase/phosphodiesterase family member 3) (PDE-3) [Includes: Alkaline phosphodiesterase I (PDE) (EC 3.1.4.1); Nucleotide pyrophosphatase (NPPase) (EC 3.6.1.9) (Nucleotide diphosphatase)]

 PDE2_CROAD              Reviewed;         810 AA.
J3SBP3;
19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
31-OCT-2012, sequence version 1.
22-NOV-2017, entry version 23.
RecName: Full=Venom phosphodiesterase 2;
AltName: Full=Ectonucleotide pyrophosphatase/phosphodiesterase family member 3;
Short=PDE-3;
Includes:
RecName: Full=Alkaline phosphodiesterase I;
Short=PDE;
EC=3.1.4.1 {ECO:0000250|UniProtKB:P06802};
Includes:
RecName: Full=Nucleotide pyrophosphatase;
Short=NPPase;
EC=3.6.1.9 {ECO:0000250|UniProtKB:P06802};
AltName: Full=Nucleotide diphosphatase {ECO:0000305};
Flags: Precursor;
Crotalus adamanteus (Eastern diamondback rattlesnake).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
NCBI_TaxID=8729;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Venom gland;
Rokyta D.R., Lemmon A.R., Margres M.J., Aronow K.;
"The venom-gland transcriptome of the eastern diamondback rattlesnake
(Crotalus adamanteus).";
BMC Genomics 13:312-312(2012).
[2]
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Venom;
PubMed=24231107; DOI=10.1016/j.jprot.2013.11.001;
Margres M.J., McGivern J.J., Wray K.P., Seavy M., Calvin K.,
Rokyta D.R.;
"Linking the transcriptome and proteome to characterize the venom of
the eastern diamondback rattlesnake (Crotalus adamanteus).";
J. Proteomics 96:145-158(2014).
-!- FUNCTION: Exhibits nuclease activity as well as pyrophosphatase
and phosphatase activities, preferentially hydrolyzing nucleoside
5'-triphosphates over nucleoside 5'-diphosphates. Is inactive upon
nucleoside 5'-monophosphates. Also inhibits platelet aggregation
induced by ADP, but not by thrombin. Polyclonal antibodies raised
against this do not abolish the lethal activity of the venom.
{ECO:0000250|UniProtKB:P06802}.
-!- CATALYTIC ACTIVITY: Hydrolytically removes 5'-nucleotides
successively from the 3'-hydroxy termini of 3'-hydroxy-terminated
oligonucleotides. {ECO:0000250|UniProtKB:P06802}.
-!- CATALYTIC ACTIVITY: A nucleoside triphosphate + H(2)O = a
nucleotide + diphosphate. {ECO:0000250|UniProtKB:P06802}.
-!- COFACTOR:
Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
Evidence={ECO:0000305};
Note=Binds 2 divalent metal cations per subunit. {ECO:0000305};
-!- ENZYME REGULATION: Inhibited by EDTA and dithiothreitol, but not
by PMSF. {ECO:0000250}.
-!- SUBUNIT: Dimer; not covalently-linked. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed by venom gland.
-!- SIMILARITY: Belongs to the nucleotide
pyrophosphatase/phosphodiesterase family. {ECO:0000305}.
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EMBL; JU173674; AFJ49200.1; -; mRNA.
SMR; J3SBP3; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0035529; F:NADH pyrophosphatase activity; IEA:UniProtKB-EC.
GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
GO; GO:0004528; F:phosphodiesterase I activity; IEA:UniProtKB-EC.
GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
GO; GO:0006955; P:immune response; IEA:InterPro.
Gene3D; 3.40.720.10; -; 1.
InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
InterPro; IPR017850; Alkaline_phosphatase_core_sf.
InterPro; IPR001604; DNA/RNA_non-sp_Endonuclease.
InterPro; IPR020821; Extracellular_endonuc_su_A.
InterPro; IPR002591; Phosphodiest/P_Trfase.
InterPro; IPR036024; Somatomedin_B-like_dom_sf.
InterPro; IPR001212; Somatomedin_B_dom.
Pfam; PF01223; Endonuclease_NS; 1.
Pfam; PF01663; Phosphodiest; 1.
Pfam; PF01033; Somatomedin_B; 1.
SMART; SM00892; Endonuclease_NS; 1.
SMART; SM00477; NUC; 1.
SMART; SM00201; SO; 1.
SUPFAM; SSF53649; SSF53649; 1.
SUPFAM; SSF90188; SSF90188; 1.
PROSITE; PS00524; SMB_1; 1.
PROSITE; PS50958; SMB_2; 1.
1: Evidence at protein level;
Disulfide bond; Glycoprotein; Hemostasis impairing toxin; Hydrolase;
Metal-binding; Platelet aggregation inhibiting toxin; Secreted;
Signal; Toxin.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 810 Venom phosphodiesterase 2.
/FTId=PRO_0000425620.
DOMAIN 33 77 SMB. {ECO:0000255|PROSITE-
ProRule:PRU00350}.
REGION 79 448 Phosphodiesterase. {ECO:0000250}.
REGION 540 809 Nuclease. {ECO:0000250}.
ACT_SITE 144 144 AMP-threonine intermediate.
{ECO:0000250}.
METAL 106 106 Divalent metal cation 2. {ECO:0000250}.
METAL 264 264 Divalent metal cation 1. {ECO:0000250}.
METAL 268 268 Divalent metal cation 1. {ECO:0000250}.
METAL 311 311 Divalent metal cation 2. {ECO:0000250}.
METAL 312 312 Divalent metal cation 2. {ECO:0000250}.
METAL 421 421 Divalent metal cation 1. {ECO:0000250}.
CARBOHYD 175 175 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 218 218 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 229 229 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 364 364 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 471 471 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 553 553 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 633 633 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 704 704 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 37 54 Alternate. {ECO:0000255|PROSITE-
ProRule:PRU00350}.
DISULFID 37 42 Alternate. {ECO:0000255|PROSITE-
ProRule:PRU00350}.
DISULFID 42 72 Alternate. {ECO:0000255|PROSITE-
ProRule:PRU00350}.
DISULFID 52 65 Alternate. {ECO:0000255|PROSITE-
ProRule:PRU00350}.
DISULFID 52 54 Alternate. {ECO:0000255|PROSITE-
ProRule:PRU00350}.
DISULFID 58 64 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 65 72 Alternate. {ECO:0000255|PROSITE-
ProRule:PRU00350}.
SEQUENCE 810 AA; 91752 MW; 2C72A91DB316A306 CRC64;
MIQQKVLFIS LVAVTLGLGL GLGLKESVQP QAQSWSCSKL RCGEKRIANV LCSCSDDCLE
KKDCCTDYKS ICKGETSWLK DKCASSGATQ CPAGFEQSPL ILFSMDGFRA GYLENWDSLM
PNINKLKTCG THAKYMRAVY PTKTFVNHYT IATGLYPESH GIIDNNIYDV NLNLNFSLSS
STARNPAWWG GQPIWHTATY QGLKAATYFW PGSEVKINGS YPTIFKNYNK SIPFEARVTE
VLKWLDLPKA KRPDFLTLYI EEPDTTGHKY GPVSGEIIKA LQMADRTLGM LMEGLKQRNL
HNCVNLILLA DHGMEEISCD RLEYMANYFN NVDFFMYEGP APRIRSKNVP KDFYTFDSEG
IVKNLTCRKP KQYFKAYLSK DLPKRLHYAN NIRIDKVNLM VDQQWMAVRD KKFTRCKGGT
HGYDNEFKSM QAIFLAHGPG FNEKNEVTSF ENIEVYNLMC DLLKLKPAPN NGTHGSLNHL
LKNPFYTPSP AKEQSSPLSC PFGPVPSPDV SGCKCSSITE LEKVNQRLNL NNQAKTESEA
HNLPYGRPQV LQNHSKYCLL HQAKYISAYS QDILMPLWSS YTIYRSTSTS VPPSASDCLR
LDVRIPAAQS QTCSNYQPDL TITPGFLYPP NFNSSNFEQY DALITSNIVP MFKGFTRLWN
YFHTTLIPKY ARERNGLNVI SGPIFDYNYD GHFDSYDTIK QHVNNTKIPI PTHYFVVLTS
CENQINTPLN CLGPLKVLSF ILPHRPDNSE SCADTSPENL WVEERIQIHT ARVRDVELLT
GLNFYSGLKQ PLPETLQLKT FLPIFVNPVN


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