PDE2_CROAD
ID PDE2_CROAD Reviewed; 810 AA.
AC J3SBP3;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Venom phosphodiesterase 2;
DE Short=PDE;
DE EC=3.6.1.- {ECO:0000250|UniProtKB:W8E7D1};
DE Flags: Precursor;
OS Crotalus adamanteus (Eastern diamondback rattlesnake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=8729;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Rokyta D.R., Lemmon A.R., Margres M.J., Aronow K.;
RT "The venom-gland transcriptome of the eastern diamondback rattlesnake
RT (Crotalus adamanteus).";
RL BMC Genomics 13:312-312(2012).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=24231107; DOI=10.1016/j.jprot.2013.11.001;
RA Margres M.J., McGivern J.J., Wray K.P., Seavy M., Calvin K., Rokyta D.R.;
RT "Linking the transcriptome and proteome to characterize the venom of the
RT eastern diamondback rattlesnake (Crotalus adamanteus).";
RL J. Proteomics 96:145-158(2014).
CC -!- FUNCTION: Hydrolyzes ADP with high activity. Shows weak or no activity
CC on 5'-AMP, 5'-GMP, 3'-AMP, ATP, cAMP, and cGMP. Is devoid of
CC monophosphatase and proteinase activities. Dose-dependently inhibits
CC platelet aggregation induced by ADP (IC(50)=0.99 uM) and collagen
CC (IC(50)=1.4 uM). {ECO:0000250|UniProtKB:W8E7D1}.
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;
CC Evidence={ECO:0000250|UniProtKB:W8E7D1};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:W8E7D1};
CC Note=Binds 2 divalent metal cations per subunit.
CC {ECO:0000250|UniProtKB:W8E7D1};
CC -!- SUBUNIT: Monomer cleaved in two subunits; disulfide-linked. Is
CC synthesized as a single-chain protein and is subsequently cleaved to
CC form a two-subunit protein held together with disulfide bonds.
CC {ECO:0000250|UniProtKB:W8E7D1}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24231107}.
CC -!- TISSUE SPECIFICITY: Expressed by venom gland.
CC {ECO:0000305|PubMed:24231107}.
CC -!- SIMILARITY: Belongs to the nucleotide pyrophosphatase/phosphodiesterase
CC family. {ECO:0000305}.
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DR EMBL; JU173674; AFJ49200.1; -; mRNA.
DR AlphaFoldDB; J3SBP3; -.
DR SMR; J3SBP3; -.
DR PRIDE; J3SBP3; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043262; F:adenosine-diphosphatase activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.570.10; -; 1.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR001604; DNA/RNA_non-sp_Endonuclease.
DR InterPro; IPR044929; DNA/RNA_non-sp_Endonuclease_sf.
DR InterPro; IPR020821; Extracellular_endonuc_su_A.
DR InterPro; IPR044925; His-Me_finger_sf.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR InterPro; IPR036024; Somatomedin_B-like_dom_sf.
DR InterPro; IPR001212; Somatomedin_B_dom.
DR Pfam; PF01223; Endonuclease_NS; 1.
DR Pfam; PF01663; Phosphodiest; 1.
DR Pfam; PF01033; Somatomedin_B; 1.
DR SMART; SM00892; Endonuclease_NS; 1.
DR SMART; SM00477; NUC; 1.
DR SMART; SM00201; SO; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
DR SUPFAM; SSF54060; SSF54060; 1.
DR SUPFAM; SSF90188; SSF90188; 1.
DR PROSITE; PS00524; SMB_1; 1.
DR PROSITE; PS50958; SMB_2; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Hemostasis impairing toxin; Hydrolase;
KW Metal-binding; Platelet aggregation inhibiting toxin; Secreted; Signal;
KW Toxin.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..810
FT /note="Venom phosphodiesterase 2"
FT /id="PRO_0000425620"
FT DOMAIN 33..77
FT /note="SMB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT ACT_SITE 144
FT /note="AMP-threonine intermediate"
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT BINDING 106
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT BINDING 144
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT BINDING 230
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT BINDING 264
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT BINDING 268
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT BINDING 268
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT BINDING 311
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT BINDING 312
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT BINDING 421
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 553
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 633
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 704
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 37..54
FT /note="Alternate"
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT DISULFID 37..42
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 42..72
FT /note="Alternate"
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT DISULFID 52..65
FT /note="Alternate"
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT DISULFID 52..54
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 58..64
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT DISULFID 65..72
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 83..129
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT DISULFID 91..303
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT DISULFID 319..416
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT DISULFID 367..752
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT DISULFID 500..558
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT DISULFID 513..613
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT DISULFID 515..598
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT DISULFID 721..731
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
SQ 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
