PDE1_CROAD
ID PDE1_CROAD Reviewed; 851 AA.
AC J3SEZ3; F8S0Z8;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 2.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Venom phosphodiesterase 1;
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;
RX PubMed=21255598; DOI=10.1016/j.toxicon.2011.01.008;
RA Rokyta D.R., Wray K.P., Lemmon A.R., Lemmon E.M., Caudle S.B.;
RT "A high-throughput venom-gland transcriptome for the eastern diamondback
RT rattlesnake (Crotalus adamanteus) and evidence for pervasive positive
RT selection across toxin classes.";
RL Toxicon 57:657-671(2011).
RN [2]
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 [3]
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 and collagen.
CC {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AFJ50876.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; HQ414102; AEJ31980.1; -; mRNA.
DR EMBL; JU175352; AFJ50876.1; ALT_INIT; mRNA.
DR AlphaFoldDB; J3SEZ3; -.
DR SMR; J3SEZ3; -.
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; 2.
DR SMART; SM00892; Endonuclease_NS; 1.
DR SMART; SM00477; NUC; 1.
DR SMART; SM00201; SO; 2.
DR SUPFAM; SSF53649; SSF53649; 1.
DR SUPFAM; SSF54060; SSF54060; 1.
DR SUPFAM; SSF90188; SSF90188; 2.
DR PROSITE; PS00524; SMB_1; 2.
DR PROSITE; PS50958; SMB_2; 2.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Hemostasis impairing toxin; Hydrolase;
KW Metal-binding; Platelet aggregation inhibiting toxin; Repeat; Secreted;
KW Signal; Toxin.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..851
FT /note="Venom phosphodiesterase 1"
FT /id="PRO_5000771368"
FT DOMAIN 30..73
FT /note="SMB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DOMAIN 74..118
FT /note="SMB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT MOTIF 58..60
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT ACT_SITE 185
FT /note="AMP-threonine intermediate"
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT BINDING 147
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT BINDING 185
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT BINDING 271
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT BINDING 305
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT BINDING 309
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT BINDING 309
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT BINDING 352
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT BINDING 353
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT BINDING 462
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 512
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 594
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 674
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 745
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 34..51
FT /note="Alternate"
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT DISULFID 34..38
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 38..69
FT /note="Alternate"
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT DISULFID 49..62
FT /note="Alternate"
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT DISULFID 49..51
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 55..61
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT DISULFID 62..69
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 78..95
FT /note="Alternate"
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT DISULFID 78..83
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 83..113
FT /note="Alternate"
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT DISULFID 93..106
FT /note="Alternate"
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT DISULFID 93..95
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 99..105
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT DISULFID 106..113
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 124..170
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT DISULFID 132..344
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT DISULFID 360..457
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT DISULFID 408..793
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT DISULFID 541..599
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT DISULFID 554..654
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT DISULFID 556..639
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
FT DISULFID 762..772
FT /evidence="ECO:0000250|UniProtKB:A0A2D0TC04"
SQ SEQUENCE 851 AA; 96373 MW; 7E1A9CBB0F91C754 CRC64;
MIQQKVLFIS LVAVTLGLGL GLGLKESVQP QVSCRYRCNE TFSKMASGCS CDDKCTERQA
CCSDYEDTCV LPTQSWSCSK LRCGEKRIAN VLCSCSDDCL EKKDCCTDYK SICKGETSWL
KDKCASSGAT QCPAGFEQSP LILFSMDGFR AGYLENWDSL MPNINKLKTC GTHAKYMRAV
YPTKTFVNHY TIATGLYPES HGIIDNNIYD VNLNLNFSLS SSTARNPAWW GGQPIWHTAT
YQGLKAATYF WPGSEVKING SYPTIFKNYN KSIPFEARVT EVLKWLDLPK AKRPDFLTLY
IEEPDTTGHK YGPVSGEIIK ALQMADRTLG MLMEGLKQRN LHNCVNLILL ADHGMEEISC
DRLEYMANYF NNVDFFMYEG PAPRIRSKNV PKDFYTFDSE GIVKNLTCRK PKQYFKAYLS
KDLPKRLHYA NNIRIDKVNL MVDQQWMAVR DKKFTRCKGG THGYDNEFKS MQAIFLAHGP
GFNEKNEVTS FENIEVYNLM CDLLKLKPAP NNGTHGSLNH LLKNPFYTPS PAKEQSSPLS
CPFGPVPSPD VSGCKCSSIT ELEKVNQRLN LNNQAKTESE AHNLPYGRPQ VLQNHSKYCL
LHQAKYISAY SQDILMPLWS SYTIYRSTST SVPPSASDCL RLDVRIPAAQ SQTCSNYQPD
LTITPGFLYP PNFNSSNFEQ YDALITSNIV PMFKGFTRLW NYFHTTLIPK YARERNGLNV
ISGPIFDYNY DGHFDSYDTI KQHVNNTKIP IPTHYFVVLT SCENQINTPL NCLGPLKVLS
FILPHRPDNS ESCADTSPEN LWVEERIQIH TARVRDVELL TGLNFYSGLK QPLPETLQLK
TFLPIFVNPV N
