V5NTD_CROAD
ID V5NTD_CROAD Reviewed; 588 AA.
AC F8S0Z7; J3S3V4;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 2.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Snake venom 5'-nucleotidase;
DE Short=5'-NT;
DE EC=3.1.3.5;
DE AltName: Full=Ecto-5'-nucleotidase;
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=23025625; DOI=10.1186/1471-2164-13-312;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 63-588.
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY.
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).
RN [4]
RP REVIEW, AND FUNCTION.
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 (By similarity).
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:0000250|UniProtKB:P0DJJ5,
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P0DJJ5}; Lipid-
CC anchor, GPI-anchor {ECO:0000250|UniProtKB:P21589}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
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 EMBL; JU173671; AFJ49197.1; -; mRNA.
DR EMBL; HQ414101; AEJ31979.1; -; mRNA.
DR AlphaFoldDB; F8S0Z7; -.
DR SMR; F8S0Z7; -.
DR PRIDE; F8S0Z7; -.
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 GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 3.90.780.10; -; 1.
DR InterPro; IPR008334; 5'-Nucleotdase_C.
DR InterPro; IPR036907; 5'-Nucleotdase_C_sf.
DR InterPro; IPR006146; 5'-Nucleotdase_CS.
DR InterPro; IPR006179; 5_nucleotidase/apyrase.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR PANTHER; PTHR11575; PTHR11575; 1.
DR Pfam; PF02872; 5_nucleotid_C; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR01607; APYRASEFAMLY.
DR SUPFAM; SSF55816; SSF55816; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR PROSITE; PS00785; 5_NUCLEOTIDASE_1; 1.
DR PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein; Membrane;
KW Metal-binding; Nucleotide-binding; Signal; Zinc.
FT SIGNAL 1..40
FT /evidence="ECO:0000255"
FT CHAIN 41..564
FT /note="Snake venom 5'-nucleotidase"
FT /id="PRO_0000418208"
FT PROPEP 565..588
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P21589"
FT /id="PRO_0000418209"
FT BINDING 51
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A0A2I4HXH5"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A0A2I4HXH5"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A0A2I4HXH5"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0A2I4HXH5"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0A2I4HXH5"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0A2I4HXH5"
FT BINDING 257
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0A2I4HXH5"
FT BINDING 259
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P21589"
FT BINDING 368
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P21589"
FT BINDING 404
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P21589"
FT BINDING 409
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P21589"
FT BINDING 432
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P21589"
FT BINDING 515..521
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P21589"
FT SITE 132
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P21589"
FT SITE 135
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P21589"
FT LIPID 564
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000250|UniProtKB:P21589"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 532
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 66..71
FT /evidence="ECO:0000250|UniProtKB:A0A2I4HXH5"
FT DISULFID 367..372
FT /evidence="ECO:0000250|UniProtKB:A0A2I4HXH5"
FT DISULFID 379..401
FT /evidence="ECO:0000250|UniProtKB:A0A2I4HXH5"
FT DISULFID 491..494
FT /evidence="ECO:0000250|UniProtKB:A0A2I4HXH5"
SQ SEQUENCE 588 AA; 64682 MW; BEB908B23F8FFF74 CRC64;
MQTPKRRRGA QGCPRSSPSP PLLLLVRAVW FCAALSVAAG SFELTILHTN DVHARVEQTS
RDSGKCTGQD CYGGVARRAT KIRELRAKHR HVLLLDAGDQ YQGTVWFNFF KGREVVKFMN
SLRYDAMALG NHEFDNGLAG LLDPLLKHAN FPILSANIRP KGSIASNISG YILPYKIINV
GSEKVGIIGY TTKETPVLSN PGPYLEFRDE VEELQNHANK LTTLGVNKII ALGHSGFSED
QRIARKVKGV DVVVGGHTNT FLYTGSPPST EVAAGNYPFM VQSDDGRQVP VVQAYAFGKY
LGYLNVIFDD KGNVIKSSGN PILLNKDISE DQDIKAEVNK MKIQLHNYSS QEIGKTIVYL
NGTTQACRFH ECNLGNLICD AVIYNNVRHP DDNEWNHVSM CIVNGGGIRS PIDERTNNGT
ITLEELTAVL PFGGTFDLLQ IKGSALKQAF EHSVHRHGEG MGELLQVSGI KVVYDLSRKP
GSRVLSLNVL CTECRVPTYV PLEKEKTYKL LLPSFLAAGG DGYHMLKGDS SNHSSGNLDI
SIVGDYIKRM GKVFPAVEGR MIFSAGTLFQ AQLFLTWGLC VSLLYFIL
