ID   VESP_CROAD              Reviewed;         222 AA.
AC   F8S122;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 1.
DT   25-MAY-2022, entry version 25.
DE   RecName: Full=Vespryn;
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.
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: Neurotoxin. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the ohanin/vespryn family. {ECO:0000305}.
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DR   EMBL; HQ414126; AEJ32004.1; -; mRNA.
DR   EMBL; JU173741; AFJ49267.1; -; mRNA.
DR   AlphaFoldDB; F8S122; -.
DR   SMR; F8S122; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.920; -; 1.
DR   InterPro; IPR001870; B30.2/SPRY.
DR   InterPro; IPR043136; B30.2/SPRY_sf.
DR   InterPro; IPR003879; Butyrophylin_SPRY.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR006574; PRY.
DR   InterPro; IPR003877; SPRY_dom.
DR   Pfam; PF13765; PRY; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   PRINTS; PR01407; BUTYPHLNCDUF.
DR   SMART; SM00589; PRY; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Neurotoxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..44
FT                   /evidence="ECO:0000255"
FT   PROPEP          45..52
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000425651"
FT   CHAIN           53..159
FT                   /note="Vespryn"
FT                   /id="PRO_0000425652"
FT   PROPEP          160..222
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000425653"
FT   DOMAIN          53..159
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   CARBOHYD        195
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   222 AA;  24735 MW;  2945008F4CDFA8E9 CRC64;
     MSPSAGLQFS LYFLQTKKVL WKLTDKEKGL CYILLFTLCF FADQENGGKA LASPPGIWKR
     ADVTFDSNTA FSSLVVSANK KTVKNVGVPQ VVPDNPERFN SSPCVLGSPG FRSGKHYFEV
     KYGTQREWAV GIAGKSVKRK GNLMLVPEER IWQMGLWWLR HLETDPGRVH STSGKITVFV
     DYNGGNVIFD LNRINTTLKA NFNGEEVVPF FYLGGTVSLT TL