ID   CRVP_CROAD              Reviewed;         240 AA.
AC   F8S0Y4;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 1.
DT   03-AUG-2022, entry version 32.
DE   RecName: Full=Cysteine-rich secretory protein;
DE            Short=CRVP;
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   PROTEIN SEQUENCE OF 20-34, AND 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: Weakly blocks contraction of smooth muscle elicited by high
CC       potassium-induced depolarization, but does not block caffeine-
CC       stimulated contraction. May target voltage-gated calcium channels on
CC       smooth muscle (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
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DR   EMBL; HQ414088; AEJ31966.1; -; mRNA.
DR   EMBL; JU173623; AFJ49149.1; -; mRNA.
DR   AlphaFoldDB; F8S0Y4; -.
DR   SMR; F8S0Y4; -.
DR   PRIDE; F8S0Y4; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005246; F:calcium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   CDD; cd05383; CAP_CRISP; 1.
DR   Gene3D; 1.10.10.740; -; 1.
DR   Gene3D; 3.40.33.10; -; 1.
DR   InterPro; IPR018244; Allrgn_V5/Tpx1_CS.
DR   InterPro; IPR014044; CAP_domain.
DR   InterPro; IPR035940; CAP_sf.
DR   InterPro; IPR042076; Crisp-like_dom.
DR   InterPro; IPR001283; CRISP-related.
DR   InterPro; IPR013871; Cysteine_rich_secretory.
DR   InterPro; IPR034117; SCP_CRISP.
DR   InterPro; IPR003582; ShKT_dom.
DR   InterPro; IPR002413; V5_allergen-like.
DR   PANTHER; PTHR10334; PTHR10334; 1.
DR   Pfam; PF00188; CAP; 1.
DR   Pfam; PF08562; Crisp; 1.
DR   PRINTS; PR00838; V5ALLERGEN.
DR   PRINTS; PR00837; V5TPXLIKE.
DR   SMART; SM00198; SCP; 1.
DR   SUPFAM; SSF55797; SSF55797; 1.
DR   PROSITE; PS01009; CRISP_1; 1.
DR   PROSITE; PS01010; CRISP_2; 1.
DR   PROSITE; PS51670; SHKT; 1.
PE   1: Evidence at protein level;
KW   Calcium channel impairing toxin; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:24231107"
FT   CHAIN           20..240
FT                   /note="Cysteine-rich secretory protein"
FT                   /id="PRO_5000771356"
FT   DOMAIN          38..166
FT                   /note="SCP"
FT   DOMAIN          202..235
FT                   /note="ShKT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        75..153
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        92..167
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        148..164
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        186..193
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        189..198
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        202..235
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        211..229
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        220..233
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
SQ   SEQUENCE   240 AA;  26629 MW;  123E310E7D798E0B CRC64;
     MIAFIVLPIL AAVLQQSSGS VDFDSESPRK PEIQNKIVDL HNSLRRSVNP TASNMLKMEW
     YPEAADNAER WAYRCIDSHS PRDSRVLGGI KCGENIYISP VPIKWTEIIH AWHGENKNFK
     YGIGADPPNA VTGHFTQIVW YKSYHVGCAA AYCPSSEYSY FYVCQYCPAG NIRGKTATPY
     KSGPPCGDCP SACDNGLCTN PCTKEDKYSN CKSLVQQAGC QDKQMQSDCS AICFCQNKII