ID   CRVP_AGKPI              Reviewed;         240 AA.
AC   Q7ZTA0;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Cysteine-rich venom protein piscivorin;
DE   Flags: Precursor;
OS   Agkistrodon piscivorus piscivorus (Eastern cottonmouth).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Agkistrodon.
OX   NCBI_TaxID=8716;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-82; 92-117; 121-142;
RP   176-201 AND 208-238, CHARACTERIZATION, FUNCTION, AND MASS SPECTROMETRY.
RC   TISSUE=Venom gland;
RX   PubMed=12646276; DOI=10.1016/s0003-9861(03)00028-6;
RA   Yamazaki Y., Hyodo F., Morita T.;
RT   "Wide distribution of cysteine-rich secretory proteins in snake venoms:
RT   isolation and cloning of novel snake venom cysteine-rich secretory
RT   proteins.";
RL   Arch. Biochem. Biophys. 412:133-141(2003).
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. {ECO:0000269|PubMed:12646276}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MASS SPECTROMETRY: Mass=24842.8; Mass_error=131.7; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:12646276};
CC   -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Piscivorin entry;
CC       URL="https://en.wikipedia.org/wiki/Piscivorin";
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DR   EMBL; AY181982; AAO62994.1; -; mRNA.
DR   AlphaFoldDB; Q7ZTA0; -.
DR   SMR; Q7ZTA0; -.
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:12646276"
FT   CHAIN           20..240
FT                   /note="Cysteine-rich venom protein piscivorin"
FT                   /id="PRO_0000006274"
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;  26682 MW;  B360237DEC9364DC CRC64;
     MIAFIVLPIL AAVLQQSSGS VDFDSESPRK PEIQNQIVDL HNSLRRSVNP TASNMLKMEW
     YPEAAANAER WAYRCIESHS PRNSRVLGGI KCGENIYMSS IPIKWTEIIH AWHGENKNFK
     YGIGADPPNA VIGHFTQIVW YKSYLVGCAA AYCPSSEYSY FYVCQYCPAG NIIGKIATPY
     KSGPPCGDCP SACVNGLCTN PCTKEDKYTN CKSLVQQYGC QDKQMQSECS AICFCQNKII