ID   CRVP_GLOBL              Reviewed;         240 AA.
AC   Q8JI40;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Cysteine-rich venom protein ablomin;
DE   Flags: Precursor;
OS   Gloydius blomhoffii (Mamushi) (Agkistrodon halys blomhoffi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius.
OX   NCBI_TaxID=242054;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-59; 121-172; 176-205 AND
RP   209-204, AND FUNCTION.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=12047379; DOI=10.1046/j.1432-1033.2002.02940.x;
RA   Yamazaki Y., Koike H., Sugiyama Y., Motoyoshi K., Wada T., Hishinuma S.,
RA   Mita M., Morita T.;
RT   "Cloning and characterization of novel snake venom proteins that block
RT   smooth muscle contraction.";
RL   Eur. J. Biochem. 269:2708-2715(2002).
RN   [2]
RP   FUNCTION.
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: Blocks contraction of smooth muscle elicited by high
CC       potassium-induced depolarization, but does not block caffeine-
CC       stimulated contraction. Since high potassium-treatment activates
CC       voltage-gated channels and caffeine exposure activates ryanodine
CC       receptors, this toxin may target L-type voltage-gated calcium channels
CC       (Cav) (and not ryanodine receptors) on smooth muscle (PubMed:12047379).
CC       This toxin also shows a little inhibition on cyclic nucleotide-gated
CC       CNGA1 channel (PubMed:12646276). {ECO:0000269|PubMed:12047379,
CC       ECO:0000269|PubMed:12646276}.
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; AF384218; AAM45664.1; -; mRNA.
DR   AlphaFoldDB; Q8JI40; -.
DR   SMR; Q8JI40; -.
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;
KW   Voltage-gated calcium channel impairing toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:12047379"
FT   CHAIN           20..240
FT                   /note="Cysteine-rich venom protein ablomin"
FT                   /id="PRO_0000006273"
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;  26914 MW;  254798B93F3D8567 CRC64;
     MIVFIVLPIL AAVLQQSSGN VDFDSESPRK PEIQNEIVDL HNSLRRSVNP TASNMLKMEW
     YPEAAANAER WAYRCIEDHS SPDSRVLEGI KCGENIYMSP IPMKWTDIIH IWHDEYKNFK
     YGIGADPPNA VSGHFTQIVW YKSYRAGCAA AYCPSSEYSY FYVCQYCPAG NMRGKTATPY
     TSGPPCGDCP SACDNGLCTN PCTQEDVFTN CNSLVQQSNC QHNYIKTNCP ASCFCHNEIK