ID   CRVP_CROAT              Reviewed;         240 AA.
AC   Q7ZT99;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Cysteine-rich venom protein catrin;
DE            Short=CRVP;
DE   AltName: Full=Catrin-1;
DE   AltName: Full=Catrin-2;
DE   Flags: Precursor;
OS   Crotalus atrox (Western 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=8730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-74; 76-77; 92-117;
RP   121-144; 158-204 AND 213-238, 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).
RN   [2]
RP   PROTEIN SEQUENCE OF 20-34; 58-70; 146-157 AND 213-240, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=19371136; DOI=10.1021/pr900249q;
RA   Calvete J.J., Fasoli E., Sanz L., Boschetti E., Righetti P.G.;
RT   "Exploring the venom proteome of the western diamondback rattlesnake,
RT   Crotalus atrox, via snake venomics and combinatorial peptide ligand library
RT   approaches.";
RL   J. Proteome Res. 8:3055-3067(2009).
CC   -!- FUNCTION: Catrin-2 weakly blocks contraction of smooth muscle elicited
CC       by high potassium-induced depolarization, but does not block caffeine-
CC       stimulated contraction. Catrin-1 has no significant effect. May target
CC       voltage-gated calcium channels on smooth muscle.
CC       {ECO:0000269|PubMed:12646276}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MASS SPECTROMETRY: Mass=24747.1; Mass_error=71.8; Method=MALDI;
CC       Note=Catrin-1.; Evidence={ECO:0000269|PubMed:12646276};
CC   -!- MASS SPECTROMETRY: Mass=24729.9; Mass_error=54.4; Method=MALDI;
CC       Note=Catrin-2.; Evidence={ECO:0000269|PubMed:12646276};
CC   -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
CC   -!- CAUTION: Some authors describe two catrins (catrin-1 and -2), with
CC       different activities and masses, but no difference in sequence is
CC       described. {ECO:0000305|PubMed:12646276}.
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DR   EMBL; AY181983; AAO62995.1; -; mRNA.
DR   AlphaFoldDB; Q7ZT99; -.
DR   SMR; Q7ZT99; -.
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                   ECO:0000269|PubMed:19371136"
FT   CHAIN           20..240
FT                   /note="Cysteine-rich venom protein catrin"
FT                   /id="PRO_0000006275"
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"
FT   CONFLICT        178
FT                   /note="T -> Y (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   240 AA;  26647 MW;  849256FD28AF787D CRC64;
     MIAFIVLPIL AAVLQQSSGS VDFDSESPRK PEIQNKIVDL HNFLRRSVNP TASNMLKMEW
     YPEAAANAER WAYRCIESHS PRDSRVLGGI KCGENIYMSP VPIKWTEIIH AWHGENKNFK
     YGIGAVPPNA VTGHFSQVVW YKSYRIGCAA AYCPSSKYSY FYVCQYCPAG NIIGKTATPY
     KSGPPCGDCP SACDNGLCTN PCTKEDKYTN CKSLVQQAGC QDKQMQSDCP AICFCQNKII