ID   DIDA_AGKPI              Reviewed;         111 AA.
AC   Q805F5;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Disintegrin piscivostatin-alpha;
DE            Short=PVS-alpha;
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 {ECO:0000312|EMBL:BAC55946.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SUBUNIT.
RC   TISSUE=Venom {ECO:0000269|PubMed:12450389};
RX   PubMed=12450389; DOI=10.1021/bi025876s;
RA   Okuda D., Koike H., Morita T.;
RT   "A new gene structure of the disintegrin family: a subunit of dimeric
RT   disintegrin has a short coding region.";
RL   Biochemistry 41:14248-14254(2002).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 45-109, AND CHARACTERIZATION.
RC   TISSUE=Venom {ECO:0000269|PubMed:11530017};
RX   PubMed=11530017; DOI=10.1093/oxfordjournals.jbchem.a003000;
RA   Okuda D., Morita T.;
RT   "Purification and characterization of a new RGD/KGD-containing dimeric
RT   disintegrin, piscivostatin, from the venom of Agkistrodon piscivorus
RT   piscivorus: the unique effect of piscivostatin on platelet aggregation.";
RL   J. Biochem. 130:407-415(2001).
RN   [3]
RP   CRYSTALLIZATION.
RC   TISSUE=Venom;
RX   PubMed=11752794; DOI=10.1107/s090744490101736x;
RA   Fujii Y., Okuda D., Fujimoto Z., Morita T., Mizuno H.;
RT   "Crystallization and preliminary crystallographic studies of dimeric
RT   disintegrins from the venom of two Agkistrodon snakes.";
RL   Acta Crystallogr. D 58:145-147(2002).
CC   -!- FUNCTION: Inhibits fibrinogen interaction with platelets. Acts by
CC       binding to alpha-IIb/beta-3 (ITGA2B/ITGB3) on the platelet surface and
CC       inhibits both ADP-induced platelet aggregation and platelet aggregate
CC       dissociation in human platelet-rich plasma.
CC   -!- SUBUNIT: Heterodimer with piscivostatin-beta; disulfide-linked.
CC       {ECO:0000269|PubMed:12450389}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the disintegrin family. Dimeric disintegrin
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AB078905; BAC55946.1; -; mRNA.
DR   AlphaFoldDB; Q805F5; -.
DR   SMR; Q805F5; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   Gene3D; 4.10.70.10; -; 1.
DR   InterPro; IPR018358; Disintegrin_CS.
DR   InterPro; IPR001762; Disintegrin_dom.
DR   InterPro; IPR036436; Disintegrin_dom_sf.
DR   Pfam; PF00200; Disintegrin; 1.
DR   PRINTS; PR00289; DISINTEGRIN.
DR   SMART; SM00050; DISIN; 1.
DR   SUPFAM; SSF57552; SSF57552; 1.
DR   PROSITE; PS00427; DISINTEGRIN_1; 1.
DR   PROSITE; PS50214; DISINTEGRIN_2; 1.
PE   1: Evidence at protein level;
KW   Cell adhesion impairing toxin; Direct protein sequencing; Disulfide bond;
KW   Hemostasis impairing toxin; Platelet aggregation inhibiting toxin;
KW   Secreted; Signal; Toxin.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..44
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000007239"
FT   CHAIN           45..109
FT                   /note="Disintegrin piscivostatin-alpha"
FT                   /id="PRO_0000007240"
FT   PROPEP          110..111
FT                   /id="PRO_0000007241"
FT   DOMAIN          45..111
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   MOTIF           89..91
FT                   /note="Cell attachment site"
FT   DISULFID        53..76
FT                   /evidence="ECO:0000250|UniProtKB:P81742,
FT                   ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        54
FT                   /note="Interchain (with C-426 in subunit beta)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        59
FT                   /note="Interchain (with C-431 in subunit beta)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        67..73
FT                   /evidence="ECO:0000250|UniProtKB:P81742,
FT                   ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        72..97
FT                   /evidence="ECO:0000250|UniProtKB:P81742,
FT                   ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        85..104
FT                   /evidence="ECO:0000250|UniProtKB:P81742,
FT                   ECO:0000255|PROSITE-ProRule:PRU00068"
SQ   SEQUENCE   111 AA;  12119 MW;  E72A6809BCE07836 CRC64;
     MIQVLLVTIC LAVFPYQGSS IILESGNVND YEVVYPRKIT PLPKGAVQPK NPCCDAATCK
     LTPGSQCAEG LCCDQCKFIK AGKICRRARG DNPDYRCTGQ SGDCPRKHFY A