ID   VM2C_PROFL              Reviewed;          75 AA.
AC   P23323;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Disintegrin CTF-II;
DE   AltName: Full=Cytotoxic factor 2;
DE   Contains:
DE     RecName: Full=Disintegrin CTF-I;
DE     AltName: Full=Cytotoxic factor 1;
OS   Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Protobothrops.
OX   NCBI_TaxID=88087;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Venom;
RX   PubMed=1917887; DOI=10.1093/oxfordjournals.jbchem.a123437;
RA   Yamakawa Y., Omori-Satoh T., Maeyama J.;
RT   "Primary structures of cytotoxic factors isolated from habu (Trimeresurus
RT   flavoviridis) venom.";
RL   J. Biochem. 109:667-669(1991).
CC   -!- FUNCTION: Inhibits fibrinogen interaction with platelet receptors, and
CC       inhibits aggregation induced by ADP, thrombin, collagen and platelet-
CC       activating factor. Acts by binding to the alpha-IIb/beta-3
CC       (ITGA2B/ITGB3) on the platelet surface (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Monomer (disintegrin). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MISCELLANEOUS: The disintegrin belongs to the medium disintegrin
CC       subfamily.
CC   -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II
CC       subfamily. P-IIa sub-subfamily. {ECO:0000305}.
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DR   PIR; JX0169; JX0169.
DR   AlphaFoldDB; P23323; -.
DR   SMR; P23323; -.
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; Toxin.
FT   CHAIN           1..75
FT                   /note="Disintegrin CTF-II"
FT                   /id="PRO_0000007244"
FT   CHAIN           4..75
FT                   /note="Disintegrin CTF-I"
FT                   /id="PRO_0000007245"
FT   DOMAIN          1..75
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   MOTIF           54..56
FT                   /note="Cell attachment site"
FT   DISULFID        9..18
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        11..19
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        24..38
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        32..62
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        37..41
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        50..69
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
SQ   SEQUENCE   75 AA;  8328 MW;  329B00C6F08F62A3 CRC64;
     ELLEEGEDCY CHIPPNPCCD PATCKLTPGS QCAEGLCCDQ CRFKKKGTIC RIARGDFPDD
     RCTGLSDDCP RWNDL