ID   VM2_CROTA               Reviewed;          71 AA.
AC   C0HK50;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2016, sequence version 1.
DT   25-MAY-2022, entry version 9.
DE   RecName: Full=Disintegrin tzabcanin {ECO:0000303|PubMed:26163300};
OS   Crotalus tzabcan (Yucatan neotropical rattlesnake) (Crotalus simus
OS   tzabcan).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX   NCBI_TaxID=1043006 {ECO:0000303|PubMed:26163300};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-34, FUNCTION, AND
RP   SUBCELLULAR LOCATION.
RC   TISSUE=Venom {ECO:0000303|PubMed:26163300};
RX   PubMed=26163300; DOI=10.1016/j.biochi.2015.07.005;
RA   Saviola A.J., Modahl C.M., Mackessy S.P.;
RT   "Disintegrins of Crotalus simus tzabcan venom: Isolation, characterization
RT   and evaluation of the cytotoxic and anti-adhesion activities of tzabcanin,
RT   a new RGD disintegrin.";
RL   Biochimie 116:92-102(2015).
RN   [2]
RP   FUNCTION.
RX   PubMed=27060015; DOI=10.1016/j.ijbiomac.2016.04.008;
RA   Saviola A.J., Burns P.D., Mukherjee A.K., Mackessy S.P.;
RT   "The disintegrin tzabcanin inhibits adhesion and migration in melanoma and
RT   lung cancer cells.";
RL   Int. J. Biol. Macromol. 88:457-464(2016).
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 aggregation induced by ADP, thrombin, platelet-activating
CC       factor and collagen (By similarity). Inhibits cell adhesion to
CC       vitronectin, probably by blocking its receptor integrin alpha-V/beta-3
CC       (ITGAV/ITGB3), and to fibronectin in vitro (PubMed:26163300,
CC       PubMed:27060015). Shows little to no cytotoxicity in vitro
CC       (PubMed:26163300, PubMed:27060015). {ECO:0000250|UniProtKB:P18618,
CC       ECO:0000269|PubMed:26163300, ECO:0000269|PubMed:27060015}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26163300}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:26163300}.
CC   -!- MISCELLANEOUS: The disintegrin belongs to the medium disintegrin
CC       subfamily. {ECO:0000305|PubMed:26163300}.
CC   -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II
CC       subfamily. P-IIa sub-subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; C0HK50; -.
DR   SMR; C0HK50; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; 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; Cell adhesion impairing toxin; Direct protein sequencing;
KW   Disulfide bond; Hemostasis impairing toxin;
KW   Platelet aggregation inhibiting toxin; Secreted; Toxin.
FT   CHAIN           1..71
FT                   /note="Disintegrin tzabcanin"
FT                   /id="PRO_0000437868"
FT   DOMAIN          1..71
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   MOTIF           49..51
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        4..19
FT                   /evidence="ECO:0000250|UniProtKB:P21859"
FT   DISULFID        6..14
FT                   /evidence="ECO:0000250|UniProtKB:P21859"
FT   DISULFID        13..36
FT                   /evidence="ECO:0000250|UniProtKB:P21859"
FT   DISULFID        27..33
FT                   /evidence="ECO:0000250|UniProtKB:P21859"
FT   DISULFID        32..57
FT                   /evidence="ECO:0000250|UniProtKB:P21859"
FT   DISULFID        45..64
FT                   /evidence="ECO:0000250|UniProtKB:P21859"
SQ   SEQUENCE   71 AA;  7591 MW;  7081ED8D1428D371 CRC64;
     GEECDCGSPA NPCCDAATCK LRPGAQCADG LCCDQCRFIK KGTICRRARG DNPDDRCTGQ
     SADCPRNHFH A