ID   VM2G_TRIAB              Reviewed;          73 AA.
AC   P62384; P17496;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Disintegrin albolabrin;
DE   AltName: Full=Platelet aggregation activation inhibitor;
OS   Trimeresurus albolabris (White-lipped pit viper) (Cryptelytrops
OS   albolabris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Trimeresurus.
OX   NCBI_TaxID=8765;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Venom;
RX   PubMed=2191722; DOI=10.1016/0167-4838(90)90229-9;
RA   Williams J., Rucinski B., Holt J., Niewiarowski S.;
RT   "Elegantin and albolabrin purified peptides from viper venoms: homologies
RT   with the RGDS domain of fibrinogen and von Willebrand factor.";
RL   Biochim. Biophys. Acta 1039:81-89(1990).
RN   [2]
RP   DISULFIDE BONDS.
RC   TISSUE=Venom;
RX   PubMed=2036389; DOI=10.1021/bi00235a016;
RA   Calvete J.J., Schaefer W., Soszka T., Lu W., Cook J.J., Jameson B.A.,
RA   Niewiarowski S.;
RT   "Identification of the disulfide bond pattern in albolabrin, an RGD-
RT   containing peptide from the venom of Trimeresurus albolabris: significance
RT   for the expression of platelet aggregation inhibitory activity.";
RL   Biochemistry 30:5225-5229(1991).
RN   [3]
RP   STRUCTURE BY NMR.
RX   PubMed=8281937; DOI=10.1111/j.1432-1033.1993.tb18441.x;
RA   Jaseja M., Smith K.J., Lu X., Williams J.A., Trayer H., Trayer I.P.,
RA   Hyde E.I.;
RT   "1H-NMR studies and secondary structure of the RGD-containing snake toxin,
RT   albolabrin.";
RL   Eur. J. Biochem. 218:853-860(1993).
RN   [4]
RP   STRUCTURE BY NMR.
RX   PubMed=8897089; DOI=10.1111/j.1399-3011.1996.tb00835.x;
RA   Smith K.J., Jaseja M., Lu X., Williams J.A., Hyde E.I., Trayer I.P.;
RT   "Three-dimensional structure of the RGD-containing snake toxin albolabrin
RT   in solution, based on 1H NMR spectroscopy and simulated annealing
RT   calculations.";
RL   Int. J. Pept. Protein Res. 48:220-228(1996).
CC   -!- FUNCTION: Inhibits fibrinogen interaction with platelet receptors. Acts
CC       by binding to alpha-IIb/beta-3 (ITGA2B/ITGB3) on the platelet surface
CC       and inhibits aggregation induced by ADP, thrombin, platelet-activating
CC       factor and collagen.
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; A23731; A23731.
DR   AlphaFoldDB; P62384; -.
DR   SMR; P62384; -.
DR   ELM; P62384; -.
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..73
FT                   /note="Disintegrin albolabrin"
FT                   /id="PRO_0000101809"
FT   DOMAIN          1..73
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   MOTIF           51..53
FT                   /note="Cell attachment site"
FT   DISULFID        6..15
FT                   /evidence="ECO:0000305|PubMed:2036389"
FT   DISULFID        8..16
FT                   /evidence="ECO:0000305|PubMed:2036389"
FT   DISULFID        21..35
FT                   /evidence="ECO:0000305|PubMed:2036389"
FT   DISULFID        29..59
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT                   ECO:0000269|PubMed:2036389"
FT   DISULFID        34..38
FT                   /evidence="ECO:0000305|PubMed:2036389"
FT   DISULFID        47..66
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT                   ECO:0000269|PubMed:2036389"
SQ   SEQUENCE   73 AA;  7574 MW;  F7E011E2F46FEF14 CRC64;
     EAGEDCDCGS PANPCCDAAT CKLLPGAQCG EGLCCDQCSF MKKGTICRRA RGDDLDDYCN
     GISAGCPRNP LHA