ID   DID1B_MACLB             Reviewed;          64 AA.
AC   P83254;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Disintegrin lebein-1-beta;
DE   AltName: Full=MS-II;
DE   AltName: Full=Platelet aggregation activation inhibitor;
OS   Macrovipera lebetina (Levantine viper) (Vipera lebetina).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Macrovipera.
OX   NCBI_TaxID=8709 {ECO:0000305};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, SUBUNIT, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=11343790; DOI=10.1016/s0167-4838(01)00168-6;
RA   Gasmi A., Srairi N., Guermazi S., Dekhil H., Karoui H., El Ayeb M.;
RT   "Amino acid structure and characterization of a heterodimeric disintegrin
RT   from Vipera lebetina venom.";
RL   Biochim. Biophys. Acta 1547:51-56(2001).
RN   [2]
RP   ERRATUM OF PUBMED:11343790.
RA   Gasmi A., Srairi N., Guermazi S., Dekhil H., Karoui H., El Ayeb M.;
RL   Biochim. Biophys. Acta 1764:1525-1525(2006).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-15; 17-30 AND 43-59, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=16411889; DOI=10.1042/bj20051678;
RA   Sanz L., Bazaa A., Marrakchi N., Perez A., Chenik M., Bel Lasfer Z.,
RA   El Ayeb M., Calvete J.J.;
RT   "Molecular cloning of disintegrins from Cerastes vipera and Macrovipera
RT   lebetina transmediterranea venom gland cDNA libraries: insight into the
RT   evolution of the snake venom integrin-inhibition system.";
RL   Biochem. J. 395:385-392(2006).
RN   [4]
RP   PROTEIN SEQUENCE OF 1-8, FUNCTION, SUBUNIT, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=12719418; DOI=10.1074/jbc.m301860200;
RA   Eble J.A., Bruckner P., Mayer U.;
RT   "Vipera lebetina venom contains two disintegrins inhibiting laminin-binding
RT   beta1 integrins.";
RL   J. Biol. Chem. 278:26488-26496(2003).
CC   -!- FUNCTION: Strongly inhibits ADP-induced platelet aggregation on human
CC       platelet-rich plasma. Also avidly binds to the laminin-binding beta-1
CC       integrins (alpha-3/beta-1, alpha-6/beta-1, and alpha-7/beta-1) in an
CC       RGD-independent manner. {ECO:0000269|PubMed:11343790,
CC       ECO:0000269|PubMed:12719418}.
CC   -!- SUBUNIT: Heterodimer with subunit alpha; disulfide-linked.
CC       {ECO:0000269|PubMed:11343790, ECO:0000269|PubMed:12719418}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MASS SPECTROMETRY: Mass=7117.62; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:11343790};
CC   -!- MASS SPECTROMETRY: Mass=14083; Method=MALDI; Note=Heterodimer.;
CC       Evidence={ECO:0000269|PubMed:12719418};
CC   -!- MISCELLANEOUS: Does not interact with the collagen-binding alpha-
CC       1/beta-1 (ITGA1/ITGB1) and alpha-2/beta-1 (ITGA2/ITGB1) integrins.
CC       {ECO:0000305|PubMed:12719418}.
CC   -!- SIMILARITY: Belongs to the disintegrin family. Dimeric disintegrin
CC       subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P83254; -.
DR   SMR; P83254; -.
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; TAS:UniProtKB.
DR   GO; GO:0030195; P:negative regulation of blood coagulation; TAS:UniProtKB.
DR   Gene3D; 4.10.70.10; -; 1.
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; 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..64
FT                   /note="Disintegrin lebein-1-beta"
FT                   /id="PRO_0000101813"
FT   DOMAIN          1..64
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   MOTIF           42..44
FT                   /note="Cell attachment site"
FT   DISULFID        6..29
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        7
FT                   /note="Interchain (with C-54 in alpha subunit)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        12
FT                   /note="Interchain (with C-59 in alpha subunit)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        20..26
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        25..50
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        38..57
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
SQ   SEQUENCE   64 AA;  7121 MW;  619A5AD340184FBC CRC64;
     NSGNPCCDPV TCKPRRGWHC VSNPCCDNCK FMRAGTICNR ARGDDMNDYC TGISSDCPRN
     PYKD