ID   DIS_MACLB               Reviewed;         107 AA.
AC   Q3BK14;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=Disintegrin lebestatin;
DE   AltName: Full=ML-(6,9,10);
DE   AltName: Full=ML-4;
DE   Flags: Precursor;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
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   [2]
RP   PROTEIN SEQUENCE OF 65-105, FUNCTION, SUBUNIT, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=16200076; DOI=10.1038/labinvest.3700350;
RA   Kallech-Ziri O., Luis J., Daoud S., Bazaa A., Srairi Abid N., Andreotti N.,
RA   Lehmann M., Zouari R., Mabrouk K., Marvaldi J., Sabatier J.-M., El Ayeb M.,
RA   Marrakchi N.;
RT   "Lebestatin, a disintegrin from Macrovipera venom, inhibits integrin-
RT   mediated cell adhesion, migration and angiogenesis.";
RL   Lab. Invest. 85:1507-1516(2005).
RN   [3]
RP   PROTEIN SEQUENCE OF 65-76, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=16206329; DOI=10.1002/pmic.200402024;
RA   Bazaa A., Marrakchi N., El Ayeb M., Sanz L., Calvete J.J.;
RT   "Snake venomics: comparative analysis of the venom proteomes of the
RT   Tunisian snakes Cerastes cerastes, Cerastes vipera and Macrovipera
RT   lebetina.";
RL   Proteomics 5:4223-4235(2005).
CC   -!- FUNCTION: Specifically interacts with the alpha-1/beta-1 integrin
CC       (ITGA1/ITGB1). Exhibits highly inhibitory effects on cell adhesion and
CC       cell migration to collagens I and IV. Also shows in vivo anti-
CC       angiogenic activity. {ECO:0000269|PubMed:16200076}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16200076}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MASS SPECTROMETRY: Mass=4408.8; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:16206329};
CC   -!- MASS SPECTROMETRY: Mass=4411.52; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:16200076};
CC   -!- SIMILARITY: Belongs to the disintegrin family. Short disintegrin
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AM114015; CAJ34939.1; -; mRNA.
DR   AlphaFoldDB; Q3BK14; -.
DR   SMR; Q3BK14; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   Gene3D; 4.10.70.10; -; 1.
DR   InterPro; IPR036436; Disintegrin_dom_sf.
DR   SUPFAM; SSF57552; SSF57552; 1.
PE   1: Evidence at protein level;
KW   Angiogenesis; Cell adhesion impairing toxin; Developmental protein;
KW   Differentiation; Direct protein sequencing; Disulfide bond; Secreted;
KW   Signal; Toxin.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..64
FT                   /id="PRO_0000318187"
FT   CHAIN           65..105
FT                   /note="Disintegrin lebestatin"
FT                   /id="PRO_0000318188"
FT   PROPEP          106..107
FT                   /id="PRO_0000318189"
FT   DOMAIN          65..105
FT                   /note="Disintegrin"
FT   MOTIF           85..87
FT                   /note="Cell attachment site; atypical (KTS)"
FT   DISULFID        65..74
FT                   /evidence="ECO:0000250"
FT   DISULFID        70..93
FT                   /evidence="ECO:0000250"
FT   DISULFID        71..98
FT                   /evidence="ECO:0000250"
FT   DISULFID        83..100
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   107 AA;  11498 MW;  A0143385AF6D713C CRC64;
     MIQVLLVIIC LAVFPFQGSS KTLKSGNVND YEVVNPGTVT GLPKGAVEEK HEPMKGNTLQ
     KFPLCTTGPC CRQCKLKPAG TTCWKTSRTS HYCTGKSCDC PSYPGNG