DID1A_MACLB
ID DID1A_MACLB Reviewed; 111 AA.
AC P83253; Q2PZH2; Q3BK12;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Disintegrin lebein-1-alpha;
DE AltName: Full=ML-3;
DE AltName: Full=MS-II;
DE AltName: Full=Platelet aggregation activation inhibitor;
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], PROTEIN SEQUENCE OF 48-62; 64-74; 78-87 AND
RP 90-106, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom, and 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 NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Siigur E., Aaspollu A., Siigur J.;
RT "Lebein alpha, a subunit of dimeric disintegrin with a short coding
RT region.";
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 48-111, FUNCTION, SUBUNIT, MASS SPECTROMETRY, AND
RP SUBCELLULAR LOCATION.
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 [4]
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 [5]
RP PROTEIN SEQUENCE OF 48-55, 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 beta; disulfide-linked.
CC {ECO:0000269|PubMed:11343790, ECO:0000269|PubMed:12719418}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11343790}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:11343790}.
CC -!- MASS SPECTROMETRY: Mass=6992.05; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:11343790};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM114017; CAJ34941.1; -; mRNA.
DR EMBL; DQ288157; ABC00778.1; -; mRNA.
DR AlphaFoldDB; P83253; -.
DR SMR; P83253; -.
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; 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; Signal; Toxin.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..47
FT /evidence="ECO:0000269|PubMed:11343790,
FT ECO:0000269|PubMed:12719418, ECO:0000269|PubMed:16411889"
FT /id="PRO_0000318090"
FT CHAIN 48..111
FT /note="Disintegrin lebein-1-alpha"
FT /id="PRO_5000076857"
FT DOMAIN 47..111
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 89..91
FT /note="Cell attachment site"
FT DISULFID 53..76
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 54
FT /note="Interchain (with C-7 in subunit beta)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 59
FT /note="Interchain (with C-12 in subunit beta)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 67..73
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 72..97
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 85..104
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT CONFLICT 32
FT /note="E -> D (in Ref. 2; ABC00778)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="P -> L (in Ref. 2; ABC00778)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 111 AA; 12099 MW; 040234D8F7597A0C CRC64;
MIQVLLVTIC LAVFPYQGSS IILESGNVND YEIVYPKKVT VLPTGAMNSG NPCCDPVTCK
PRRGEHCVSG PCCRNCKFLN AGTICNRARG DDMNDYCTGI SSDCPRNPYK D
