DID2A_MACLB
ID DID2A_MACLB Reviewed; 128 AA.
AC Q3BK13; Q1JRG8; Q2PXP4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 54.
DE RecName: Full=Disintegrin lebein-2-alpha;
DE AltName: Full=ML-(2,8,15);
DE AltName: Full=MS-I;
DE AltName: Full=VLDA;
DE AltName: Full=ml-G2;
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; 64-86 AND 88-106,
RP 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 "Cloning of dimeric disintegrins from Vipera lebetina venom.";
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 47-111.
RX PubMed=17177090; DOI=10.1007/s00239-006-0161-4;
RA Bazaa A., Juarez P., Marrakchi N., Bel Lasfer Z., El Ayeb M., Calvete J.J.,
RA Sanz L.;
RT "Loss of introns along the evolutionary diversification pathway of snake
RT venom disintegrins evidenced by sequence analysis of genomic DNA from
RT Macrovipera lebetina transmediterranea and Echis ocellatus.";
RL J. Mol. Evol. 64:261-271(2007).
RN [4]
RP PROTEIN SEQUENCE OF 47-57, SUBUNIT, FUNCTION, 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: Inhibits ADP-induced human platelet aggregation. Antagonist
CC of alpha-IIb/beta-3 (ITGA2B/ITGB3) (By similarity). Also avidly binds
CC to the laminin-binding beta-1 integrins (alpha-3/beta-1 (ITGA3/ITGB1),
CC alpha-6/beta-1 (ITGA6/ITGB1), and alpha-7/beta-1 (ITGA7/ITGB1)) in an
CC RGD-independent manner. {ECO:0000250, ECO:0000269|PubMed:12719418}.
CC -!- SUBUNIT: Heterodimer with subunit beta; disulfide-linked.
CC {ECO:0000269|PubMed:12719418}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=14735; Method=MALDI; Note=Heterodimer.;
CC Evidence={ECO:0000269|PubMed:12719418};
CC -!- MISCELLANEOUS: Has no interaction 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 EMBL; AM114016; CAJ34940.1; -; mRNA.
DR EMBL; DQ295886; ABC18317.1; -; mRNA.
DR EMBL; AM261812; CAK12655.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3BK13; -.
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; Signal; Toxin.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..46
FT /evidence="ECO:0000269|PubMed:12719418"
FT /id="PRO_0000318185"
FT CHAIN 47..111
FT /note="Disintegrin lebein-2-alpha"
FT /id="PRO_5000076856"
FT PROPEP 112..128
FT /id="PRO_0000318186"
FT DOMAIN 47..111
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 89..91
FT /note="Cell attachment site; atypical (MLD)"
FT DISULFID 53..76
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 54
FT /note="Interchain (with C-? in subunit beta)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 59
FT /note="Interchain (with C-? 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 56
FT /note="P -> D (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="I -> V (in Ref. 2; ABC18317)"
FT /evidence="ECO:0000305"
FT CONFLICT 109..111
FT /note="WKS -> YKD (in Ref. 3; CAK12655)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="G -> D (in Ref. 2; ABC18317)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 128 AA; 14020 MW; DBA231407BE11EB0 CRC64;
MIQVLLVTIC LAVFPFHGSS IILESGNVND YEVVYPKKVT LLPTGAMNSA NPCCDPITCK
PRKGEHCVSG PCCRNCKFLN PGTICKRTML DGLNDYCTGI TSDCPRNPWK SEEDEMKWSA
TAKGSVLM
