LEB_MACLB
ID LEB_MACLB Reviewed; 38 AA.
AC Q7LZ09; Q7LZ10;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Lebetin-2-alpha {ECO:0000303|PubMed:11910186, ECO:0000303|PubMed:8769304};
DE Short=L2alpha {ECO:0000303|PubMed:11910186};
DE Contains:
DE RecName: Full=Lebetin-1-alpha {ECO:0000303|PubMed:11910186, ECO:0000303|PubMed:8769304, ECO:0000303|PubMed:9839678};
DE Short=L1alpha {ECO:0000303|PubMed:11910186, ECO:0000303|PubMed:9839678};
DE Contains:
DE RecName: Full=Lebetin-1-beta {ECO:0000303|PubMed:11910186, ECO:0000303|PubMed:8769304, ECO:0000303|PubMed:9839678};
DE Short=L1beta {ECO:0000303|PubMed:11910186, ECO:0000303|PubMed:9839678};
DE Contains:
DE RecName: Full=Lebetin-1-gamma {ECO:0000303|PubMed:11910186, ECO:0000303|PubMed:8769304, ECO:0000303|PubMed:9839678};
DE Short=L1gamma {ECO:0000303|PubMed:11910186, ECO:0000303|PubMed:9839678};
DE Contains:
DE RecName: Full=Lebetin-2-beta {ECO:0000303|PubMed:11910186, ECO:0000303|PubMed:8769304};
DE Short=L2beta {ECO:0000303|PubMed:11910186};
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 PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=8769304; DOI=10.1016/0014-5793(96)00774-0;
RA Barbouche R., Marrakchi N., Mansuelle P., Krifi M.N., Fenouillet E.,
RA Rochat H., el Ayeb M.;
RT "Novel anti-platelet aggregation polypeptides from Vipera lebetina venom:
RT isolation and characterization.";
RL FEBS Lett. 392:6-10(1996).
RN [2]
RP SYNTHESIS OF 1-13 AND 2-13, AND FUNCTION.
RC TISSUE=Venom;
RX PubMed=9839678; DOI=10.1016/s0041-0101(98)00118-4;
RA Barbouche R., Marrakchi N., Mabrouk K., Krifi M.N., Van Rietschoten J.,
RA Fenouillet E., El Ayeb M., Rochat H.;
RT "Anti-platelet activity of the peptides composing the lebetin 1 family, a
RT new class of inhibitors of platelet aggregation.";
RL Toxicon 36:1939-1947(1998).
RN [3]
RP FUNCTION, MUTAGENESIS OF ASN-3; LYS-4; PRO-5; PRO-6; LYS-7; LYS-8; GLY-9;
RP PRO-10; PRO-11 AND ASN-12, SYNTHESIS 1-38; 1-13; 2-38; 2-13 AND 3-13, AND
RP MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=11910186; DOI=10.1159/000048064;
RA Marrakchi N., Mabrouk K., Regaya I., Sarray S., Fathallah M., Rochat H.,
RA El Ayeb M.;
RT "Lebetin peptides: potent platelet aggregation inhibitors.";
RL Haemostasis 31:207-210(2001).
RN [4]
RP STRUCTURE BY NMR OF LEBETIN-2-ALPHA, AND DISULFIDE BOND.
RA Mosbah A., Marrakchi N., Ganzalez M.J., Van Rietschoten J., Giralt E.,
RA El Ayeb M., Rochat H., Sabatier J.M., Darbon H., Mabrouk K.;
RT "Lebetin peptides, a new class of potent aggregation inhibitors.";
RL Submitted (JUL-2003) to the PDB data bank.
CC -!- FUNCTION: [Lebetin-1-alpha]: Inhibits platelet aggregation induced by
CC thrombin, collagen and PAF-acether (PubMed:8769304, PubMed:9839678).
CC Human platelet aggregation induced by thrombin is inhibited by
CC synthetic lebetin-1-alpha with (IC(50)=140 nM) (PubMed:11910186). In
CC vivo, inhibits collagen-induced thrombocytopenia in rats
CC (PubMed:8769304, PubMed:9839678). Is not toxic upon intravenous
CC injection into mice and rats (PubMed:8769304).
CC {ECO:0000269|PubMed:11910186, ECO:0000269|PubMed:8769304,
CC ECO:0000269|PubMed:9839678}.
CC -!- FUNCTION: [Lebetin-1-beta]: Inhibits platelet aggregation induced by
CC thrombin, collagen and PAF-acether (PubMed:8769304, PubMed:9839678).
CC Human platelet aggregation induced by thrombin is inhibited by
CC synthetic lebetin-1-beta with (IC(50)=32 nM) (PubMed:11910186). In
CC vivo, inhibits collagen-induced thrombocytopenia in rats
CC (PubMed:8769304, PubMed:9839678). Is not toxic upon intravenous
CC injection into mice and rats (PubMed:8769304).
CC {ECO:0000269|PubMed:11910186, ECO:0000269|PubMed:8769304,
CC ECO:0000269|PubMed:9839678}.
CC -!- FUNCTION: [Lebetin-1-gamma]: Inhibits platelet aggregation induced by
CC thrombin, collagen and PAF-acether (PubMed:8769304, PubMed:9839678).
CC Human platelet aggregation induced by thrombin is inhibited by
CC synthetic lebetin-1-gamma with (IC(50)=5 nM) (PubMed:11910186). In
CC vivo, inhibits collagen-induced thrombocytopenia in rats
CC (PubMed:8769304, PubMed:9839678). Is not toxic upon intravenous
CC injection into mice and rats (PubMed:8769304).
CC {ECO:0000269|PubMed:11910186, ECO:0000269|PubMed:8769304,
CC ECO:0000269|PubMed:9839678}.
CC -!- FUNCTION: [Lebetin-2-alpha]: Inhibits platelet aggregation induced by
CC thrombin, collagen and PAF-acether (PubMed:8769304, PubMed:9839678).
CC Human platelet aggregation induced by thrombin is inhibited by
CC synthetic lebetin-1-alpha with (IC(50)=2.5 nM) (PubMed:11910186). In
CC vivo, inhibits collagen-induced thrombocytopenia in rats
CC (PubMed:8769304, PubMed:9839678). Is not toxic upon intravenous
CC injection into mice and rats (PubMed:8769304).
CC {ECO:0000269|PubMed:11910186, ECO:0000269|PubMed:8769304,
CC ECO:0000269|PubMed:9839678}.
CC -!- FUNCTION: [Lebetin-2-beta]: Inhibits platelet aggregation induced by
CC thrombin, collagen and PAF-acether (PubMed:8769304, PubMed:9839678).
CC Human platelet aggregation induced by thrombin is inhibited by
CC synthetic lebetin-1-alpha with (IC(50)=2.8 nM) (PubMed:11910186). In
CC vivo, inhibits collagen-induced thrombocytopenia in rats
CC (PubMed:8769304, PubMed:9839678). Is not toxic upon intravenous
CC injection into mice and rats (PubMed:8769304).
CC {ECO:0000269|PubMed:8769304, ECO:0000269|PubMed:9839678}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8769304}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:8769304}.
CC -!- MASS SPECTROMETRY: [Lebetin-2-alpha]: Mass=3943.74; Mass_error=0.46;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:8769304};
CC -!- MASS SPECTROMETRY: [Lebetin-1-alpha]: Mass=1305.74; Mass_error=0.38;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:8769304};
CC -!- MASS SPECTROMETRY: [Lebetin-2-beta]: Mass=3886.92; Mass_error=0.38;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:8769304};
CC -!- MASS SPECTROMETRY: [Lebetin-1-beta]: Mass=1248.69; Mass_error=0.31;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:8769304};
CC -!- MASS SPECTROMETRY: [Lebetin-1-gamma]: Mass=1191.45; Mass_error=0.43;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:11910186};
CC -!- MISCELLANEOUS: Mutagenesis was carried out on lebetin-1-gamma.
CC {ECO:0000305|PubMed:11910186}.
CC -!- SIMILARITY: Belongs to the natriuretic peptide family. {ECO:0000305}.
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DR PIR; S71380; S71380.
DR PIR; S71381; S71381.
DR PDB; 1Q01; NMR; -; A=1-38.
DR PDBsum; 1Q01; -.
DR AlphaFoldDB; Q7LZ09; -.
DR SMR; Q7LZ09; -.
DR EvolutionaryTrace; Q7LZ09; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0008217; P:regulation of blood pressure; IEA:UniProtKB-KW.
DR InterPro; IPR000663; Natr_peptide.
DR InterPro; IPR030480; Natr_peptide_CS.
DR InterPro; IPR002408; Natriuretic_peptide_brain.
DR Pfam; PF00212; ANP; 1.
DR PRINTS; PR00712; BNATPEPTIDE.
DR PRINTS; PR00710; NATPEPTIDES.
DR SMART; SM00183; NAT_PEP; 1.
DR PROSITE; PS00263; NATRIURETIC_PEPTIDE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Hemostasis impairing toxin; Hypotensive agent;
KW Platelet aggregation inhibiting toxin; Secreted; Toxin.
FT PEPTIDE 1..38
FT /note="Lebetin-2-alpha"
FT /evidence="ECO:0000269|PubMed:8769304"
FT /id="PRO_0000335995"
FT PEPTIDE 1..13
FT /note="Lebetin-1-alpha"
FT /evidence="ECO:0000269|PubMed:8769304"
FT /id="PRO_0000335996"
FT PEPTIDE 2..38
FT /note="Lebetin-2-beta"
FT /evidence="ECO:0000269|PubMed:8769304"
FT /id="PRO_0000335997"
FT PEPTIDE 2..13
FT /note="Lebetin-1-beta"
FT /evidence="ECO:0000269|PubMed:8769304"
FT /id="PRO_0000335998"
FT PEPTIDE 3..13
FT /note="Lebetin-1-gamma"
FT /evidence="ECO:0000269|PubMed:8769304"
FT /id="PRO_0000335999"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 14..30
FT /evidence="ECO:0000269|Ref.4, ECO:0000312|PDB:1Q01"
FT MUTAGEN 3
FT /note="N->A: Little decrease of antiplatelet activity."
FT /evidence="ECO:0000269|PubMed:11910186"
FT MUTAGEN 4
FT /note="K->A: 10-fold increase of antiplatelet activity."
FT /evidence="ECO:0000269|PubMed:11910186"
FT MUTAGEN 5
FT /note="P->A: Important decrease of antiplatelet activity."
FT /evidence="ECO:0000269|PubMed:11910186"
FT MUTAGEN 6
FT /note="P->A: 10-fold increase of antiplatelet activity."
FT /evidence="ECO:0000269|PubMed:11910186"
FT MUTAGEN 7
FT /note="K->A: Little decrease of antiplatelet activity."
FT /evidence="ECO:0000269|PubMed:11910186"
FT MUTAGEN 8
FT /note="K->A: 10-fold increase of antiplatelet activity."
FT /evidence="ECO:0000269|PubMed:11910186"
FT MUTAGEN 9
FT /note="G->A: Important decrease of antiplatelet activity."
FT /evidence="ECO:0000269|PubMed:11910186"
FT MUTAGEN 10
FT /note="P->A: Important decrease of antiplatelet activity."
FT /evidence="ECO:0000269|PubMed:11910186"
FT MUTAGEN 11
FT /note="P->A: Important decrease of antiplatelet activity."
FT /evidence="ECO:0000269|PubMed:11910186"
FT MUTAGEN 12
FT /note="N->A: Important decrease of antiplatelet activity."
FT /evidence="ECO:0000269|PubMed:11910186"
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:1Q01"
SQ SEQUENCE 38 AA; 3945 MW; 831FA5C9B1B09377 CRC64;
GDNKPPKKGP PNGCFGHKID RIGSHSGLGC NKVDDNKG
