SLAA_BOTJA
ID SLAA_BOTJA Reviewed; 155 AA.
AC Q56EB1; Q9PRZ4;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=Snaclec bothrojaracin subunit alpha;
DE Short=BJC subunit alpha;
DE Flags: Precursor;
OS Bothrops jararaca (Jararaca) (Bothrops jajaraca).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=8724;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-31; 44-50; 61-67; 82-94;
RP 106-120 AND 131-149, AND FUNCTION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=9346315; DOI=10.1111/j.1432-1033.1997.00550.x;
RA Arocas V., Castro H.C., Zingali R.B., Guillin M.-C., Jandrot-Perrus M.,
RA Bon C., Wisner A.;
RT "Molecular cloning and expression of bothrojaracin, a potent thrombin
RT inhibitor from snake venom.";
RL Eur. J. Biochem. 248:550-557(1997).
RN [2]
RP PROTEIN SEQUENCE OF 24-39, AND FUNCTION.
RC TISSUE=Venom;
RX PubMed=8399228; DOI=10.1021/bi00091a034;
RA Zingali R.B., Jandrot-Perrus M., Guillin M.-C., Bon C.;
RT "Bothrojaracin, a new thrombin inhibitor isolated from Bothrops jararaca
RT venom: characterization and mechanism of thrombin inhibition.";
RL Biochemistry 32:10794-10802(1993).
RN [3]
RP PROTEIN SEQUENCE OF 24-51, AND VARIANTS PRO-31; GLN-34; GLN-35; VAL-40;
RP GLU-43; GLN-43; HIS-46; ASN-46 AND TYR-51.
RC TISSUE=Venom;
RA Monteiro R.Q., Carlini C.R., Guimaraes J.A., Bon C., Zingali R.B.;
RT "Distinct bothrojaracin isoforms produced by individual jararaca (Bothrops
RT jararaca) snakes.";
RL Toxicon 35:649-657(1997).
RN [4]
RP PROTEIN SEQUENCE OF 24-38; 44-51 AND 82-94, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=18221976; DOI=10.1016/j.toxicon.2007.11.026;
RA Oliveira-Carvalho A.L., Guimaraes P.R., Abreu P.A., Dutra D.L.S.,
RA Junqueira-de-Azevedo I.L.M., Rodrigues C.R., Ho P.L., Castro H.C.,
RA Zingali R.B.;
RT "Identification and characterization of a new member of snake venom
RT thrombin inhibitors from Bothrops insularis using a proteomic approach.";
RL Toxicon 51:659-671(2008).
RN [5]
RP FUNCTION.
RX PubMed=8703912; DOI=10.1021/bi960043l;
RA Arocas V., Zingali R.B., Guillin M.-C., Bon C., Jandrot-Perrus M.;
RT "Bothrojaracin: a potent two-site-directed thrombin inhibitor.";
RL Biochemistry 35:9083-9089(1996).
RN [6]
RP FUNCTION.
RX PubMed=9657441;
RA Arocas V., Lemaire C., Bouton M.C., Bezeaud A., Bon C., Guillin M.-C.,
RA Jandrot-Perrus M.;
RT "Inhibition of thrombin-catalyzed factor V activation by bothrojaracin.";
RL Thromb. Haemost. 79:1157-1161(1998).
RN [7]
RP FUNCTION.
RX PubMed=11051105; DOI=10.1006/abbi.2000.2006;
RA Monteiro R.Q., Zingali R.B.;
RT "Inhibition of prothrombin activation by bothrojaracin, a C-type lectin
RT from Bothrops jararaca venom.";
RL Arch. Biochem. Biophys. 382:123-128(2000).
RN [8]
RP FUNCTION.
RX PubMed=11910195; DOI=10.1159/000048073;
RA Zingali R.B., Bianconi M.L., Monteiro R.Q.;
RT "Interaction of bothrojaracin with prothrombin.";
RL Haemostasis 31:273-278(2001).
RN [9]
RP FUNCTION.
RX PubMed=11514680; DOI=10.1110/ps.09001;
RA Monteiro R.Q., Bock P.E., Bianconi M.L., Zingali R.B.;
RT "Characterization of bothrojaracin interaction with human prothrombin.";
RL Protein Sci. 10:1897-1904(2001).
RN [10]
RP FUNCTION.
RX PubMed=11858489;
RA Monteiro R.Q., Zingali R.B.;
RT "Bothrojaracin, a proexosite I ligand, inhibits factor Va-accelerated
RT prothrombin activation.";
RL Thromb. Haemost. 87:288-293(2002).
RN [11]
RP FUNCTION, ION-DEPENDENCE, AND BIOASSAY.
RX PubMed=16707920; DOI=10.1159/000092416;
RA Zingali R.B., Ferreira M.S., Assafim M., Frattani F.S., Monteiro R.Q.;
RT "Bothrojaracin, a Bothrops jararaca snake venom-derived (pro)thrombin
RT inhibitor, as an anti-thrombotic molecule.";
RL Pathophysiol. Haemost. Thromb. 34:160-163(2005).
CC -!- FUNCTION: This potent antithrombotic agent acts in a calcium-
CC independent manner. Exerts its anticoagulant effect by two distinct
CC mechanisms. It binds to activated thrombin through exosite 1, blocking
CC fibrinogen clotting, platelet activation, factor V activation and other
CC effects, and it interacts with prothrombin (F2), decreasing its
CC proteolytic activation -especially in the presence of factor Va. In
CC vivo, intravenous injection before thrombosis induction causes a
CC significant decrease in thrombus weight. Furthermore, BJC shows a
CC prolonged effect by remaining in the plasma bound to prothrombin for at
CC least 12 hours. {ECO:0000269|PubMed:11051105,
CC ECO:0000269|PubMed:11514680, ECO:0000269|PubMed:11858489,
CC ECO:0000269|PubMed:11910195, ECO:0000269|PubMed:16707920,
CC ECO:0000269|PubMed:8399228, ECO:0000269|PubMed:8703912,
CC ECO:0000269|PubMed:9346315, ECO:0000269|PubMed:9657441}.
CC -!- SUBUNIT: Heterodimer of subunits alpha and beta; disulfide-linked.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR EMBL; AY962524; AAX68503.1; -; mRNA.
DR PIR; A48630; A48630.
DR AlphaFoldDB; Q56EB1; -.
DR SMR; Q56EB1; -.
DR MEROPS; I63.002; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR016187; CTDL_fold.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW Blood coagulation cascade inhibiting toxin; Direct protein sequencing;
KW Disulfide bond; Hemostasis impairing toxin;
KW Platelet aggregation inhibiting toxin; Secreted; Signal; Toxin.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:18221976,
FT ECO:0000269|PubMed:8399228, ECO:0000269|PubMed:9346315,
FT ECO:0000269|Ref.3"
FT CHAIN 24..155
FT /note="Snaclec bothrojaracin subunit alpha"
FT /id="PRO_5000095800"
FT DOMAIN 32..151
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 25..36
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 53..150
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 102
FT /note="Interchain (with C-98 in subunit beta)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 125..142
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT VARIANT 31
FT /note="S -> P"
FT /evidence="ECO:0000269|Ref.3"
FT VARIANT 34
FT /note="G -> Q"
FT /evidence="ECO:0000269|Ref.3"
FT VARIANT 35
FT /note="H -> Q"
FT /evidence="ECO:0000269|Ref.3"
FT VARIANT 40
FT /note="F -> V"
FT /evidence="ECO:0000269|Ref.3"
FT VARIANT 43
FT /note="K -> E"
FT /evidence="ECO:0000269|Ref.3"
FT VARIANT 43
FT /note="K -> Q"
FT /evidence="ECO:0000269|Ref.3"
FT VARIANT 46
FT /note="W -> H"
FT /evidence="ECO:0000269|Ref.3"
FT VARIANT 46
FT /note="W -> N"
FT /evidence="ECO:0000269|Ref.3"
FT VARIANT 51
FT /note="R -> Y"
FT /evidence="ECO:0000269|Ref.3"
FT CONFLICT 32..33
FT /note="HE -> YG (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="H -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 155 AA; 17577 MW; D3AF68BB7F1F2F77 CRC64;
MGRFLFVSFG LLVVFLSLSG TAADCPSDWS SHEGHCYKFF QQKMNWADAE RFCSEQAKGG
HLVSFQSDGE TDFVVNLVTE KIQSTDLYAW IGLRVQNKEK QCSSKWSDGS SVSYENVVGR
TVKKCFALEK EQEFFVWINI YCGQQNPFVC KSPPP
