VM2JC_BOTJA
ID VM2JC_BOTJA Reviewed; 161 AA.
AC P31989; Q0NZX4;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Zinc metalloproteinase/disintegrin;
DE Contains:
DE RecName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE EC=3.4.24.-;
DE Contains:
DE RecName: Full=Disintegrin jararacin {ECO:0000303|PubMed:8419314};
DE AltName: Full=Platelet aggregation activation inhibitor;
DE Contains:
DE RecName: Full=Disintegrin jararacin-AGEEC;
DE Contains:
DE RecName: Full=Disintegrin jararacin-GEEC;
DE Contains:
DE RecName: Full=Disintegrin jararacin-EC;
DE Flags: Precursor; Fragment;
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], MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=16919699; DOI=10.1016/j.toxicon.2006.07.010;
RA Cidade D.A.P., Wermelinger L.S., Lobo-Hajdu G., Davila A.M.R., Bon C.,
RA Zingali R.B., Albano R.M.;
RT "Molecular diversity of disintegrin-like domains within metalloproteinase
RT precursors of Bothrops jararaca.";
RL Toxicon 48:590-599(2006).
RN [2]
RP PROTEIN SEQUENCE OF 89-161, FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=8419314; DOI=10.1016/s0021-9258(18)54041-2;
RA Scarborough R.M., Rose J.W., Naughton M.A., Phillips D.R., Nannizzi L.,
RA Arfsten A., Campbell A.M., Charo I.F.;
RT "Characterization of the integrin specificities of disintegrins isolated
RT from American pit viper venoms.";
RL J. Biol. Chem. 268:1058-1065(1993).
CC -!- FUNCTION: [Snake venom metalloproteinase]: Impairs hemostasis in the
CC envenomed animal. {ECO:0000250}.
CC -!- FUNCTION: Disintegrin: inhibit platelet aggregation induced by ADP,
CC thrombin, platelet-activating factor and collagen. Acts by inhibiting
CC fibrinogen interaction with platelet receptors GPIIb/GPIIIa
CC (ITGA2B/ITGB3) (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16919699,
CC ECO:0000269|PubMed:8419314}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:16919699, ECO:0000305|PubMed:8419314}.
CC -!- MASS SPECTROMETRY: [Disintegrin jararacin]: Mass=7738.99; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16919699};
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II
CC subfamily. P-IIa sub-subfamily. {ECO:0000305}.
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DR EMBL; DQ375442; ABD34835.1; -; mRNA.
DR AlphaFoldDB; P31989; -.
DR SMR; P31989; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.390.10; -; 1.
DR Gene3D; 4.10.70.10; -; 1.
DR InterPro; IPR018358; Disintegrin_CS.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; SSF57552; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 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; Hydrolase; Metal-binding; Metalloprotease;
KW Platelet aggregation inhibiting toxin; Protease; Secreted; Toxin; Zinc;
KW Zymogen.
FT CHAIN <1..72
FT /note="Snake venom metalloproteinase"
FT /id="PRO_0000318085"
FT PROPEP 73..88
FT /evidence="ECO:0000250"
FT /id="PRO_0000318086"
FT CHAIN 89..161
FT /note="Disintegrin jararacin"
FT /evidence="ECO:0000269|PubMed:8419314"
FT /id="PRO_0000101787"
FT CHAIN 90..161
FT /note="Disintegrin jararacin-AGEEC"
FT /id="PRO_0000318087"
FT CHAIN 91..161
FT /note="Disintegrin jararacin-GEEC"
FT /id="PRO_0000318088"
FT CHAIN 93..161
FT /note="Disintegrin jararacin-EC"
FT /id="PRO_0000318089"
FT DOMAIN <1..72
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 89..161
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 139..141
FT /note="Cell attachment site"
FT ACT_SITE 13
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 12
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 16
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 22
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 27..51
FT /evidence="ECO:0000250"
FT DISULFID 29..34
FT /evidence="ECO:0000250"
FT DISULFID 135..154
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 161 AA; 17555 MW; 36050C75AC5CEA26 CRC64;
ERDLLVAVTM DHELGHNLGI RHDTGSCSCG GYSCVMSPVI SHDISKYFSD CSYIQCWDFI
MKENPQCILN KHLRTDTVST PVSGNELLEA GEECDCGTPG NPCCDAATCK LRPGAQCAEG
LCCDQCRFKG AGKICRRARG DNPDDRCTGQ SADCPRNRFH A
