VM1B1_BOTAS
ID VM1B1_BOTAS Reviewed; 408 AA.
AC P83512; Q072L4;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Snake venom metalloproteinase BaP1;
DE Short=SVMP;
DE EC=3.4.24.-;
DE AltName: Full=Hemorrhagic metalloproteinase BaP1;
DE Short=Bap-1;
DE Flags: Precursor;
OS Bothrops asper (Terciopelo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=8722;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Arce V., Azofeifa G., Flores M., Alape A.;
RT "Molecular cloning and sequence analysis of a type I metalloproteinase from
RT Bothrops asper snake venom.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|PDB:1ND1}
RP PROTEIN SEQUENCE OF 192-394, COFACTOR, SUBUNIT, MASS SPECTROMETRY,
RP PYROGLUTAMATE FORMATION AT GLN-192, DISULFIDE BONDS, X-RAY CRYSTALLOGRAPHY
RP (1.93 ANGSTROMS) IN COMPLEX WITH ZINC ION, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=14500885; DOI=10.1110/ps.03102403;
RA Watanabe L., Shannon J.D., Valente R.H., Rucavado A., Alape-Giron A.,
RA Kamiguti A.S., Theakston R.D.G., Fox J.W., Gutierrez J.M., Arni R.K.;
RT "Amino acid sequence and crystal structure of BaP1, a metalloproteinase
RT from Bothrops asper snake venom that exerts multiple tissue-damaging
RT activities.";
RL Protein Sci. 12:2273-2281(2003).
RN [3]
RP FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=Costa Rica; TISSUE=Venom;
RX PubMed=7778126; DOI=10.1016/0041-0101(94)00138-x;
RA Gutierrez J.M., Romero M., Diaz C., Borkow G., Ovadia M.;
RT "Isolation and characterization of a metalloproteinase with weak
RT hemorrhagic activity from the venom of the snake Bothrops asper
RT (terciopelo).";
RL Toxicon 33:19-29(1995).
RN [4]
RP FUNCTION.
RX PubMed=11200361; DOI=10.1080/09629350020025728;
RA Farsky S.H.P., Goncalves L.R.C., Gutierrez J.M., Correa A.P., Rucavado A.,
RA Gasque P., Tambourgi D.V.;
RT "Bothrops asper snake venom and its metalloproteinase BaP-1 activate the
RT complement system. Role in leucocyte recruitment.";
RL Mediators Inflamm. 9:213-221(2000).
RN [5]
RP FUNCTION, AND ACTIVITY REGULATION.
RC STRAIN=Colombia; TISSUE=Venom;
RX PubMed=20600221; DOI=10.1016/j.toxicon.2010.06.016;
RA Patino A.C., Pereanez J.A., Nunez V., Benjumea D.M., Fernandez M.,
RA Rucavado A., Sanz L., Calvete J.J.;
RT "Isolation and biological characterization of Batx-I, a weak hemorrhagic
RT and fibrinogenolytic PI metalloproteinase from Colombian Bothrops atrox
RT venom.";
RL Toxicon 56:936-943(2010).
RN [6]
RP FUNCTION.
RX PubMed=23385358; DOI=10.1016/j.jprot.2013.01.021;
RA Bernardes C.P., Menaldo D.L., Camacho E., Rosa J.C., Escalante T.,
RA Rucavado A., Lomonte B., Gutierrez J.M., Sampaio S.V.;
RT "Proteomic analysis of Bothrops pirajai snake venom and characterization of
RT BpirMP, a new P-I metalloproteinase.";
RL J. Proteomics 80:250-267(2013).
CC -!- FUNCTION: Zinc metalloprotease that exhibits a weak hemorrhagic
CC activity (with a minimum hemorrhagic dose of 20 ug by intradermal and
CC intramuscular injection into mice). The basal membrane components
CC collagen (all chains of type IV) (COL4A4), laminin and nidogen are all
CC degraded by this toxin (PubMed:23385358). Rapidly degrades the Aalpha-
CC chain (FGA) of fibrinogen, and later on, degrades the Bbeta-chain (FGB)
CC of fibrinogen (PubMed:7778126). Also activates the complement system,
CC and induces rat neutrophil chemotaxis (PubMed:11200361). Induces edema
CC in mouse food pad and shows a mild myotoxicity (PubMed:7778126).
CC {ECO:0000269|PubMed:11200361, ECO:0000269|PubMed:20600221,
CC ECO:0000269|PubMed:23385358, ECO:0000269|PubMed:7778126}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA, partially inhibited by o-
CC phenantropine, and not inhibited by PMSF, pepstatin A, and aprotinin.
CC {ECO:0000269|PubMed:20600221, ECO:0000269|PubMed:7778126}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:7778126};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:14500885}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14500885,
CC ECO:0000269|PubMed:7778126}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:14500885, ECO:0000305|PubMed:7778126}.
CC -!- MASS SPECTROMETRY: Mass=22735; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:14500885};
CC -!- MISCELLANEOUS: Does not degrade the gamma-chain (FGG) of fibrinogen.
CC Lacks coagulant and defibrinating activities.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-I
CC subfamily. {ECO:0000305}.
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DR EMBL; DQ247726; ABB76282.1; -; mRNA.
DR PDB; 1ND1; X-ray; 1.93 A; A=194-394.
DR PDB; 2W12; X-ray; 1.46 A; A=194-394.
DR PDB; 2W13; X-ray; 1.14 A; A=194-394.
DR PDB; 2W14; X-ray; 1.08 A; A=194-394.
DR PDB; 2W15; X-ray; 1.05 A; A=194-394.
DR PDBsum; 1ND1; -.
DR PDBsum; 2W12; -.
DR PDBsum; 2W13; -.
DR PDBsum; 2W14; -.
DR PDBsum; 2W15; -.
DR AlphaFoldDB; P83512; -.
DR SMR; P83512; -.
DR BindingDB; P83512; -.
DR ChEMBL; CHEMBL2079851; -.
DR DrugCentral; P83512; -.
DR MEROPS; M12.311; -.
DR EvolutionaryTrace; P83512; -.
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:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chemotaxis; Complement system impairing toxin;
KW Direct protein sequencing; Disulfide bond; Fibrinogenolytic toxin;
KW Hemorrhagic toxin; Hemostasis impairing toxin; Hydrolase; Metal-binding;
KW Metalloprotease; Myotoxin; Protease; Pyrrolidone carboxylic acid; Secreted;
KW Signal; Toxin; Zinc.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..191
FT /evidence="ECO:0000305|PubMed:14500885"
FT /id="PRO_0000330008"
FT CHAIN 192..394
FT /note="Snake venom metalloproteinase BaP1"
FT /evidence="ECO:0000269|PubMed:14500885"
FT /id="PRO_0000078199"
FT PROPEP 395..408
FT /evidence="ECO:0000305|PubMed:14500885"
FT /id="PRO_0000330009"
FT DOMAIN 198..394
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT ACT_SITE 335
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 334
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:14500885,
FT ECO:0007744|PDB:1ND1"
FT BINDING 338
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:14500885,
FT ECO:0007744|PDB:1ND1"
FT BINDING 344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:14500885,
FT ECO:0007744|PDB:1ND1"
FT MOD_RES 192
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:14500885"
FT DISULFID 309..389
FT /evidence="ECO:0000269|PubMed:14500885,
FT ECO:0007744|PDB:1ND1"
FT DISULFID 349..373
FT /evidence="ECO:0000269|PubMed:14500885,
FT ECO:0007744|PDB:1ND1"
FT DISULFID 351..356
FT /evidence="ECO:0000269|PubMed:14500885,
FT ECO:0007744|PDB:1ND1"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:2W15"
FT HELIX 208..213
FT /evidence="ECO:0007829|PDB:2W15"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:2W15"
FT HELIX 218..236
FT /evidence="ECO:0007829|PDB:2W15"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:2W15"
FT STRAND 245..250
FT /evidence="ECO:0007829|PDB:2W15"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:2W14"
FT HELIX 263..276
FT /evidence="ECO:0007829|PDB:2W15"
FT TURN 277..281
FT /evidence="ECO:0007829|PDB:2W15"
FT STRAND 285..291
FT /evidence="ECO:0007829|PDB:2W15"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:2W15"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:2W15"
FT TURN 311..313
FT /evidence="ECO:0007829|PDB:2W15"
FT STRAND 314..319
FT /evidence="ECO:0007829|PDB:2W15"
FT HELIX 325..339
FT /evidence="ECO:0007829|PDB:2W15"
FT STRAND 352..356
FT /evidence="ECO:0007829|PDB:2W15"
FT HELIX 372..385
FT /evidence="ECO:0007829|PDB:2W15"
FT HELIX 388..390
FT /evidence="ECO:0007829|PDB:2W15"
SQ SEQUENCE 408 AA; 45936 MW; 6488D64CAA3880D9 CRC64;
MIEVLLVTIC LAVFPYQGSS IILESGNVND YEVVYPRKVT ELPKGAVQPK YEDAMQYEFK
VNGEPVVLHL EKNKGLFSED YSETHYSPDG RKIITYPSFE DHCYYHGRIE NDADSTASIS
ACNGLKGHFK LQGETYLIEP LKLSDSEAHA VYKYENVEKE DEAPKMCGVT ETNWESYEPI
KKASQSNLTP EQQRFSPRYI ELAVVADHGI FTKYNSNLNT IRTRVHEMLN TVNGFYRSVD
VHAPLANLEV WSKQDLIKVQ KDSSKTLKSF GEWRERDLLP RISHDHAQLL TAVVFDGNTI
GRAYTGGMCD PRHSVGVVRD HSKNNLWVAV TMAHELGHNL GIHHDTGSCS CGAKSCIMAS
VLSKVLSYEF SDCSQNQYET YLTNHNPQCI LNKPLLTVSG NELLEAGE
