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Protein

Snake venom metalloproteinase BaP1

Gene
N/A
Organism
Bothrops asper (Terciopelo)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Zinc metalloprotease that exhibits a weak hemorrhagic activity (with a minimum hemorrhagic dose of 20 µg by intradermal and intramuscular injection into mice). The basal membrane components collagen (all chains of type IV) (COL4A4), laminin and nidogen are all degraded by this toxin (PubMed:23385358). Rapidly degrades the Aalpha-chain (FGA) of fibrinogen, and later on, degrades the Bbeta-chain (FGB) of fibrinogen (PubMed:7778126). Also activates the complement system, and induces rat neutrophil chemotaxis (PubMed:11200361). Induces edema in mouse food pad and a mild myotoxicity (PubMed:7778126).4 Publications

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Enzyme regulationi

Inhibited by EDTA, partially inhibited by o-phenantropine, and not inhibited by PMSF, pepstatin A, and aprotinin.2 Publications

pH dependencei

Optimum pH is 8.0.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi334 – 3341Zinc; catalytic
Active sitei335 – 3351
Metal bindingi338 – 3381Zinc; catalytic
Metal bindingi344 – 3441Zinc; catalytic

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Complement system impairing toxin, Fibrinogenolytic toxin, Hemorrhagic toxin, Hemostasis impairing toxin, Hydrolase, Metalloprotease, Myotoxin, Protease, Toxin

Keywords - Biological processi

Chemotaxis

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM12.311.

Names & Taxonomyi

Protein namesi
Recommended name:
Snake venom metalloproteinase BaP1 (EC:3.4.24.-)
Short name:
SVMP
Alternative name(s):
Hemorrhagic metalloproteinase BaP1
Short name:
Bap-1
OrganismiBothrops asper (Terciopelo)Curated
Taxonomic identifieri8722 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeBothrops

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2079851.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence analysisAdd
BLAST
Propeptidei21 – 1911711 PublicationPRO_0000330008Add
BLAST
Chaini192 – 394203Snake venom metalloproteinase BaP1PRO_0000078199Add
BLAST
Propeptidei395 – 40814PRO_0000330009Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei192 – 1921Pyrrolidone carboxylic acid1 Publication
Disulfide bondi309 ↔ 389PROSITE-ProRule annotation1 Publication
Disulfide bondi349 ↔ 373PROSITE-ProRule annotation1 Publication
Disulfide bondi351 ↔ 356PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Expressioni

Tissue specificityi

Expressed by the venom gland.1 Publication

Interactioni

Subunit structurei

Monomer.1 Publication

Chemistry

BindingDBiP83512.

Structurei

Secondary structure

1
408
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi202 – 2065Combined sources
Helixi208 – 2136Combined sources
Turni214 – 2163Combined sources
Helixi218 – 23619Combined sources
Helixi237 – 2393Combined sources
Beta strandi245 – 2506Combined sources
Beta strandi252 – 2543Combined sources
Helixi263 – 27614Combined sources
Turni277 – 2815Combined sources
Beta strandi285 – 2917Combined sources
Helixi296 – 2983Combined sources
Beta strandi301 – 3033Combined sources
Turni311 – 3133Combined sources
Beta strandi314 – 3196Combined sources
Helixi325 – 33915Combined sources
Beta strandi352 – 3565Combined sources
Helixi372 – 38514Combined sources
Helixi388 – 3903Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ND1X-ray1.93A194-394[»]
2W12X-ray1.46A194-394[»]
2W13X-ray1.14A194-394[»]
2W14X-ray1.08A194-394[»]
2W15X-ray1.05A194-394[»]
ProteinModelPortaliP83512.
SMRiP83512. Positions 193-394.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP83512.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini198 – 394197Peptidase M12BPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 peptidase M12B domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG006978.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR002870. Peptidase_M12B_N.
[Graphical view]
PfamiPF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
[Graphical view]
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P83512-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIEVLLVTIC LAVFPYQGSS IILESGNVND YEVVYPRKVT ELPKGAVQPK
60 70 80 90 100
YEDAMQYEFK VNGEPVVLHL EKNKGLFSED YSETHYSPDG RKIITYPSFE
110 120 130 140 150
DHCYYHGRIE NDADSTASIS ACNGLKGHFK LQGETYLIEP LKLSDSEAHA
160 170 180 190 200
VYKYENVEKE DEAPKMCGVT ETNWESYEPI KKASQSNLTP EQQRFSPRYI
210 220 230 240 250
ELAVVADHGI FTKYNSNLNT IRTRVHEMLN TVNGFYRSVD VHAPLANLEV
260 270 280 290 300
WSKQDLIKVQ KDSSKTLKSF GEWRERDLLP RISHDHAQLL TAVVFDGNTI
310 320 330 340 350
GRAYTGGMCD PRHSVGVVRD HSKNNLWVAV TMAHELGHNL GIHHDTGSCS
360 370 380 390 400
CGAKSCIMAS VLSKVLSYEF SDCSQNQYET YLTNHNPQCI LNKPLLTVSG

NELLEAGE
Length:408
Mass (Da):45,936
Last modified:April 29, 2008 - v2
Checksum:i6488D64CAA3880D9
GO

Mass spectrometryi

Molecular mass is 22735 Da from positions 192 - 394. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ247726 mRNA. Translation: ABB76282.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ247726 mRNA. Translation: ABB76282.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ND1X-ray1.93A194-394[»]
2W12X-ray1.46A194-394[»]
2W13X-ray1.14A194-394[»]
2W14X-ray1.08A194-394[»]
2W15X-ray1.05A194-394[»]
ProteinModelPortaliP83512.
SMRiP83512. Positions 193-394.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiP83512.
ChEMBLiCHEMBL2079851.

Protein family/group databases

MEROPSiM12.311.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG006978.

Miscellaneous databases

EvolutionaryTraceiP83512.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR002870. Peptidase_M12B_N.
[Graphical view]
PfamiPF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
[Graphical view]
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning and sequence analysis of a type I metalloproteinase from Bothrops asper snake venom."
    Arce V., Azofeifa G., Flores M., Alape A.
    Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Venom gland.
  2. "Amino acid sequence and crystal structure of BaP1, a metalloproteinase from Bothrops asper snake venom that exerts multiple tissue-damaging activities."
    Watanabe L., Shannon J.D., Valente R.H., Rucavado A., Alape-Giron A., Kamiguti A.S., Theakston R.D.G., Fox J.W., Gutierrez J.M., Arni R.K.
    Protein Sci. 12:2273-2281(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 192-394, COFACTOR, SUBUNIT, TISSUE SPECIFICITY, MASS SPECTROMETRY, PYROGLUTAMATE FORMATION AT GLN-192, DISULFIDE BONDS, X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) IN COMPLEX WITH ZINC ION.
    Tissue: Venom1 Publication.
  3. "Isolation and characterization of a metalloproteinase with weak hemorrhagic activity from the venom of the snake Bothrops asper (terciopelo)."
    Gutierrez J.M., Romero M., Diaz C., Borkow G., Ovadia M.
    Toxicon 33:19-29(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: Costa Rica.
    Tissue: Venom.
  4. "Bothrops asper snake venom and its metalloproteinase BaP-1 activate the complement system. Role in leucocyte recruitment."
    Farsky S.H.P., Goncalves L.R.C., Gutierrez J.M., Correa A.P., Rucavado A., Gasque P., Tambourgi D.V.
    Mediators Inflamm. 9:213-221(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Isolation and biological characterization of Batx-I, a weak hemorrhagic and fibrinogenolytic PI metalloproteinase from Colombian Bothrops atrox venom."
    Patino A.C., Pereanez J.A., Nunez V., Benjumea D.M., Fernandez M., Rucavado A., Sanz L., Calvete J.J.
    Toxicon 56:936-943(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION.
    Strain: Colombia.
    Tissue: Venom.
  6. "Proteomic analysis of Bothrops pirajai snake venom and characterization of BpirMP, a new P-I metalloproteinase."
    Bernardes C.P., Menaldo D.L., Camacho E., Rosa J.C., Escalante T., Rucavado A., Lomonte B., Gutierrez J.M., Sampaio S.V.
    J. Proteomics 80:250-267(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiVM1B1_BOTAS
AccessioniPrimary (citable) accession number: P83512
Secondary accession number(s): Q072L4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 29, 2008
Last modified: October 14, 2015
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Does not degrade the gamma-chain (FGG) of fibrinogen. Lacks coagulant and defibrinating activities.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.