Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Zinc metalloproteinase-disintegrin-like bothropasin

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

Functioni

Zinc metalloproteinase-disintegrin-like bothropasin: has caseinolytic activity. Causes hemorrhage on rabbit skin and causes myonecrosis in mouse tibialis anterior muscle.
Disintegrin-like bothropasin: inhibits platelet aggregation.

Catalytic activityi

Cleavage of 5-His-|-Leu-6, 10-His-|-Leu-11, 14-Ala-|-Leu-15, 16-Tyr-|-Leu-17 and 24-Phe-|-Phe-25 in insulin B chain.1 Publication

Cofactori

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

Enzyme regulationi

Inhibited by EDTA and EGTA.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi201 – 2011Calcium 1
Metal bindingi285 – 2851Calcium 1
Metal bindingi334 – 3341Zinc; catalytic1 Publication
Active sitei335 – 3351PROSITE-ProRule annotation
Metal bindingi338 – 3381Zinc; catalytic1 Publication
Metal bindingi344 – 3441Zinc; catalytic1 Publication
Sitei378 – 3781Necessary, but not sufficient, for proteolytic processingBy similarity
Metal bindingi389 – 3891Calcium 1; via carbonyl oxygen
Metal bindingi392 – 3921Calcium 1
Metal bindingi404 – 4041Calcium 2; via carbonyl oxygen
Metal bindingi407 – 4071Calcium 2
Metal bindingi409 – 4091Calcium 2; via carbonyl oxygen
Metal bindingi411 – 4111Calcium 2
Metal bindingi414 – 4141Calcium 2
Metal bindingi417 – 4171Calcium 2
Metal bindingi468 – 4681Calcium 3
Metal bindingi469 – 4691Calcium 3; via carbonyl oxygen
Metal bindingi471 – 4711Calcium 3
Metal bindingi483 – 4831Calcium 3
Metal bindingi484 – 4841Calcium 3; via carbonyl oxygen

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Cell adhesion impairing toxin, Hemorrhagic toxin, Hemostasis impairing toxin, Hydrolase, Metalloprotease, Platelet aggregation inhibiting toxin, Protease, Toxin

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.24.49. 911.

Protein family/group databases

MEROPSiM12.140.

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc metalloproteinase-disintegrin-like bothropasin (EC:3.4.24.49)
Alternative name(s):
Snake venom metalloproteinase
Short name:
SVMP
Cleaved into the following chain:
OrganismiBothrops jararaca (Jararaca) (Bothrops jajaraca)
Taxonomic identifieri8724 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeBothrops

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence analysisAdd
BLAST
Propeptidei21 – 191171By similarityPRO_0000326418Add
BLAST
Chaini192 – 610419Zinc metalloproteinase-disintegrin-like bothropasinPRO_0000326419Add
BLAST
Chaini399 – 610212Disintegrin-like bothropasinBy similarityPRO_0000326420Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei192 – 1921Pyrrolidone carboxylic acid1 Publication
Disulfide bondi309 ↔ 389In zinc metalloproteinase-disintegrin-like bothropasin1 Publication
Disulfide bondi349 ↔ 373In zinc metalloproteinase-disintegrin-like bothropasin1 Publication
Disulfide bondi351 ↔ 356In zinc metalloproteinase-disintegrin-like bothropasin1 Publication
Glycosylationi372 – 3721N-linked (GlcNAc...)1 Publication
Disulfide bondi405 ↔ 434In zinc metalloproteinase-disintegrin-like bothropasin; alternate1 Publication
Disulfide bondi405 ↔ 424In disintegrin-like bothropasin; alternateBy similarity
Disulfide bondi416 ↔ 434In disintegrin-like bothropasin; alternateBy similarity
Disulfide bondi416 ↔ 429In zinc metalloproteinase-disintegrin-like bothropasin; alternate1 Publication
Disulfide bondi418 ↔ 424In zinc metalloproteinase-disintegrin-like bothropasin; alternate1 Publication
Disulfide bondi428 ↔ 451In zinc metalloproteinase-disintegrin-like bothropasin1 Publication
Disulfide bondi442 ↔ 448In zinc metalloproteinase-disintegrin-like bothropasin1 Publication
Disulfide bondi447 ↔ 473In zinc metalloproteinase-disintegrin-like bothropasin1 Publication
Disulfide bondi460 ↔ 480In both disintegrin-like bothropasin and zinc metalloproteinase-disintegrin-like bothropasinPROSITE-ProRule annotation1 Publication
Disulfide bondi467 ↔ 499In zinc metalloproteinase-disintegrin-like bothropasin; alternate1 Publication
Disulfide bondi467 ↔ 492In disintegrin-like bothropasin; alternateBy similarity
Disulfide bondi492 ↔ 504In zinc metalloproteinase-disintegrin-like bothropasin; alternate1 Publication
Disulfide bondi499 ↔ 504In disintegrin-like bothropasinBy similarity
Disulfide bondi511 ↔ 561In zinc metalloproteinase-disintegrin-like bothropasin; alternate1 Publication
Disulfide bondi511 ↔ 526In disintegrin-like bothropasin; alternateBy similarity
Disulfide bondi526 ↔ 572In zinc metalloproteinase-disintegrin-like bothropasin; alternate1 Publication
Disulfide bondi539 ↔ 549In zinc metalloproteinase-disintegrin-like bothropasin; alternate1 Publication
Disulfide bondi549 ↔ 556In disintegrin-like bothropasin; alternateBy similarity
Disulfide bondi556 ↔ 598In zinc metalloproteinase-disintegrin-like bothropasin; alternate1 Publication
Disulfide bondi561 ↔ 572In disintegrin-like bothropasinBy similarity
Disulfide bondi592 ↔ 603In zinc metalloproteinase-disintegrin-like bothropasin; alternate1 Publication
Disulfide bondi598 ↔ 603In disintegrin-like bothropasinBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid, Zymogen

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Monomer.2 Publications

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DSLX-ray2.70A/B192-610[»]
ProteinModelPortaliO93523.
SMRiO93523. Positions 195-610.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO93523.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini198 – 394197Peptidase M12BPROSITE-ProRule annotationAdd
BLAST
Domaini402 – 48887DisintegrinPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi466 – 4683D/ECD-tripeptide

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi489 – 610122Cys-richAdd
BLAST

Sequence similaritiesi

Contains 1 disintegrin domain.PROSITE-ProRule annotation
Contains 1 peptidase M12B domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG006978.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
4.10.70.10. 1 hit.
InterProiIPR006586. ADAM_Cys-rich.
IPR018358. Disintegrin_CS.
IPR001762. Disintegrin_dom.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR002870. Peptidase_M12B_N.
[Graphical view]
PfamiPF08516. ADAM_CR. 1 hit.
PF00200. Disintegrin. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
[Graphical view]
PRINTSiPR00289. DISINTEGRIN.
SMARTiSM00608. ACR. 1 hit.
SM00050. DISIN. 1 hit.
[Graphical view]
SUPFAMiSSF57552. SSF57552. 1 hit.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS00427. DISINTEGRIN_1. 1 hit.
PS50214. DISINTEGRIN_2. 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.

O93523-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIEVLLVTIC LAAFPYQGSS IILESGNVND YEVVYPRKVT ALPKGAVQPK
60 70 80 90 100
YEDAMQYEFK VNGEPVVLHL EKNKGLFSKD YSETHYSPDG REITTYPAVE
110 120 130 140 150
DHCYYHGRIE NDADSTASIS ACNGLKGHFK LQRETYFIEP LKLSNSEAHA
160 170 180 190 200
VFKYENVEKE DEAPKMCGVT QNWKSYEPIK KASQLVVTAE QQKYNPFRYV
210 220 230 240 250
ELFIVVDQGM VTKNNGDLDK IKARMYELAN IVNEILRYLY MHAALVGLEI
260 270 280 290 300
WSNGDKITVK PDVDYTLNSF AEWRKTDLLT RKKHDNAQLL TAIDFNGPTI
310 320 330 340 350
GYAYIGSMCH PKRSVAIVED YSPINLVVAV IMAHEMGHNL GIHHDTDFCS
360 370 380 390 400
CGDYPCIMGP TISNEPSKFF SNCSYIQCWD FIMKENPQCI LNEPLGTDIV
410 420 430 440 450
SPPVCGNELL EVGEECDCGT PENCQNECCD AATCKLKSGS QCGHGDCCEQ
460 470 480 490 500
CKFSKSGTEC RASMSECDPA EHCTGQSSEC PADVFHKNGQ PCLDNYGYCY
510 520 530 540 550
NGNCPIMYHQ CYALFGADVY EAEDSCFKDN QKGNYYGYCR KENGKKIPCA
560 570 580 590 600
PEDVKCGRLY CKDNSPGQNN PCKMFYSNDD EHKGMVLPGT KCADGKVCSN
610
GHCVDVATAY
Length:610
Mass (Da):68,213
Last modified:November 1, 1999 - v2
Checksum:i014C8AE6B86F25DD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF056025 mRNA. Translation: AAC61986.2.

Genome annotation databases

KEGGiag:AAC61986.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF056025 mRNA. Translation: AAC61986.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DSLX-ray2.70A/B192-610[»]
ProteinModelPortaliO93523.
SMRiO93523. Positions 195-610.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM12.140.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAC61986.

Phylogenomic databases

HOVERGENiHBG006978.

Enzyme and pathway databases

BRENDAi3.4.24.49. 911.

Miscellaneous databases

EvolutionaryTraceiO93523.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
4.10.70.10. 1 hit.
InterProiIPR006586. ADAM_Cys-rich.
IPR018358. Disintegrin_CS.
IPR001762. Disintegrin_dom.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR002870. Peptidase_M12B_N.
[Graphical view]
PfamiPF08516. ADAM_CR. 1 hit.
PF00200. Disintegrin. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
[Graphical view]
PRINTSiPR00289. DISINTEGRIN.
SMARTiSM00608. ACR. 1 hit.
SM00050. DISIN. 1 hit.
[Graphical view]
SUPFAMiSSF57552. SSF57552. 1 hit.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS00427. DISINTEGRIN_1. 1 hit.
PS50214. DISINTEGRIN_2. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning and expression of structural domains of bothropasin, a P-III metalloproteinase from the venom of Bothrops jararaca."
    Assakura M.T., Silva C.A., Mentele R., Camargo A.C.M., Serrano S.M.T.
    Toxicon 41:217-227(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 248-253; 257-268; 273-276; 296-303 AND 395-420, FUNCTION.
    Tissue: Venom and Venom gland.
  2. "Isolation and characterization of a proteolytic enzyme from the venom of the snake Bothrops jararaca (Jararaca)."
    Mandelbaum F.R., Reichel A.P., Assakura M.T.
    Toxicon 20:955-972(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBUNIT.
    Tissue: Venom.
  3. "The three-dimensional structure of bothropasin, the main hemorrhagic factor from Bothrops jararaca venom: insights for a new classification of snake venom metalloprotease subgroups."
    Muniz J.R.C., Ambrosio A.L.B., Selistre-de-Araujo H.S., Cominetti M.R., Moura-da-Silva A.M., Oliva G., Garratt R.C., Souza D.H.F.
    Toxicon 52:807-816(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 192-610 IN COMPLEX WITH ZINC AND CALCIUM IONS, COFACTOR, METAL-BINDING SITES, GLYCOSYLATION AT ASN-372, PYROGLUTAMATE FORMATION AT GLN-192, DISULFIDE BONDS.
    Tissue: Venom.

Entry informationi

Entry nameiVM3BP_BOTJA
AccessioniPrimary (citable) accession number: O93523
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: November 1, 1999
Last modified: March 16, 2016
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Miscellaneous

The metalloproteinase domain which is released from the cleavage of the disintegrin bothropasin may be unstable.

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.