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Protein

Zinc metalloproteinase leucurolysin-B

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

Functioni

Snake venom zinc metalloproteinase that acts as a potent hemorrhagic toxin. Hydrolyzes the insulin B chain at the 14-Ala-|-Leu-15 bond but not the 16-Tyr-|-Leu-17 bond. Degrades the alpha-chain of fibrin and hydrolyzes the Aalpha-chain of fibrinogen (FGA) while leaving the beta and gamma chains unaffected. Degrades type-I collagen and its gelatin. Degrades the alpha-1 chain of type-IV collagen and its gelatin but not the alpha-2 chain. Degrades plasma fibronectin, plasma vitronectin and basement membrane enactin. It inhibits collagen-induced platelet aggregation.1 Publication

Miscellaneous

Does not interact with alpha-1/beta-1 or alpha-2/beta-1 integrin.1 Publication

Cofactori

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

Enzyme regulationi

Inhibited by EDTA, but not by PMSF. Pre-incubation with 2 mM DTT completely abolishes activity.1 Publication

pH dependencei

Optimum pH is 7.5-9.3 with dimethyl casein as substrate.1 Publication

Temperature dependencei

Optimum temperature is 30 degrees Celsius with dimethyl casein as substrate.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi11Calcium 1By similarity1
Metal bindingi59Zinc; catalyticBy similarity1
Active sitei60PROSITE-ProRule annotation1
Metal bindingi63Zinc; catalyticBy similarity1
Metal bindingi69Zinc; catalyticBy similarity1
Metal bindingi114Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi117Calcium 1By similarity1
Metal bindingi129Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi132Calcium 2By similarity1
Metal bindingi134Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi136Calcium 2By similarity1
Metal bindingi139Calcium 2By similarity1
Metal bindingi142Calcium 2By similarity1

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • metalloendopeptidase activity Source: UniProtKB
  • toxin activity Source: UniProtKB-KW

GO - Biological processi

  • blood coagulation Source: UniProtKB
  • pathogenesis Source: UniProtKB

Keywordsi

Molecular functionFibrinogenolytic toxin, Fibrinolytic toxin, Hemorrhagic toxin, Hemostasis impairing toxin, Hydrolase, Metalloprotease, Platelet aggregation inhibiting toxin, Protease, Toxin
LigandCalcium, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc metalloproteinase leucurolysin-B1 Publication (EC:3.4.24.-)
Short name:
Leuc-B
Alternative name(s):
Snake venom metalloproteinase
Short name:
SVMP
OrganismiBothrops leucurus (Whitetail lancehead)
Taxonomic identifieri157295 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeBothrops

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000363164‹1 – 324Zinc metalloproteinase leucurolysin-BAdd BLAST›324

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi34 ↔ 114By similarity
Disulfide bondi74 ↔ 98By similarity
Disulfide bondi76 ↔ 81By similarity
Glycosylationi97N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi130 ↔ 159By similarity
Disulfide bondi141 ↔ 154By similarity
Disulfide bondi143 ↔ 149By similarity
Disulfide bondi153 ↔ 176By similarity
Disulfide bondi167 ↔ 173By similarity
Disulfide bondi172 ↔ 198By similarity
Disulfide bondi185 ↔ 205Sequence analysis
Disulfide bondi192 ↔ 224By similarity
Disulfide bondi217 ↔ 229By similarity
Disulfide bondi236 ↔ 286By similarity
Disulfide bondi251 ↔ 295By similarity
Disulfide bondi264 ↔ 274By similarity
Disulfide bondi281 ↔ 315By similarity
Glycosylationi296N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi305N-linked (GlcNAc...) asparagineSequence analysis1

Post-translational modificationi

N-glycosylated.1 Publication
The N-terminus is blocked.Curated1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Expressed by the venom gland.1 Publication

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

3D structure databases

ProteinModelPortaliP86092.
SMRiP86092.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini‹1 – 119Peptidase M12BPROSITE-ProRule annotationAdd BLAST›119
Domaini127 – 213DisintegrinPROSITE-ProRule annotationAdd BLAST87

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi191 – 193D/ECD-tripeptide3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi214 – 324Cys-richAdd BLAST111

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG006978.

Family and domain databases

CDDicd04269. ZnMc_adamalysin_II_like. 1 hit.
Gene3Di3.40.390.10. 1 hit.
4.10.70.10. 1 hit.
InterProiView protein in InterPro
IPR006586. ADAM_Cys-rich.
IPR018358. Disintegrin_CS.
IPR001762. Disintegrin_dom.
IPR036436. Disintegrin_dom_sf.
IPR024079. MetalloPept_cat_dom_sf.
IPR001590. Peptidase_M12B.
IPR034027. Reprolysin_adamalysin.
PfamiView protein in Pfam
PF08516. ADAM_CR. 1 hit.
PF00200. Disintegrin. 1 hit.
PF01421. Reprolysin. 1 hit.
PRINTSiPR00289. DISINTEGRIN.
SMARTiView protein in SMART
SM00608. ACR. 1 hit.
SM00050. DISIN. 1 hit.
SUPFAMiSSF57552. SSF57552. 1 hit.
PROSITEiView protein in PROSITE
PS50215. ADAM_MEPRO. 1 hit.
PS00427. DISINTEGRIN_1. 1 hit.
PS50214. DISINTEGRIN_2. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.

Sequencei

Sequence statusi: Fragment.

P86092-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
DTVLLNRISH DNAQLLAIVF NENVIGKAYT GGMCDPRYSV GVVMDHSPIN
60 70 80 90 100
RLVADTMAHE MGHNLGIHHD TGSCSCGGHS CIMSRVISHQ PLQYFSNCSY
110 120 130 140 150
IEYWDFITKL NPQCILNEPL RTDIVSPPVC GNELLEMGEE CDCGSPRNCR
160 170 180 190 200
DLCCDAATCK LHSWVECESG ECCDQCRFIK AGNVCRPPRK ECDVAEACTG
210 220 230 240 250
QSAQCPTDDF KRNGQPCLNN YAYCYQGNCP IMYHQCYALF GSDATMAQDS
260 270 280 290 300
CFQVNKKGNE YFYCRLENGI NIPCAQEDVK CGRLFCHNMK YEQDCNYSDR
310 320
GMVDNGTKCA EGKVCNSNRQ AYQR
Length:324
Mass (Da):36,262
Last modified:February 10, 2009 - v1
Checksum:i7A6F2716C810BC09
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11 Publication1

Similar proteinsi

Entry informationi

Entry nameiVM3LB_BOTLC
AccessioniPrimary (citable) accession number: P86092
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: February 10, 2009
Last modified: November 22, 2017
This is version 39 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families