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Protein

Kunitz-type serine protease inhibitor homolog dendrotoxin I

Gene
N/A
Organism
Dendroaspis polylepis polylepis (Black mamba)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Serine protease inhibitor homolog that blocks voltage-gated potassium channels (Kv1.1/KCNA1, Kv1.2/KCNA2, and Kv1.6/KCNA6) (IC50=0.13-50 nM).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei5 – 51May be the major determinant of the binding affinity for potassium channels
Sitei9 – 91Important for binding to potassium channels
Sitei19 – 191Not important for inhibition of potassium channels

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Ion channel impairing toxin, Neurotoxin, Potassium channel impairing toxin, Toxin, Voltage-gated potassium channel impairing toxin

Names & Taxonomyi

Protein namesi
Recommended name:
Kunitz-type serine protease inhibitor homolog dendrotoxin I
Short name:
DTX-I
Alternative name(s):
Dendrotoxin-1
Venom basic protease inhibitor 1
OrganismiDendroaspis polylepis polylepis (Black mamba)
Taxonomic identifieri8620 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeElapinaeDendroaspis

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Toxic dosei

LD50 is 38 mg/kg by intravenous injection.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 6060Kunitz-type serine protease inhibitor homolog dendrotoxin IPRO_0000155434Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi7 ↔ 57
Disulfide bondi16 ↔ 40
Disulfide bondi32 ↔ 53

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.

Structurei

Secondary structure

1
60
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 73Combined sources
Beta strandi20 – 256Combined sources
Beta strandi29 – 379Combined sources
Beta strandi47 – 493Combined sources
Helixi50 – 578Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DEMNMR-A1-60[»]
1DENNMR-A1-60[»]
ProteinModelPortaliP00979.
SMRiP00979. Positions 1-60.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00979.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 5751BPTI/Kunitz inhibitorPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the venom Kunitz-type family.Curated
Contains 1 BPTI/Kunitz inhibitor domain.PROSITE-ProRule annotation

Phylogenomic databases

HOVERGENiHBG006193.

Family and domain databases

Gene3Di4.10.410.10. 1 hit.
InterProiIPR002223. Kunitz_BPTI.
IPR020901. Prtase_inh_Kunz-CS.
[Graphical view]
PfamiPF00014. Kunitz_BPTI. 1 hit.
[Graphical view]
PRINTSiPR00759. BASICPTASE.
SMARTiSM00131. KU. 1 hit.
[Graphical view]
SUPFAMiSSF57362. SSF57362. 1 hit.
PROSITEiPS00280. BPTI_KUNITZ_1. 1 hit.
PS50279. BPTI_KUNITZ_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00979-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
QPLRKLCILH RNPGRCYQKI PAFYYNQKKK QCEGFTWSGC GGNSNRFKTI
60
EECRRTCIRK
Length:60
Mass (Da):7,155
Last modified:April 1, 1993 - v2
Checksum:i94E5CD5609E7AD81
GO

Sequence databases

PIRiA01211. TIEPVI.

Cross-referencesi

Sequence databases

PIRiA01211. TIEPVI.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DEMNMR-A1-60[»]
1DENNMR-A1-60[»]
ProteinModelPortaliP00979.
SMRiP00979. Positions 1-60.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG006193.

Miscellaneous databases

EvolutionaryTraceiP00979.

Family and domain databases

Gene3Di4.10.410.10. 1 hit.
InterProiIPR002223. Kunitz_BPTI.
IPR020901. Prtase_inh_Kunz-CS.
[Graphical view]
PfamiPF00014. Kunitz_BPTI. 1 hit.
[Graphical view]
PRINTSiPR00759. BASICPTASE.
SMARTiSM00131. KU. 1 hit.
[Graphical view]
SUPFAMiSSF57362. SSF57362. 1 hit.
PROSITEiPS00280. BPTI_KUNITZ_1. 1 hit.
PS50279. BPTI_KUNITZ_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Protease inhibitors as snake venom toxins."
    Strydom D.J.
    Nature New Biol. 243:88-89(1973) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Tissue: Venom.
  2. "Twenty years of dendrotoxins."
    Harvey A.L.
    Toxicon 39:15-26(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  3. "Protease inhibitors from marine venomous animals and their counterparts in terrestrial venomous animals."
    Mourao C.B., Schwartz E.F.
    Mar. Drugs 11:2069-2112(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW, SITE LYS-5; LEU-9 AND LYS-19.
  4. "Novel effects of dendrotoxin homologues on subtypes of mammalian Kv1 potassium channels expressed in Xenopus oocytes."
    Robertson B., Owen D., Stow J., Butler C., Newland C.
    FEBS Lett. 383:26-30(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Sequence-specific 1H-NMR assignment and secondary structure of black mamba dendrotoxin I, a highly selective blocker of voltage-gated potassium channels."
    Foray M.-F., Lancelin J.-M., Hollecker M., Marion D.
    Eur. J. Biochem. 211:813-820(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  6. "Proteinase inhibitor homologues as potassium channel blockers."
    Lancelin J.-M., Foray M.-F., Poncin M.-F., Hollecker M., Marion D.
    Nat. Struct. Biol. 1:246-250(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiVKTH1_DENPO
AccessioniPrimary (citable) accession number: P00979
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1993
Last modified: December 9, 2015
This is version 98 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

Does not inhibit serine proteases.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.