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P00980

- VKTHA_DENAN

UniProt

P00980 - VKTHA_DENAN

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Protein

Kunitz-type serine protease inhibitor homolog alpha-dendrotoxin

Gene
N/A
Organism
Dendroaspis angusticeps (Eastern green mamba) (Naja angusticeps)
Status
Reviewed - 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=0.4-150 nM) and facilitates neurotransmitter release.2 Publications

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

  1. serine-type endopeptidase inhibitor activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

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

Protein family/group databases

MEROPSiI02.056.

Names & Taxonomyi

Protein namesi
Recommended name:
Kunitz-type serine protease inhibitor homolog alpha-dendrotoxin
Short name:
Alpha-DTX
Alternative name(s):
Protease inhibitor 1 homolog
Toxin C13S2C3
Venom basic protease inhibitor 1 homolog
OrganismiDendroaspis angusticeps (Eastern green mamba) (Naja angusticeps)
Taxonomic identifieri8618 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeElapinaeDendroaspis

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Toxic dosei

LD50 is 23 mg/kg by intravenous injection.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 5959Kunitz-type serine protease inhibitor homolog alpha-dendrotoxinPRO_0000155433Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11Pyrrolidone carboxylic acid1 Publication
Disulfide bondi7 ↔ 571 PublicationPROSITE-ProRule annotation
Disulfide bondi16 ↔ 401 PublicationPROSITE-ProRule annotation
Disulfide bondi32 ↔ 531 PublicationPROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Expressioni

Tissue specificityi

Expressed by the venom gland.

Structurei

Secondary structure

1
59
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 84
Beta strandi15 – 173
Beta strandi20 – 267
Turni27 – 304
Beta strandi31 – 377
Beta strandi47 – 493
Helixi50 – 578

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DTXX-ray2.20A2-59[»]
ProteinModelPortaliP00980.
SMRiP00980. Positions 1-59.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00980.

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. Prot_inh_Kunz-m.
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.

P00980-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
QPRRKLCILH RNPGRCYDKI PAFYYNQKKK QCERFDWSGC GGNSNRFKTI

EECRRTCIG
Length:59
Mass (Da):7,071
Last modified:July 21, 1986 - v1
Checksum:i96B60752E8AD81AE
GO

Sequence databases

PIRiA01212. VIEPIA.

Cross-referencesi

Sequence databases

PIRi A01212. VIEPIA.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DTX X-ray 2.20 A 2-59 [» ]
ProteinModelPortali P00980.
SMRi P00980. Positions 1-59.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi I02.056.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG006193.

Miscellaneous databases

EvolutionaryTracei P00980.

Family and domain databases

Gene3Di 4.10.410.10. 1 hit.
InterProi IPR002223. Prot_inh_Kunz-m.
IPR020901. Prtase_inh_Kunz-CS.
[Graphical view ]
Pfami PF00014. Kunitz_BPTI. 1 hit.
[Graphical view ]
PRINTSi PR00759. BASICPTASE.
SMARTi SM00131. KU. 1 hit.
[Graphical view ]
SUPFAMi SSF57362. SSF57362. 1 hit.
PROSITEi PS00280. BPTI_KUNITZ_1. 1 hit.
PS50279. BPTI_KUNITZ_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Snake venoms. The amino acid sequences of two proteinase inhibitor homologues from Dendroaspis angusticeps venom."
    Joubert F.J., Taljaard N.
    Hoppe-Seyler's Z. Physiol. Chem. 361:661-674(1980) [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, FUNCTION.
  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, FUNCTION, SITE LYS-5; LEU-9 AND LYS-19.
  4. "Crystal structure of alpha-dendrotoxin from the green mamba venom and its comparison with the structure of bovine pancreatic trypsin inhibitor."
    Skarzynski T.
    J. Mol. Biol. 224:671-683(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

Entry informationi

Entry nameiVKTHA_DENAN
AccessioniPrimary (citable) accession number: P00980
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 29, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Does not inhibit serine proteases and voltage-gated potassium channels Kvl.3/KCNA3, Kv1.4/KCNA4, Kv1.5/KCNA5, Kv3.1/KCNC1, Kv3.4/KCNC4, and Kv4.1/KCND1.

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

External Data

Dasty 3