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G9I929

- VKTA_MICTN

UniProt

G9I929 - VKTA_MICTN

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Protein

Kunitz-type neurotoxin MitTx-alpha

Gene
N/A
Organism
Micrurus tener tener (Texas coral snake)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

This heterodimeric toxin potently activates mouse acid-sensing ion channel ASIC1/ACCN2 expressed in Xenopus oocytes. Both alternatively spliced isoforms ASIC1a and ASIC1b are activated, with a higher potency for ASIC1a (EC(50)=9.4 nM) vs ASIC1b (EC(50)=23 nM). The ASIC3/ACCN3 subtype is also sensitive to the heterodimer, but with a lower potency (EC(50)=830 nM). On ASIC2a/ACCN1, the toxin shows a very weak activation, but produces a remarkable potentiation (>100-fold) of protons when the extracellular pH drops below neutrality. The toxin interacts with the extracellular region of the channel, since responses are only observed in the outside-out configuration. In vivo, the heterodimer elicits robust pain-related behavior in mice by activation of ASIC1/ACCN2 channels on capsaicin-sensitive nerve fibers.1 Publication

GO - Molecular functioni

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

Keywords - Molecular functioni

Ion channel impairing toxin, Neurotoxin, Protease inhibitor, Serine protease inhibitor, Toxin

Protein family/group databases

MEROPSiI02.065.

Names & Taxonomyi

Protein namesi
Recommended name:
Kunitz-type neurotoxin MitTx-alpha
OrganismiMicrurus tener tener (Texas coral snake)
Taxonomic identifieri1114302 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeElapinaeMicrurus

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Add
BLAST
Chaini25 – 8460Kunitz-type neurotoxin MitTx-alphaPRO_5000828217Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei25 – 251Pyrrolidone carboxylic acid1 Publication
Disulfide bondi31 ↔ 82PROSITE-ProRule annotation
Disulfide bondi41 ↔ 65PROSITE-ProRule annotation
Disulfide bondi57 ↔ 78PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta chains.1 Publication

Structurei

Secondary structure

1
84
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi29 – 324Combined sources
Beta strandi45 – 517Combined sources
Turni52 – 554Combined sources
Beta strandi56 – 627Combined sources
Beta strandi67 – 693Combined sources
Beta strandi72 – 743Combined sources
Helixi75 – 839Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4NTWX-ray2.07B25-84[»]
4NTXX-ray2.27B25-84[»]
4NTYX-ray2.65B25-84[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 8252BPTI/Kunitz inhibitorPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Signal

Family and domain databases

Gene3Di4.10.410.10. 1 hit.
InterProiIPR002223. Prot_inh_Kunz-m.
[Graphical view]
PfamiPF00014. Kunitz_BPTI. 1 hit.
[Graphical view]
SMARTiSM00131. KU. 1 hit.
[Graphical view]
SUPFAMiSSF57362. SSF57362. 1 hit.
PROSITEiPS50279. BPTI_KUNITZ_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

G9I929-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSGGLLLLL GLLTLCAELT PVSSQIRPAF CYEDPPFFQK CGAFVDSYYF
60 70 80
NRSRITCVHF FYGQCDVNQN HFTTMSECNR VCHG
Length:84
Mass (Da):9,498
Last modified:February 22, 2012 - v1
Checksum:i7D5C274A6ABDA89D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
JN613325 mRNA. Translation: AET85559.1.

Cross-referencesi

Web resourcesi

Protein Spotlight

The poison in pain - Issue 140 of July 2012

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
JN613325 mRNA. Translation: AET85559.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4NTW X-ray 2.07 B 25-84 [» ]
4NTX X-ray 2.27 B 25-84 [» ]
4NTY X-ray 2.65 B 25-84 [» ]
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi I02.065.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 4.10.410.10. 1 hit.
InterProi IPR002223. Prot_inh_Kunz-m.
[Graphical view ]
Pfami PF00014. Kunitz_BPTI. 1 hit.
[Graphical view ]
SMARTi SM00131. KU. 1 hit.
[Graphical view ]
SUPFAMi SSF57362. SSF57362. 1 hit.
PROSITEi PS50279. BPTI_KUNITZ_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "A heteromeric Texas coral snake toxin targets acid-sensing ion channels to produce pain."
    Bohlen C.J., Chesler A.T., Sharif-Naeini R., Medzihradszky K.F., Zhou S., King D., Sanchez E.E., Burlingame A.L., Basbaum A.I., Julius D.
    Nature 479:410-414(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBUNIT, PYROGLUTAMATE FORMATION AT GLN-25.
    Tissue: Venom and Venom gland.

Entry informationi

Entry nameiVKTA_MICTN
AccessioniPrimary (citable) accession number: G9I929
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2012
Last sequence update: February 22, 2012
Last modified: October 29, 2014
This is version 18 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

This toxin has been studied to probe molecular mechanisms underlying pain sensation. By targeting ASIC1/ACCN2, it reveals an unexpected contribution of this channel to nociception (PubMed:22094702).1 Publication
The heterodimeric toxin does not affect ASIC2b/ACCN1, ASIC4/ACCN4, Kv2.1/KCNB1, Cav3.3/CACNA1I, ENaC/SCNN1A, TRPA1, TRPV1, TRPV3, TRPM8, P2X2/P2RX2, and 5-HT3/HTR3A channels.1 Publication

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3