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G9I929

- VKTA_MICTN

UniProt

G9I929 - VKTA_MICTN

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
  1. 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

    Keywords - Molecular functioni

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

    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-SubCell

    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 – 324
    Beta strandi45 – 517
    Turni52 – 554
    Beta strandi56 – 627
    Beta strandi67 – 693
    Beta strandi72 – 743
    Helixi75 – 839

    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

    MSSGGLLLLL GLLTLCAELT PVSSQIRPAF CYEDPPFFQK CGAFVDSYYF   50
    NRSRITCVHF FYGQCDVNQN HFTTMSECNR VCHG 84
    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...

    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 1, 2014
    This is version 17 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