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Kunitz-type neurotoxin MitTx-alpha

 VKTA_MICTN              Reviewed;          84 AA.
G9I929;
18-APR-2012, integrated into UniProtKB/Swiss-Prot.
22-FEB-2012, sequence version 1.
22-NOV-2017, entry version 28.
RecName: Full=Kunitz-type neurotoxin MitTx-alpha {ECO:0000303|PubMed:22094702};
Flags: Precursor;
Micrurus tener tener (Texas coral snake).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Elapidae; Elapinae; Micrurus.
NCBI_TaxID=1114302;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-50 AND 59-67,
FUNCTION, SUBUNIT, AND PYROGLUTAMATE FORMATION AT GLN-25.
TISSUE=Venom, and Venom gland;
PubMed=22094702; DOI=10.1038/nature10607;
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.;
"A heteromeric Texas coral snake toxin targets acid-sensing ion
channels to produce pain.";
Nature 479:410-414(2011).
[2]
X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) OF 25-84 IN COMPLEX WITH
MITTX-BETA AND THE CHICKEN ASIC1 IN AN OPEN STATE, DISULFIDE BONDS,
AND FUNCTION.
PubMed=24507937; DOI=10.1016/j.cell.2014.01.011;
Baconguis I., Bohlen C.J., Goehring A., Julius D., Gouaux E.;
"X-ray structure of acid-sensing ion channel 1-snake toxin complex
reveals open state of a Na(+)-selective channel.";
Cell 156:717-729(2014).
-!- FUNCTION: MitTx, a heteromeric complex between Kunitz- and
phospholipase-A2-like proteins, potently, persistently and
selectively activates rat and chicken acid-sensing ion channel
ASIC1 (PubMed:22094702, PubMed:24507937). Both alternatively
spliced rat isoforms ASIC1a and ASIC1b are activated, with a
higher potency for ASIC1a (EC(50)=9.4 nM) vs ASIC1b (EC(50)=23 nM)
(PubMed:22094702). The rat ASIC3 subtype is also sensitive to the
heterodimer, but with a lower potency (EC(50)=830 nM)
(PubMed:22094702). On rat ASIC2a, the toxin shows a very weak
activation, but produces a remarkable potentiation (>100-fold) of
protons when the extracellular pH drops below neutrality
(PubMed:22094702). Moderate and weak activations are also observed
on the heterotrimers Asic1a-Asic2a and Asic1a-Asic3 (expressed in
CHO cells), respectively (PubMed:22094702). The binding sites of
the beta subunit of MitTx and the spider psalmotoxin-1 overlap,
explaining why these toxins are mutually exclusive
(PubMed:22094702. PubMed:24507937). In vivo, the heterodimer
elicits robust pain-related behavior in mice by activation of
ASIC1 channels on capsaicin-sensitive nerve fibers
(PubMed:22094702). {ECO:0000269|PubMed:22094702,
ECO:0000269|PubMed:24507937}.
-!- SUBUNIT: Heterodimer of an alpha (Kunitz-type) and a beta
(phospholipase A2 homolog) chains; non-covalently-linked.
{ECO:0000269|PubMed:22094702}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22094702}.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
{ECO:0000305|PubMed:22094702}.
-!- DOMAIN: The toxin-channel complex has a triskelion-like shape with
one toxin heterodimer radiating from each ASIC1 subunit. Toxin
subunits protrude from the edges of the channel trimer, with each
heterodimer interacting almost exclusively with a single subunit.
{ECO:0000269|PubMed:24507937}.
-!- MISCELLANEOUS: The heterodimeric toxin does not affect ASIC2b,
ASIC4, Asic2a-Asic3 heterotrimer, Kv2.1/KCNB1, Cav3.3/CACNA1I,
ENaC alpha/beta/gamma (SCNN1A/SCNN1B/SCNN1G), TRPA1, TRPV1, TRPV3,
TRPM8, P2X2/P2RX2, and 5-HT3/HTR3A channels.
{ECO:0000305|PubMed:22094702}.
-!- SIMILARITY: Belongs to the venom Kunitz-type family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Protein Spotlight; Note=The poison in pain
- Issue 140 of July 2012;
URL="https://web.expasy.org/spotlight/back_issues/140";
-----------------------------------------------------------------------
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EMBL; JN613325; AET85559.1; -; mRNA.
PDB; 4NTW; X-ray; 2.07 A; B=25-84.
PDB; 4NTX; X-ray; 2.27 A; B=25-84.
PDB; 4NTY; X-ray; 2.65 A; B=25-84.
PDBsum; 4NTW; -.
PDBsum; 4NTX; -.
PDBsum; 4NTY; -.
SMR; G9I929; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
Gene3D; 4.10.410.10; -; 1.
InterPro; IPR002223; Kunitz_BPTI.
InterPro; IPR036880; Kunitz_BPTI_sf.
Pfam; PF00014; Kunitz_BPTI; 1.
SMART; SM00131; KU; 1.
SUPFAM; SSF57362; SSF57362; 1.
PROSITE; PS50279; BPTI_KUNITZ_2; 1.
1: Evidence at protein level;
3D-structure; Direct protein sequencing; Disulfide bond;
Ion channel impairing toxin; Protease inhibitor;
Proton-gated sodium channel impairing toxin;
Pyrrolidone carboxylic acid; Secreted; Serine protease inhibitor;
Signal; Toxin.
SIGNAL 1 24 {ECO:0000269|PubMed:22094702}.
CHAIN 25 84 Kunitz-type neurotoxin MitTx-alpha.
{ECO:0000305|PubMed:22094702}.
/FTId=PRO_5000828217.
DOMAIN 31 82 BPTI/Kunitz inhibitor.
{ECO:0000255|PROSITE-ProRule:PRU00031}.
MOD_RES 25 25 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:22094702}.
DISULFID 31 82 {ECO:0000269|PubMed:24507937,
ECO:0000312|PDB:4NTW,
ECO:0000312|PDB:4NTX,
ECO:0000312|PDB:4NTY}.
DISULFID 41 65 {ECO:0000269|PubMed:24507937,
ECO:0000312|PDB:4NTW,
ECO:0000312|PDB:4NTX,
ECO:0000312|PDB:4NTY}.
DISULFID 57 78 {ECO:0000269|PubMed:24507937,
ECO:0000312|PDB:4NTW,
ECO:0000312|PDB:4NTX,
ECO:0000312|PDB:4NTY}.
HELIX 29 32 {ECO:0000244|PDB:4NTW}.
STRAND 45 51 {ECO:0000244|PDB:4NTW}.
TURN 52 55 {ECO:0000244|PDB:4NTW}.
STRAND 56 62 {ECO:0000244|PDB:4NTW}.
STRAND 67 69 {ECO:0000244|PDB:4NTW}.
STRAND 72 74 {ECO:0000244|PDB:4NTW}.
HELIX 75 83 {ECO:0000244|PDB:4NTW}.
SEQUENCE 84 AA; 9498 MW; 7D5C274A6ABDA89D CRC64;
MSSGGLLLLL GLLTLCAELT PVSSQIRPAF CYEDPPFFQK CGAFVDSYYF NRSRITCVHF
FYGQCDVNQN HFTTMSECNR VCHG


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