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Kunitz-type serine protease inhibitor homolog alpha-dendrotoxin (Alpha-DTX) (Protease inhibitor 1 homolog) (Toxin C13S2C3) (Venom basic protease inhibitor 1 homolog)

 VKTHA_DENAN             Reviewed;          59 AA.
P00980;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
22-NOV-2017, entry version 107.
RecName: Full=Kunitz-type serine protease inhibitor homolog alpha-dendrotoxin;
Short=Alpha-DTX;
AltName: Full=Protease inhibitor 1 homolog;
AltName: Full=Toxin C13S2C3;
AltName: Full=Venom basic protease inhibitor 1 homolog;
Dendroaspis angusticeps (Eastern green mamba) (Naja angusticeps).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Elapidae; Elapinae; Dendroaspis.
NCBI_TaxID=8618;
[1]
PROTEIN SEQUENCE, AND PYROGLUTAMATE FORMATION AT GLN-1.
TISSUE=Venom;
PubMed=7429422;
Joubert F.J., Taljaard N.;
"Snake venoms. The amino acid sequences of two proteinase inhibitor
homologues from Dendroaspis angusticeps venom.";
Hoppe-Seyler's Z. Physiol. Chem. 361:661-674(1980).
[2]
REVIEW, AND FUNCTION.
PubMed=10936620; DOI=10.1016/S0041-0101(00)00162-8;
Harvey A.L.;
"Twenty years of dendrotoxins.";
Toxicon 39:15-26(2001).
[3]
REVIEW, FUNCTION, AND SITE LYS-5; LEU-9 AND LYS-19.
PubMed=23771044; DOI=10.3390/md11062069;
Mourao C.B., Schwartz E.F.;
"Protease inhibitors from marine venomous animals and their
counterparts in terrestrial venomous animals.";
Mar. Drugs 11:2069-2112(2013).
[4]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
PubMed=1373774; DOI=10.1016/0022-2836(92)90552-U;
Skarzynski T.;
"Crystal structure of alpha-dendrotoxin from the green mamba venom and
its comparison with the structure of bovine pancreatic trypsin
inhibitor.";
J. Mol. Biol. 224:671-683(1992).
-!- FUNCTION: Serine protease inhibitor homolog that blocks voltage-
gated potassium channels (Kv1.1/KCNA1, Kv1.2/KCNA2, and
Kv1.6/KCNA6) (IC(50)=0.4-150 nM) and facilitates neurotransmitter
release. {ECO:0000269|PubMed:10936620,
ECO:0000269|PubMed:23771044}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
-!- TOXIC DOSE: LD(50) is 23 mg/kg by intravenous injection.
-!- 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.
-!- SIMILARITY: Belongs to the venom Kunitz-type family.
{ECO:0000305}.
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PIR; A01212; VIEPIA.
PDB; 1DTX; X-ray; 2.20 A; A=2-59.
PDBsum; 1DTX; -.
ProteinModelPortal; P00980; -.
SMR; P00980; -.
HOVERGEN; HBG006193; -.
EvolutionaryTrace; P00980; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
CDD; cd00109; KU; 1.
Gene3D; 4.10.410.10; -; 1.
InterPro; IPR002223; Kunitz_BPTI.
InterPro; IPR036880; Kunitz_BPTI_sf.
InterPro; IPR020901; Prtase_inh_Kunz-CS.
Pfam; PF00014; Kunitz_BPTI; 1.
PRINTS; PR00759; BASICPTASE.
SMART; SM00131; KU; 1.
SUPFAM; SSF57362; SSF57362; 1.
PROSITE; PS00280; BPTI_KUNITZ_1; 1.
PROSITE; PS50279; BPTI_KUNITZ_2; 1.
1: Evidence at protein level;
3D-structure; Direct protein sequencing; Disulfide bond;
Ion channel impairing toxin; Neurotoxin;
Potassium channel impairing toxin; Pyrrolidone carboxylic acid;
Secreted; Toxin; Voltage-gated potassium channel impairing toxin.
CHAIN 1 59 Kunitz-type serine protease inhibitor
homolog alpha-dendrotoxin.
/FTId=PRO_0000155433.
DOMAIN 7 57 BPTI/Kunitz inhibitor.
{ECO:0000255|PROSITE-ProRule:PRU00031}.
SITE 5 5 May be the major determinant of the
binding affinity for potassium channels.
SITE 9 9 Important for binding to potassium
channels.
SITE 19 19 Not important for inhibition of potassium
channels.
MOD_RES 1 1 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:7429422}.
DISULFID 7 57 {ECO:0000255|PROSITE-ProRule:PRU00031,
ECO:0000269|PubMed:7429422}.
DISULFID 16 40 {ECO:0000255|PROSITE-ProRule:PRU00031,
ECO:0000269|PubMed:7429422}.
DISULFID 32 53 {ECO:0000255|PROSITE-ProRule:PRU00031,
ECO:0000269|PubMed:7429422}.
HELIX 5 8 {ECO:0000244|PDB:1DTX}.
STRAND 15 17 {ECO:0000244|PDB:1DTX}.
STRAND 20 26 {ECO:0000244|PDB:1DTX}.
TURN 27 30 {ECO:0000244|PDB:1DTX}.
STRAND 31 37 {ECO:0000244|PDB:1DTX}.
STRAND 47 49 {ECO:0000244|PDB:1DTX}.
HELIX 50 57 {ECO:0000244|PDB:1DTX}.
SEQUENCE 59 AA; 7071 MW; 96B60752E8AD81AE CRC64;
QPRRKLCILH RNPGRCYDKI PAFYYNQKKK QCERFDWSGC GGNSNRFKTI EECRRTCIG


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