ID   VKT12_DENAN             Reviewed;          59 AA.
AC   P0DMJ6;
DT   11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT   11-JUN-2014, sequence version 1.
DT   25-MAY-2022, entry version 20.
DE   RecName: Full=Kunitz-type serine protease inhibitor dendrotoxin DaE1;
DE   Contains:
DE     RecName: Full=Kunitz-type protease inhibitor dendrotoxin DaE2;
OS   Dendroaspis angusticeps (Eastern green mamba) (Naja angusticeps).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Dendroaspis.
OX   NCBI_TaxID=8618;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=11240130; DOI=10.1016/s0014-5793(01)02201-3;
RA   Tytgat J., Vandenberghe I., Ulens C., Van Beeumen J.;
RT   "New polypeptide components purified from mamba venom.";
RL   FEBS Lett. 491:217-221(2001).
CC   -!- FUNCTION: DaE1 and DaE2 are serine protease inhibitors that inhibit
CC       voltage-gated potassium channels Kv1.1/KCNA1 channels (IC(50)=300 nM).
CC       {ECO:0000269|PubMed:11240130}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MASS SPECTROMETRY: [Kunitz-type serine protease inhibitor dendrotoxin
CC       DaE1]: Mass=6631.5; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:11240130};
CC   -!- MASS SPECTROMETRY: [Kunitz-type protease inhibitor dendrotoxin DaE2]:
CC       Mass=6389.0; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:11240130};
CC   -!- MISCELLANEOUS: Neither DaE1 nor DaE2 affect Kir2.1/KCNJ2 channels.
CC   -!- SIMILARITY: Belongs to the venom Kunitz-type family. {ECO:0000305}.
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DR   AlphaFoldDB; P0DMJ6; -.
DR   BMRB; P0DMJ6; -.
DR   SMR; P0DMJ6; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   CDD; cd00109; KU; 1.
DR   Gene3D; 4.10.410.10; -; 1.
DR   InterPro; IPR002223; Kunitz_BPTI.
DR   InterPro; IPR036880; Kunitz_BPTI_sf.
DR   InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR   Pfam; PF00014; Kunitz_BPTI; 1.
DR   PRINTS; PR00759; BASICPTASE.
DR   SMART; SM00131; KU; 1.
DR   SUPFAM; SSF57362; SSF57362; 1.
DR   PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR   PROSITE; PS50279; BPTI_KUNITZ_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Potassium channel impairing toxin; Protease inhibitor; Secreted;
KW   Serine protease inhibitor; Toxin;
KW   Voltage-gated potassium channel impairing toxin.
FT   CHAIN           1..59
FT                   /note="Kunitz-type serine protease inhibitor dendrotoxin
FT                   DaE1"
FT                   /id="PRO_0000429468"
FT   CHAIN           3..59
FT                   /note="Kunitz-type protease inhibitor dendrotoxin DaE2"
FT                   /id="PRO_0000429469"
FT   DOMAIN          7..57
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   SITE            17..18
FT                   /note="Reactive bond for trypsin"
FT                   /evidence="ECO:0000250"
FT   DISULFID        7..57
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        16..40
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        32..53
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ   SEQUENCE   59 AA;  6639 MW;  E87BFBECD5E90276 CRC64;
     LQHRTFCKLP AEPGPCKASI PAFYYNWAAK KCQLFHYGGC KGNANRFSTI EKCRRACVG