ID   VKTE_DENPO              Reviewed;          59 AA.
AC   P00984;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Kunitz-type serine protease inhibitor dendrotoxin E;
DE            Short=DTX-E;
DE   AltName: Full=Venom basic protease inhibitor E;
OS   Dendroaspis polylepis polylepis (Black mamba).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Dendroaspis.
OX   NCBI_TaxID=8620;
RN   [1]
RP   PROTEIN SEQUENCE, AND FUNCTION.
RC   TISSUE=Venom;
RX   PubMed=668688; DOI=10.1111/j.1432-1033.1978.tb12366.x;
RA   Joubert F.J., Strydom D.J.;
RT   "Snake venoms. The amino-acid sequence of trypsin inhibitor E of
RT   Dendroaspis polylepis polylepis (black mamba) venom.";
RL   Eur. J. Biochem. 87:191-198(1978).
CC   -!- FUNCTION: Serine protease inhibitor that inhibits trypsin (Kd=1 nM) and
CC       chymotrypsin (Kd=100 nM). May also inhibit voltage-gated potassium
CC       channels (Kv). Binds transition metal ions such as copper and cobalt.
CC       {ECO:0000269|PubMed:668688}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the venom Kunitz-type family. {ECO:0000305}.
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DR   PIR; A01215; TIEPED.
DR   AlphaFoldDB; P00984; -.
DR   BMRB; P00984; -.
DR   SMR; P00984; -.
DR   MEROPS; I02.056; -.
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   Copper; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Potassium channel impairing toxin;
KW   Protease inhibitor; Secreted; Serine protease inhibitor; Toxin;
KW   Voltage-gated potassium channel impairing toxin.
FT   CHAIN           1..59
FT                   /note="Kunitz-type serine protease inhibitor dendrotoxin E"
FT                   /id="PRO_0000155436"
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;  6620 MW;  E87BFBECC0090276 CRC64;
     LQHRTFCKLP AEPGPCKASI PAFYYNWAAK KCQLFHYGGC KGNANRFSTI EKCRHACVG