ID   VKTRE_DENAN             Reviewed;          59 AA.
AC   Q7LZS8;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Kunitz-type serine protease inhibitor long epsilon-dendrotoxin Arg55;
DE   Contains:
DE     RecName: Full=Kunitz-type serine protease inhibitor short epsilon-dendrotoxin Arg55;
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, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=11711127; DOI=10.1016/s0041-0101(01)00227-6;
RA   Sigle R., Hackett M., Aird S.D.;
RT   "Primary structures of four trypsin inhibitor E homologs from venom of
RT   Dendroaspis angusticeps: structure-function comparisons with other
RT   dendrotoxin homologs.";
RL   Toxicon 40:297-308(2002).
CC   -!- FUNCTION: Serine protease inhibitor that inhibits trypsin.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MASS SPECTROMETRY: [Kunitz-type serine protease inhibitor long epsilon-
CC       dendrotoxin Arg55]: Mass=7124; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:11711127};
CC   -!- MASS SPECTROMETRY: [Kunitz-type serine protease inhibitor short
CC       epsilon-dendrotoxin Arg55]: Mass=6883; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:11711127};
CC   -!- SIMILARITY: Belongs to the venom Kunitz-type family. {ECO:0000305}.
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DR   PIR; A59399; A59399.
DR   AlphaFoldDB; Q7LZS8; -.
DR   BMRB; Q7LZS8; -.
DR   SMR; Q7LZS8; -.
DR   MEROPS; I02.056; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor 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; Protease inhibitor;
KW   Secreted; Serine protease inhibitor.
FT   CHAIN           1..59
FT                   /note="Kunitz-type serine protease inhibitor long epsilon-
FT                   dendrotoxin Arg55"
FT                   /id="PRO_0000016867"
FT   CHAIN           3..59
FT                   /note="Kunitz-type serine protease inhibitor short epsilon-
FT                   dendrotoxin Arg55"
FT                   /id="PRO_0000016868"
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