VSPE2_CROAT
ID VSPE2_CROAT Reviewed; 25 AA.
AC Q7LZF6;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Kallikrein-like EII;
DE EC=3.4.21.-;
DE Flags: Fragment;
OS Crotalus atrox (Western diamondback rattlesnake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=8730;
RN [1]
RP PROTEIN SEQUENCE, AND FUNCTION.
RC TISSUE=Venom;
RX PubMed=6355088; DOI=10.1016/s0021-9258(17)44214-1;
RA Bjarnason J.B., Barish A., Direnzo G.S., Campbell R., Fox J.W.;
RT "Kallikrein-like enzymes from Crotalus atrox venom.";
RL J. Biol. Chem. 258:12566-12573(1983).
CC -!- FUNCTION: Cleaves a kininogen analog to release bradykinin.
CC {ECO:0000269|PubMed:6355088}.
CC -!- ACTIVITY REGULATION: Inhibited by aprotinin and PMSF, but not by EDTA.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MISCELLANEOUS: Does not have plasmin or fibrinolytic activity.
CC {ECO:0000305|PubMed:6355088}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR PIR; B20596; B20596.
DR AlphaFoldDB; Q7LZF6; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Protease; Secreted; Serine protease;
KW Toxin.
FT CHAIN 1..>25
FT /note="Kallikrein-like EII"
FT /id="PRO_0000407588"
FT DOMAIN 1..>25
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT NON_TER 25
SQ SEQUENCE 25 AA; 2881 MW; 3F3C8B5ABA619B6E CRC64;
HVGGDECNIN EHRSLVAIFV FTEFF