VKT_OXYMI
ID VKT_OXYMI Reviewed; 17 AA.
AC P0DJ63;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 25-MAY-2022, entry version 18.
DE RecName: Full=Kunitz-type serine protease inhibitor OMI;
DE Flags: Fragment;
OS Oxyuranus microlepidotus (Inland taipan) (Diemenia microlepidota).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Acanthophiinae; Oxyuranus.
OX NCBI_TaxID=111177;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=21843588; DOI=10.1016/j.biochi.2011.08.003;
RA Earl S.T., Richards R., Johnson L.A., Flight S., Anderson S., Liao A.,
RA de Jersey J., Masci P.P., Lavin M.F.;
RT "Identification and characterisation of Kunitz-type plasma kallikrein
RT inhibitors unique to Oxyuranus sp. snake venoms.";
RL Biochimie 94:365-373(2012).
CC -!- FUNCTION: Serine protease inhibitor that inhibits plasma kallikrein
CC (Ki=1.7 nM), and plasmin (Ki=33.0 nM). {ECO:0000269|PubMed:21843588}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21843588}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:21843588}.
CC -!- SIMILARITY: Belongs to the venom Kunitz-type family. {ECO:0000305}.
CC -!- CAUTION: Attempts to clone the transcript coding for this protein
CC failed. {ECO:0000305}.
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DR AlphaFoldDB; P0DJ63; -.
DR PRIDE; P0DJ63; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Protease inhibitor; Secreted;
KW Serine protease inhibitor; Toxin.
FT CHAIN 1..>17
FT /note="Kunitz-type serine protease inhibitor OMI"
FT /id="PRO_0000413846"
FT DOMAIN 4..>17
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT SITE 14..15
FT /note="Reactive bond for trypsin"
FT /evidence="ECO:0000250"
FT DISULFID 4..?
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 13..?
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT NON_TER 17
SQ SEQUENCE 17 AA; 1850 MW; 3315988A299DB1ED CRC64;
KDFCHLPPKP GPCRAAI