ID   VKT_AUSLA               Reviewed;         252 AA.
AC   B2BS84;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   25-MAY-2022, entry version 43.
DE   RecName: Full=Putative Kunitz-type serine protease inhibitor;
DE   Flags: Precursor;
OS   Austrelaps labialis (Pygmy copperhead) (Denisonia superba).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Acanthophiinae; Austrelaps.
OX   NCBI_TaxID=471292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=18307759; DOI=10.1186/1471-2148-8-70;
RA   Doley R., Tram N.N.B., Reza M.A., Kini R.M.;
RT   "Unusual accelerated rate of deletions and insertions in toxin genes in the
RT   venom glands of the pygmy copperhead (Austrelaps labialis) from Kangaroo
RT   island.";
RL   BMC Evol. Biol. 8:70-70(2008).
CC   -!- FUNCTION: Serine protease inhibitor. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the venom Kunitz-type family. {ECO:0000305}.
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DR   EMBL; EU012449; ABW90603.1; -; mRNA.
DR   AlphaFoldDB; B2BS84; -.
DR   SMR; B2BS84; -.
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; 2.
DR   Gene3D; 4.10.410.10; -; 2.
DR   InterPro; IPR002223; Kunitz_BPTI.
DR   InterPro; IPR036880; Kunitz_BPTI_sf.
DR   InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR   Pfam; PF00014; Kunitz_BPTI; 2.
DR   PRINTS; PR00759; BASICPTASE.
DR   SMART; SM00131; KU; 2.
DR   SUPFAM; SSF57362; SSF57362; 2.
DR   PROSITE; PS00280; BPTI_KUNITZ_1; 2.
DR   PROSITE; PS50279; BPTI_KUNITZ_2; 2.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Protease inhibitor; Repeat; Secreted;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000250"
FT   CHAIN           21..252
FT                   /note="Putative Kunitz-type serine protease inhibitor"
FT                   /id="PRO_0000376867"
FT   DOMAIN          27..77
FT                   /note="BPTI/Kunitz inhibitor 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DOMAIN          118..168
FT                   /note="BPTI/Kunitz inhibitor 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   SITE            37..38
FT                   /note="Reactive bond for trypsin"
FT                   /evidence="ECO:0000250"
FT   SITE            128..129
FT                   /note="Reactive bond for trypsin"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        46
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        27..77
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        36..60
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        52..73
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        118..168
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        127..151
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        143..164
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ   SEQUENCE   252 AA;  27571 MW;  235BA4A5D228151D CRC64;
     MTREKSLALL ITLAAALAAA ESPPGRCHSP KTVGPCRASF HRWRYNATSQ MCQEFIFGGC
     KGNANNFVSK QDCFQTCIRG GAAEATVVPS GPATEVATPR AGHLPEAYEN RPGFREFCAA
     PRVVGPCRAS FLRWYFDLES RMCKMFIYGG CRGNKNNYLF EEHCWSQCTG DGEITEEPGD
     AGAQPPLPSE PFSFSTRAVV LAVLPAILVT ILLGSMGVFF VKICRKNPEL SVGTVWSTLD
     DKEYLMSNAY TL