ID   VKT2_PSETT              Reviewed;          83 AA.
AC   Q90WA0; B5L5Q0;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=Kunitz-type serine protease inhibitor textilinin-2;
DE            Short=Txln-2;
DE   Flags: Precursor;
OS   Pseudonaja textilis textilis (Eastern brown snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Acanthophiinae; Pseudonaja.
OX   NCBI_TaxID=169397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   TISSUE=Venom gland;
RX   PubMed=12406072; DOI=10.1046/j.1365-2141.2002.03878.x;
RA   Filippovich I., Sorokina N., Masci P.P., de Jersey J., Whitaker A.N.,
RA   Winzor D.J., Gaffney P.J., Lavin M.F.;
RT   "A family of textilinin genes, two of which encode proteins with
RT   antihaemorrhagic properties.";
RL   Br. J. Haematol. 119:376-384(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Venom gland;
RX   PubMed=18979207; DOI=10.1007/s00018-008-8573-5;
RA   St Pierre L., Earl S.T., Filippovich I., Sorokina N., Masci P.P.,
RA   De Jersey J., Lavin M.F.;
RT   "Common evolution of waprin and Kunitz-like toxin families in Australian
RT   venomous snakes.";
RL   Cell. Mol. Life Sci. 65:4039-4054(2008).
RN   [3]
RP   PROTEIN SEQUENCE OF 25-83, FUNCTION, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=10847427; DOI=10.1097/00001721-200006000-00011;
RA   Masci P.P., Whitaker A.N., Sparrow L.G., de Jersey J., Winzor D.J.,
RA   Watters D.J., Lavin M.F., Gaffney P.J.;
RT   "Textilinins from Pseudonaja textilis textilis. Characterization of two
RT   plasmin inhibitors that reduce bleeding in an animal model.";
RL   Blood Coagul. Fibrinolysis 11:385-393(2000).
CC   -!- FUNCTION: Serine protease inhibitor that inhibits plasmin (Ki=2.2 nM),
CC       and reduces blood loss in the mouse tail vein blood loss model.
CC       {ECO:0000269|PubMed:10847427, ECO:0000269|PubMed:12406072}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MASS SPECTROMETRY: Mass=6682.4; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:10847427};
CC   -!- SIMILARITY: Belongs to the venom Kunitz-type family. {ECO:0000305}.
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DR   EMBL; AF402325; AAK95520.1; -; mRNA.
DR   EMBL; EU401838; ACC77787.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q90WA0; -.
DR   SMR; Q90WA0; -.
DR   MEROPS; I02.052; -.
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   Direct protein sequencing; Disulfide bond; Protease inhibitor; Secreted;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:10847427"
FT   CHAIN           25..83
FT                   /note="Kunitz-type serine protease inhibitor textilinin-2"
FT                   /id="PRO_5000395638"
FT   DOMAIN          31..81
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   SITE            41..42
FT                   /note="Reactive bond for trypsin"
FT                   /evidence="ECO:0000250"
FT   DISULFID        31..81
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        40..64
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        56..77
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ   SEQUENCE   83 AA;  9179 MW;  67E589AD27175930 CRC64;
     MSSGGLLLLL GLLTLWEVLT PVSSKDRPEL CELPPDTGPC RVRFPSFYYN PDEQKCLEFI
     YGGCEGNANN FITKEECEST CAA