ID   BPT2_BOVIN              Reviewed;         100 AA.
AC   P04815;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 2.
DT   25-MAY-2022, entry version 116.
DE   RecName: Full=Spleen trypsin inhibitor I;
DE            Short=SI-I;
DE   Contains:
DE     RecName: Full=Spleen trypsin inhibitor II;
DE              Short=SI-II;
DE   Contains:
DE     RecName: Full=Spleen trypsin inhibitor III;
DE              Short=SI-III;
DE   Flags: Precursor;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2441071; DOI=10.1016/0022-2836(87)90711-x;
RA   Creighton T.E., Charles I.G.;
RT   "Sequences of the genes and polypeptide precursors for two bovine protease
RT   inhibitors.";
RL   J. Mol. Biol. 194:11-22(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2456884; DOI=10.1101/sqb.1987.052.01.058;
RA   Creighton T.E., Charles I.G.;
RT   "Biosynthesis, processing, and evolution of bovine pancreatic trypsin
RT   inhibitor.";
RL   Cold Spring Harb. Symp. Quant. Biol. 52:511-519(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE OF 34-97.
RX   PubMed=2420326; DOI=10.1042/bj2330443;
RA   Kingston I.B., Anderson S.;
RT   "Sequences encoding two trypsin inhibitors occur in strikingly similar
RT   genomic environments.";
RL   Biochem. J. 233:443-450(1986).
RN   [4]
RP   PROTEIN SEQUENCE OF 34-99.
RX   PubMed=2462435;
RA   Fioretti E., Angeletti M., Fiorucci L., Barra D., Bossa F., Ascoli F.;
RT   "Aprotinin-like isoinhibitors in bovine organs.";
RL   Biol. Chem. Hoppe-Seyler 369:37-42(1988).
RN   [5]
RP   PROTEIN SEQUENCE OF 34-99.
RC   TISSUE=Spleen;
RX   PubMed=3654647; DOI=10.1016/s0021-9258(18)47881-7;
RA   Barra D., Simmaco M., Bossa F., Fioretti E., Angeletti M., Ascoli F.;
RT   "Primary structure of a protease isoinhibitor from bovine spleen. A
RT   possible intermediate in the processing of the primary gene product.";
RL   J. Biol. Chem. 262:13916-13919(1987).
RN   [6]
RP   PROTEIN SEQUENCE OF 36-93.
RC   TISSUE=Spleen;
RX   PubMed=2413011; DOI=10.1016/s0021-9258(17)39049-x;
RA   Fioretti E., Iacopino G., Angeletti M., Barra D., Bossa F., Ascoli F.;
RT   "Primary structure and antiproteolytic activity of a Kunitz-type inhibitor
RT   from bovine spleen.";
RL   J. Biol. Chem. 260:11451-11455(1985).
RN   [7]
RP   PROTEIN SEQUENCE OF 36-97.
RC   TISSUE=Spleen;
RX   PubMed=1986787; DOI=10.1016/0167-4838(91)90231-n;
RA   Barra D., Fioretti E., Angeletti M., Maras B., Bossa F., Ascoli F.;
RT   "Proteinase isoinhibitors from bovine spleen: primary structure of an
RT   intermediate in the processing of the precursor.";
RL   Biochim. Biophys. Acta 1076:143-147(1991).
CC   -!- SUBCELLULAR LOCATION: Secreted.
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DR   EMBL; M20935; AAA51418.1; -; Genomic_DNA.
DR   EMBL; M20931; AAA51418.1; JOINED; Genomic_DNA.
DR   EMBL; M20933; AAA51418.1; JOINED; Genomic_DNA.
DR   EMBL; X05275; CAA28887.1; -; mRNA.
DR   EMBL; X06685; CAA29881.1; -; Genomic_DNA.
DR   EMBL; X03366; CAA27064.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; X03366; CAA27065.1; -; Genomic_DNA.
DR   PIR; S00274; TIBOSP.
DR   RefSeq; NP_991355.1; NM_205786.1.
DR   AlphaFoldDB; P04815; -.
DR   SMR; P04815; -.
DR   STRING; 9913.ENSBTAP00000023042; -.
DR   MEROPS; I02.002; -.
DR   PaxDb; P04815; -.
DR   PRIDE; P04815; -.
DR   GeneID; 404103; -.
DR   KEGG; bta:404103; -.
DR   eggNOG; KOG3540; Eukaryota.
DR   OrthoDB; 1533593at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
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;
KW   Reference proteome; Secreted; Serine protease inhibitor; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..33
FT                   /id="PRO_0000016855"
FT   CHAIN           34..99
FT                   /note="Spleen trypsin inhibitor I"
FT                   /id="PRO_0000016856"
FT   CHAIN           36..97
FT                   /note="Spleen trypsin inhibitor III"
FT                   /id="PRO_0000016857"
FT   CHAIN           36..93
FT                   /note="Spleen trypsin inhibitor II"
FT                   /id="PRO_0000016858"
FT   PROPEP          100
FT                   /id="PRO_0000016859"
FT   DOMAIN          40..90
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   SITE            50..51
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   DISULFID        40..90
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        49..73
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        65..86
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ   SEQUENCE   100 AA;  10843 MW;  39069734B8ACF4E3 CRC64;
     MKMSRLCLSI ALLVLLGTLA ASTPGCDTSN QAKAQRPDFC LEPPYTGPCK AKMIRYFYNA
     KAGFCETFVY GGCKAKSNNF RSAEDCMRTC GGAIGPRENL