ID   IBPC_BOVIN              Reviewed;          67 AA.
AC   P00976;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 2.
DT   11-DEC-2019, entry version 87.
DE   RecName: Full=Colostrum trypsin inhibitor;
DE   AltName: Full=Colostrum BPI;
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   PROTEIN SEQUENCE.
RA   Cechova D., Jonakova V., Sorm F.;
RT   "Primary structure of trypsin inhibitor from cow colostrum (component
RT   B2).";
RL   Collect. Czech. Chem. Commun. 36:3342-3357(1971).
RN   [2]
RP   DISULFIDE BONDS.
RA   Cechova D., Ber E.;
RT   "Disulfide bonds of trypsin inhibitor from cow colostrum.";
RL   Collect. Czech. Chem. Commun. 39:680-688(1974).
RN   [3]
RP   CHARACTERIZATION.
RX   PubMed=11947537; DOI=10.1016/0014-5793(70)80230-7;
RA   Cechova D., Muszynska G.;
RT   "Role of lysine 18 in active center of cow colostrum trypsin inhibitor.";
RL   FEBS Lett. 8:84-86(1970).
CC   -!- SUBCELLULAR LOCATION: Secreted.
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DR   PIR; A01207; TIBOC.
DR   MEROPS; I02.003; -.
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; Glycoprotein;
KW   Protease inhibitor; Reference proteome; Secreted;
KW   Serine protease inhibitor.
FT   CHAIN           1..67
FT                   /note="Colostrum trypsin inhibitor"
FT                   /id="PRO_0000155407"
FT   DOMAIN          8..58
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   SITE            18..19
FT                   /note="Reactive bond for trypsin"
FT   CARBOHYD        27
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   DISULFID        8..58
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031,
FT                   ECO:0000269|Ref.2"
FT   DISULFID        17..41
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031,
FT                   ECO:0000269|Ref.2"
FT   DISULFID        33..54
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031,
FT                   ECO:0000269|Ref.2"
SQ   SEQUENCE   67 AA;  7511 MW;  E2B2093B7CD207CD CRC64;
     FQTPPDLCQL PQARGPCKAA LLRYFYNSTS NACEPFTYGG CQGNNBNFET TEMCLRICEP
     PQQTDKS