ID   IPSG_PANLE              Reviewed;         112 AA.
AC   P08481;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Double-headed protease inhibitor, submandibular gland;
OS   Panthera leo (Lion).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Pantherinae;
OC   Panthera.
OX   NCBI_TaxID=9689;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Submandibular gland;
RX   PubMed=3304339; DOI=10.1515/bchm3.1987.368.1.717;
RA   Reisinger P.W.M., Hochstrasser K., Gottlicher I., Eulitz M., Wachter E.;
RT   "The amino-acid sequences of the double-headed proteinase inhibitors from
RT   cat, lion and dog submandibular glands.";
RL   Biol. Chem. Hoppe-Seyler 368:717-726(1987).
CC   -!- FUNCTION: This inhibitor is composed of two homologous actively
CC       inhibiting halves: one which inhibits trypsin, the other which inhibits
CC       elastase.
CC   -!- SUBCELLULAR LOCATION: Secreted.
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DR   PIR; B29654; B29654.
DR   AlphaFoldDB; P08481; -.
DR   SMR; P08481; -.
DR   MEROPS; I01.016; -.
DR   MEROPS; I01.017; -.
DR   Proteomes; UP000694399; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR002350; Kazal_dom.
DR   InterPro; IPR036058; Kazal_dom_sf.
DR   InterPro; IPR001239; Prot_inh_Kazal-m.
DR   Pfam; PF00050; Kazal_1; 2.
DR   PRINTS; PR00290; KAZALINHBTR.
DR   SMART; SM00280; KAZAL; 2.
DR   SUPFAM; SSF100895; SSF100895; 2.
DR   PROSITE; PS00282; KAZAL_1; 2.
DR   PROSITE; PS51465; KAZAL_2; 2.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Protease inhibitor;
KW   Reference proteome; Repeat; Secreted; Serine protease inhibitor.
FT   CHAIN           1..112
FT                   /note="Double-headed protease inhibitor, submandibular
FT                   gland"
FT                   /id="PRO_0000073040"
FT   DOMAIN          2..62
FT                   /note="Kazal-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DOMAIN          63..112
FT                   /note="Kazal-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   SITE            22..23
FT                   /note="Reactive bond 1 for trypsin"
FT   SITE            73..74
FT                   /note="Reactive bond 2 for elastase"
FT   DISULFID        8..42
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        20..39
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        28..60
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        64..93
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        71..90
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        79..111
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
SQ   SEQUENCE   112 AA;  12740 MW;  D8062796D3FC611C CRC64;
     ASPPEVNCSQ YNRKGSGIAC SKQLKPICGI DHKTYSNECM FCLLNQNKQF QIRKLYDDKC
     QIECTNYSAI CTMEYFPLCG SDGKVYSNKC SFCNEVVKRR GTLFLAKYGQ CK