ID   IPSG_MELME              Reviewed;         122 AA.
AC   P16226;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Double-headed protease inhibitor, submandibular gland;
OS   Meles meles (Eurasian badger).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae; Melinae;
OC   Meles.
OX   NCBI_TaxID=9662;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Submandibular gland;
RX   PubMed=2626426;
RA   Hochstrasser K., Paulus M., Wachter E., Reisinger P.W.M.;
RT   "The amino-acid sequence of the double-headed proteinase inhibitor from
RT   badger (Meles meles) submandibular glands.";
RL   Protein Seq. Data Anal. 2:453-456(1989).
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   AlphaFoldDB; P16226; -.
DR   SMR; P16226; -.
DR   MEROPS; I01.016; -.
DR   MEROPS; I01.017; -.
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; Repeat;
KW   Secreted; Serine protease inhibitor.
FT   CHAIN           1..122
FT                   /note="Double-headed protease inhibitor, submandibular
FT                   gland"
FT                   /id="PRO_0000073038"
FT   DOMAIN          10..70
FT                   /note="Kazal-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DOMAIN          71..121
FT                   /note="Kazal-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   SITE            30..31
FT                   /note="Reactive bond 1 for trypsin"
FT   SITE            81..82
FT                   /note="Reactive bond 2 for elastase"
FT   DISULFID        16..50
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        28..47
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        36..68
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        72..101
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        79..98
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        87..119
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
SQ   SEQUENCE   122 AA;  13534 MW;  342F7AE4B88E32FE CRC64;
     APPPVGDQAG GRKVNCSKYN AKGSQFACSR HLDPVCGTDH RTYSNECMFC MLTQNKRFSV
     RILQDNNCDI ECTQYSDMCT MDYLPLCGSD GNNYSNKCLF CNAVLRSRGA LFLAKHGQCE
     SP