ID   IPSG_MARMT              Reviewed;         122 AA.
AC   P81482;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Double-headed protease inhibitor, submandibular gland;
OS   Martes martes (European pine marten).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae; Guloninae;
OC   Martes.
OX   NCBI_TaxID=29065;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=8403842; DOI=10.1016/0305-0491(93)90014-v;
RA   Hochstrasser K., Wachter E., Reisinger P.W.M., Greim M., Albrecht G.J.,
RA   Gebhard W.;
RT   "Amino acid sequences of mammalian kazal-type proteinase inhibitors from
RT   salivary glands.";
RL   Comp. Biochem. Physiol. 106B:103-108(1993).
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; P81482; -.
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_0000073037"
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;  13444 MW;  985708CC8F94A403 CRC64;
     APPPVGDQAG GRKVDCFKYN TTGSAFACTR HERPVCGTDH RTYSNECMFC MLTQNKGFGV
     RILQDNECDI ECTQYSDMCT MEYLPLCGSD GKNYSNKCLF CNAVMGSRGA LFLAKHGQCQ
     SP