ID   IPSG_CANLF              Reviewed;         115 AA.
AC   P01002;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Double-headed protease inhibitor, submandibular gland;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
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).
RN   [2]
RP   PRELIMINARY PROTEIN SEQUENCE.
RC   TISSUE=Submandibular gland;
RX   PubMed=1213682; DOI=10.1515/bchm2.1975.356.2.1865;
RA   Hochstrasser K., Bretzel G., Wachter E., Heindl S.;
RT   "The amino acid sequence of the double-headed proteinase inhibitor from
RT   canine submandibular glands, III. Sequencing studies.";
RL   Hoppe-Seyler's Z. Physiol. Chem. 356:1865-1877(1975).
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.
CC   -!- MISCELLANEOUS: Three very similar inhibitors found in the submandibular
CC       glands are secreted into the saliva. The sequence shown is one of the
CC       two main inhibitors.
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DR   PIR; C29654; TIDGS.
DR   AlphaFoldDB; P01002; -.
DR   SMR; P01002; -.
DR   MEROPS; I01.016; -.
DR   MEROPS; I01.017; -.
DR   PaxDb; P01002; -.
DR   eggNOG; KOG3649; Eukaryota.
DR   Proteomes; UP000002254; 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..115
FT                   /note="Double-headed protease inhibitor, submandibular
FT                   gland"
FT                   /id="PRO_0000073035"
FT   DOMAIN          6..66
FT                   /note="Kazal-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DOMAIN          67..115
FT                   /note="Kazal-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   SITE            26..27
FT                   /note="Reactive bond 1 for trypsin"
FT   SITE            77..78
FT                   /note="Reactive bond 2 for elastase"
FT   DISULFID        12..46
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        24..43
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        32..64
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        68..97
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        75..94
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        83..115
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
SQ   SEQUENCE   115 AA;  12775 MW;  1F901F163EE2A35C CRC64;
     GPPPAIGREV DCSNYKGKGS QIACPRLHQP ICGTDHKTYS NECMFCALTL NKKFEVRKLQ
     DTACDIECTE YSDMCTMDYR PLCGSDGKNY SNKCSFCNAV KKSRGTIFLA KHGEC