ID   PEPA_CANLF              Reviewed;         386 AA.
AC   Q9GMY6;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Pepsin A;
DE            EC=3.4.23.1;
DE   Flags: Precursor;
GN   Name=PGA; Synonyms=PGNA;
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   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11603935; DOI=10.1006/mpev.2001.0996;
RA   Narita Y., Oda S., Takenaka O., Kageyama T.;
RT   "Phylogenetic position of Eulipotyphla inferred from the cDNA sequences of
RT   pepsinogens A and C.";
RL   Mol. Phylogenet. Evol. 21:32-42(2001).
CC   -!- FUNCTION: Shows particularly broad specificity; although bonds
CC       involving phenylalanine and leucine are preferred, many others are also
CC       cleaved to some extent. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: hydrophobic, preferably aromatic,
CC         residues in P1 and P1' positions. Cleaves 1-Phe-|-Val-2, 4-Gln-|-His-
CC         5, 13-Glu-|-Ala-14, 14-Ala-|-Leu-15, 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-
CC         17, 23-Gly-|-Phe-24, 24-Phe-|-Phe-25 and 25-Phe-|-Tyr-26 bonds in the
CC         B chain of insulin.; EC=3.4.23.1; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10094};
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR   EMBL; AB047246; BAB11752.1; -; mRNA.
DR   RefSeq; NP_001003117.1; NM_001003117.1.
DR   AlphaFoldDB; Q9GMY6; -.
DR   SMR; Q9GMY6; -.
DR   STRING; 9612.ENSCAFP00000024018; -.
DR   MEROPS; A01.001; -.
DR   PaxDb; Q9GMY6; -.
DR   Ensembl; ENSCAFT00845023744; ENSCAFP00845018630; ENSCAFG00845013325.
DR   GeneID; 403711; -.
DR   KEGG; cfa:403711; -.
DR   CTD; 100385980; -.
DR   VEuPathDB; HostDB:ENSCAFG00845013325; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   GeneTree; ENSGT00940000155036; -.
DR   InParanoid; Q9GMY6; -.
DR   OrthoDB; 1619495at2759; -.
DR   Proteomes; UP000002254; Chromosome 18.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05478; pepsin_A; 1.
DR   Gene3D; 2.40.70.10; -; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR012848; Aspartic_peptidase_N.
DR   InterPro; IPR034162; Pepsin_A.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966; PTHR47966; 1.
DR   Pfam; PF07966; A1_Propeptide; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; SSF50630; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 2.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   2: Evidence at transcript level;
KW   Aspartyl protease; Digestion; Disulfide bond; Hydrolase; Protease;
KW   Reference proteome; Secreted; Signal; Zymogen.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   PROPEP          16..60
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000026011"
FT   CHAIN           61..386
FT                   /note="Pepsin A"
FT                   /id="PRO_0000026012"
FT   DOMAIN          74..383
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        92
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        275
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   DISULFID        105..110
FT                   /evidence="ECO:0000250"
FT   DISULFID        266..270
FT                   /evidence="ECO:0000250"
FT   DISULFID        309..342
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   386 AA;  41551 MW;  5F0D1598322390C5 CRC64;
     MKWLLLISLV ALSECAIVKV PLVRKKSLRQ NLIEHGLLND FLKNQSPNPA SKYFPQEPTV
     LATQSLKNYM DMEYFGTIGI GTPPQEFTVI FDTGSSNLWV PSVYCSSPAC SNHNRFNPQE
     SSTYQGTNRP VSIAYGTGSM TGILGYDTVQ VGGIADTNQI FGLSETEPGS FLYYAPFDGI
     LGLAYPQISA SGATPVFDNM WNEGLVSQDL FSVYLSSDDQ SGSVVMFGGI DSSYYSGNLN
     WVPVSVEGYW QITVDSVTMN GQAIACSDGC QAIVDTGTSL LAGPTNAIAN IQSYIGASQN
     SYGQMVISCS AINSLPDIVF TINGIQYPLP PSAYILQSQQ GCVSGFQGMN LPTASGELWI
     LGDVFIRQYF AVFDRANNQV GLAPVA