ID   PEPA_RHIFE              Reviewed;         386 AA.
AC   Q9GMY7;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Pepsin A;
DE            EC=3.4.23.1;
DE   Flags: Precursor;
GN   Name=PGA; Synonyms=PGNA;
OS   Rhinolophus ferrumequinum (Greater horseshoe bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Rhinolophidae;
OC   Rhinolophinae; Rhinolophus.
OX   NCBI_TaxID=59479;
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; AB047245; BAB11751.1; -; mRNA.
DR   AlphaFoldDB; Q9GMY7; -.
DR   SMR; Q9GMY7; -.
DR   MEROPS; A01.001; -.
DR   Ensembl; ENSRFET00010002876; ENSRFEP00010002613; ENSRFEG00010001876.
DR   GeneTree; ENSGT00940000155036; -.
DR   OMA; ENYMDME; -.
DR   Proteomes; UP000472240; Chromosome 11.
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_0000026038"
FT   CHAIN           61..386
FT                   /note="Pepsin A"
FT                   /id="PRO_0000026039"
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;  41591 MW;  917EE04D3166C3A4 CRC64;
     MKWLLLLSLV ALSECYIYKV PLVKKKSLRK NLMEQGLLQD YLKTHSINPA SKYLKEAASM
     MATQPLENYM DMEYFGTIGI GTPPQEFTVI FDTGSSNLWV PSVYCSSPAC SNHNRFNPQQ
     SSTYQGTNQK LSVAYGTGSM TGILGYDTVQ VGGITDTNQI FGLSETEPGS FLYYAPFDGI
     LGLAYPSIAS SGATPVFDNI WNQGLVSQDL FSVYLSSNDQ GGSVVMFGGI DSSYFTGNLN
     WVPLSSETYW QITVDSITMN GQVIACSGSC QAIVDTGTSL LSGPTNAIAS IQGYIGASQN
     ANGEMVVSCS AINTLPNIVF TINGVQYPLP PSAYVLQSQQ GCTSGFQGMD IPTSSGELWI
     LGDVFIRQYF TVFDRGNNQV GLAPVA