ID   PEPA_BOVIN              Reviewed;         372 AA.
AC   P00792; Q6VRA9;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 2.
DT   04-NOV-2026, entry version 155.
DE   RecName: Full=Pepsin A;
DE            EC=3.4.23.1;
DE   Flags: Precursor;
GN   Name=PGA;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15128507; DOI=10.1128/aem.70.5.2588-2595.2004;
RA   Munoz R., Garcia J.L., Carrascosa A.V., Gonzalez R.;
RT   "Cloning of the authentic bovine gene encoding pepsinogen A and its
RT   expression in microbial cells.";
RL   Appl. Environ. Microbiol. 70:2588-2595(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-48.
RX   PubMed=4603017; DOI=10.1016/s0021-9258(19)42445-9;
RA   Harboe M.K., Andersen P.M., Foltmann B., Kay J., Kassell B.;
RT   "The activation of bovine pepsinogen. Sequence of the peptides released,
RT   identification of a pepsin inhibitor.";
RL   J. Biol. Chem. 249:4487-4494(1974).
RN   [3]
RP   PROTEIN SEQUENCE OF 42-111.
RX   PubMed=776669; DOI=10.1016/0014-5793(75)80435-2;
RA   Harboe M.K., Foltmann B.;
RT   "Bovine pepsin: the sequence of the first 65 amino acid residues
RT   (completing the sequence of the first 110 residues of bovine pepsinogen).";
RL   FEBS Lett. 60:133-136(1975).
CC   -!- FUNCTION: Shows particularly broad specificity; although bonds
CC       involving phenylalanine and leucine are preferred, many others are also
CC       cleaved to some extent.
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; AY330769; AAQ95219.1; -; mRNA.
DR   PIR; A92157; PEBO.
DR   RefSeq; NP_001001600.2; NM_001001600.2.
DR   AlphaFoldDB; P00792; -.
DR   SMR; P00792; -.
DR   FunCoup; P00792; 113.
DR   STRING; 9913.ENSBTAP00000019640; -.
DR   MEROPS; A01.001; -.
DR   GlyGen; P00792; 1 site.
DR   PaxDb; 9913-ENSBTAP00000019640; -.
DR   GeneID; 414350; -.
DR   KEGG; bta:414350; -.
DR   CTD; 5222; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   InParanoid; P00792; -.
DR   OMA; AACENHR; -.
DR   OrthoDB; 771136at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   CDD; cd05478; pepsin_A; 1.
DR   FunFam; 2.40.70.10:FF:000006; Cathepsin E; 1.
DR   FunFam; 2.40.70.10:FF:000004; Pepsin A; 1.
DR   Gene3D; 6.10.140.60; -; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 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; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR47966:SF22; PEPSIN A-3-RELATED; 1.
DR   Pfam; PF07966; A1_Propeptide; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 2.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   1: Evidence at protein level;
KW   Aspartyl protease; Digestion; Direct protein sequencing; Disulfide bond;
KW   Hydrolase; Phosphoprotein; Protease; Reference proteome; Secreted; Zymogen.
FT   PROPEP          1..42
FT                   /note="Activation peptide"
FT                   /id="PRO_0000026007"
FT   CHAIN           43..372
FT                   /note="Pepsin A"
FT                   /id="PRO_0000026008"
FT   DOMAIN          60..369
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        78
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        261
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   MOD_RES         114
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P03954"
FT   DISULFID        91..96
FT                   /evidence="ECO:0000269|PubMed:776669"
FT   DISULFID        252..256
FT                   /evidence="ECO:0000250"
FT   DISULFID        295..328
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   372 AA;  40003 MW;  987D573394E79C34 CRC64;
     MSVVKIPLVK KKSLRQNLIE NGKLKEFMRT HKYNLGSKYI REAATLVSEQ PLQNYLDTEY
     FGTIGIGTPA QDFTVIFDTG SSNLWVPSIY CSSEACTNHN RFNPQDSSTY EATSETLSIT
     YGTGSMTGIL GYDTVQVGGI SDTNQIFGLS ETEPGSFLYY APFDGILGLA YPSISSSGAT
     PVFDNIWDQG LVSQDLFSVY LSSNEESGSV VIFGDIDSSY YSGSLNWVPV SVEGYWQITV
     DSITMNGESI ACSDGCQAIV DTGTSLLAGP TTAISNIQSY IGASEDSSGE VVISCSSIDS
     LPDIVFTING VQYPVPPSAY ILQSNGICSS GFEGMDISTS SGDLWILGDV FIRQYFTVFD
     RGNNQIGLAP VA
//