ID   PEPA_MACMU              Reviewed;         388 AA.
AC   P11489;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Pepsin A;
DE            EC=3.4.23.1;
DE   Flags: Precursor;
GN   Name=PGA;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2900796; DOI=10.1016/0378-1119(88)90454-4;
RA   Evers M.P.J., Zelle B., Bebelman J.-P., Pronk J.C., Mager W.H.,
RA   Planta R.J., Eriksson A.W., Frants R.R.;
RT   "Cloning and sequencing of rhesus monkey pepsinogen A cDNA.";
RL   Gene 65:179-185(1988).
RN   [2]
RP   SEQUENCE REVISION.
RA   Zelle B.;
RL   Submitted (SEP-1988) to the EMBL/GenBank/DDBJ databases.
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; M20788; AAA36902.1; -; mRNA.
DR   PIR; JT0309; PEMQAR.
DR   RefSeq; NP_001098064.1; NM_001104594.1.
DR   AlphaFoldDB; P11489; -.
DR   SMR; P11489; -.
DR   STRING; 9544.ENSMMUP00000015085; -.
DR   MEROPS; A01.001; -.
DR   GeneID; 694562; -.
DR   KEGG; mcc:694562; -.
DR   CTD; 643847; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   InParanoid; P11489; -.
DR   OrthoDB; 1619495at2759; -.
DR   Proteomes; UP000006718; 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:0007586; P:digestion; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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; Phosphoprotein;
KW   Protease; Reference proteome; Secreted; Signal; Zymogen.
FT   SIGNAL          1..15
FT   PROPEP          16..62
FT                   /note="Activation peptide"
FT                   /id="PRO_0000026024"
FT   CHAIN           63..388
FT                   /note="Pepsin A"
FT                   /id="PRO_0000026025"
FT   DOMAIN          76..385
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        94
FT   ACT_SITE        277
FT   MOD_RES         130
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P03954"
FT   DISULFID        107..112
FT                   /evidence="ECO:0000250"
FT   DISULFID        268..272
FT                   /evidence="ECO:0000250"
FT   DISULFID        311..344
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   388 AA;  41697 MW;  97F6E5E3F6C2A793 CRC64;
     MKWLLLLGLV ALSECIIYKV PLVRKKSLRR NLSEHGLLKD FLKKHNRNPA SKYFPQTEAP
     TLIDEQPLEN YLDVEYFGTI GIGTPAQDFT VIFDTGSSNL WVPSVYCSSL ACTNHNLFNP
     QDSSTYQSTS GTLSITYGTG SMTGILGYDT VQVGGISDTN QIFGLSETEP GSFLYYAPFD
     GILGLAYPSI SSSGATPVFD NIWDQGLVSQ DLFSVYLSAD DQSGSVVIFG GIDSSYYTGS
     LNWVPVSVEG YWQISVDSIT MNGEAIACAE GCQAIVDTGT SLLTGPTSPI ANIQSDIGAS
     ENSDGEMVVS CSAISSLPDI VFTINGVQYP LPPSAYILQS QGSCTSGFQG MDVPTESGEL
     WILGDVFIRQ YFTVFDRANN QVGLAPVA