ID   PEPA_CALJA              Reviewed;         387 AA.
AC   Q9N2D4;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Pepsin A;
DE            EC=3.4.23.1;
DE   Flags: Precursor;
GN   Name=PGA;
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 16-25, FUNCTION, AND
RP   ACTIVITY REGULATION.
RC   TISSUE=Gastric mucosa;
RX   PubMed=10788784; DOI=10.1093/oxfordjournals.jbchem.a022668;
RA   Kageyama T.;
RT   "New World monkey pepsinogens A and C, and prochymosins. Purification,
RT   characterization of enzymatic properties, cDNA cloning, and molecular
RT   evolution.";
RL   J. Biochem. 127:761-770(2000).
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:0000269|PubMed:10788784}.
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   -!- ACTIVITY REGULATION: Inhibited by pepstatin.
CC       {ECO:0000269|PubMed:10788784}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is about 2.;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR   EMBL; AB038384; BAA90871.1; -; mRNA.
DR   PIR; JC7245; JC7245.
DR   RefSeq; NP_001254696.1; NM_001267767.1.
DR   AlphaFoldDB; Q9N2D4; -.
DR   SMR; Q9N2D4; -.
DR   STRING; 9483.ENSCJAP00000036045; -.
DR   MEROPS; A01.001; -.
DR   Ensembl; ENSCJAT00000038063; ENSCJAP00000036045; ENSCJAG00000019394.
DR   GeneID; 100385980; -.
DR   KEGG; cjc:100385980; -.
DR   CTD; 100385980; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   GeneTree; ENSGT00940000155036; -.
DR   InParanoid; Q9N2D4; -.
DR   OrthoDB; 1619495at2759; -.
DR   Proteomes; UP000008225; Chromosome 11.
DR   Bgee; ENSCJAG00000019394; Expressed in testis and 1 other tissue.
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   1: Evidence at protein level;
KW   Aspartyl protease; Digestion; Direct protein sequencing; Disulfide bond;
KW   Hydrolase; Phosphoprotein; Protease; Reference proteome; Secreted; Signal;
KW   Zymogen.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000269|PubMed:10788784"
FT   PROPEP          16..61
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000026009"
FT   CHAIN           62..387
FT                   /note="Pepsin A"
FT                   /id="PRO_0000026010"
FT   DOMAIN          75..384
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        93
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        276
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   MOD_RES         129
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P03954"
FT   DISULFID        106..111
FT                   /evidence="ECO:0000250"
FT   DISULFID        267..271
FT                   /evidence="ECO:0000250"
FT   DISULFID        310..343
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   387 AA;  41564 MW;  7A7968AA568464BD CRC64;
     MKWLLLLSLV ALSECLYKVS LIKKKSLRKN LIEHGLLKDF LKNNTLDPAS KYFPQGEAAT
     MIANQPLVNY LDMEYFGTIG IGTPAQEFTV IFDTGSSNLW VPSIYCSSPA CTNHNRFNPQ
     ESSTYQATSQ TLSIAYGTGS MTGILGYDTV QVGGIADTNQ IFGLSETEPG SFLYYSPFDG
     ILGLAYPSIS SSGATPVFDN IWNQDLVSQD LFSVYLSSND QSGSVVMFGG IDSSYYTGSL
     NWVPVSAEGY WQITVDSITM NGEAIACAEG CQAIVDTGTS LLSGPTSPIA NIQSYIGASE
     NSNGEMVVSC SAISSLPDIV FTINGIQYPV PASAYILQDE GGCTSGFQGM NIPTAYGELW
     ILGDVFIRQY FAVFDRANNQ VGLAPVA