ID   PEPA_SUNMU              Reviewed;         387 AA.
AC   P81497; Q9GMY9;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 2.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Pepsin A;
DE            EC=3.4.23.1;
DE   Flags: Precursor;
GN   Name=PGA; Synonyms=PGNA;
OS   Suncus murinus (Asian house shrew) (Musk shrew).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Soricidae; Crocidurinae; Suncus.
OX   NCBI_TaxID=9378;
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).
RN   [2]
RP   PROTEIN SEQUENCE OF 17-82.
RC   TISSUE=Gastric mucosa;
RX   PubMed=9354369; DOI=10.1093/oxfordjournals.jbchem.a021687;
RA   Narita Y., Oda S., Moriyama A., Takenaka O., Kageyama T.;
RT   "Pepsinogens and pepsins from house musk shrew, Suncus murinus:
RT   purification, characterization, determination of the amino-acid sequences
RT   of the activation segments, and analysis of proteolytic specificities.";
RL   J. Biochem. 121:1010-1017(1997).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB047243; BAB11749.1; -; mRNA.
DR   PIR; PC4360; PC4360.
DR   AlphaFoldDB; P81497; -.
DR   SMR; P81497; -.
DR   MEROPS; A01.001; -.
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; Secreted; Signal; Zymogen.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000269|PubMed:9354369"
FT   PROPEP          17..61
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000026042"
FT   CHAIN           62..387
FT                   /note="Pepsin A"
FT                   /id="PRO_0000026043"
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;  41576 MW;  7F9FF818DD8541CE CRC64;
     MKKLLLLLGL VALSECLYKV PLVKKKSLRQ NLIENGLLKD FLAKHNVNPA SKYFPTEAAT
     ELADQPLVNY MDMEYFGTIG IGTPPQEFTV IFDTGSSNLW VPSVYCSSPA CSNHNRFNPQ
     KSSTFQSTSQ TLSIAYGTGS MTGVLGYDTV QVAGIADTNQ IFGLSQTEPG SFLYYSPFDG
     ILGLAYPNIA SSGATPVFDN MWNQGLVSQD LFSVYLSSND QSGSVVIFGG IDSSYYTGNL
     NWVPLSSEGY WQITVDSITM NGQAIACSGS CQAIVDTGTS LLSGPNNAIA NIQKSIGASQ
     NANGQMVVSC SSIQSLPDIV FTINGIQYPL PASAYILQNQ QDCTSGFQGM DIPTPSGELW
     ILGDVFIRQY FAVFDRGNNR VGLAPVA