ID   PEPC_RHIFE              Reviewed;         389 AA.
AC   Q9GMY3;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Gastricsin;
DE            EC=3.4.23.3;
DE   AltName: Full=Pepsinogen C;
DE   Flags: Precursor;
GN   Name=PGC; Synonyms=PGNC;
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: Hydrolyzes a variety of proteins.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=More restricted specificity than pepsin A, but shows
CC         preferential cleavage at Tyr-|-Xaa bonds. High activity on
CC         hemoglobin.; EC=3.4.23.3;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR   EMBL; AB047249; BAB11755.1; -; mRNA.
DR   AlphaFoldDB; Q9GMY3; -.
DR   SMR; Q9GMY3; -.
DR   MEROPS; A01.003; -.
DR   Ensembl; ENSRFET00010003109; ENSRFEP00010002827; ENSRFEG00010002003.
DR   GeneTree; ENSGT00940000160626; -.
DR   Proteomes; UP000472240; Chromosome 3.
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   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; IPR033735; Gastricsin.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR13683; PTHR13683; 1.
DR   PANTHER; PTHR13683:SF292; PTHR13683:SF292; 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..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..59
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000026071"
FT   CHAIN           60..389
FT                   /note="Gastricsin"
FT                   /id="PRO_0000026072"
FT   DOMAIN          73..386
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        91
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        277
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   DISULFID        104..109
FT                   /evidence="ECO:0000250"
FT   DISULFID        268..272
FT                   /evidence="ECO:0000250"
FT   DISULFID        311..344
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   389 AA;  42921 MW;  29B482E771A357D6 CRC64;
     MKWMVVVLLC LQLLEAKVVK VPLKKLKSLR ETMKEKGLLE EFLKNHKYDP AQKYRYTDFS
     VAYEPMAYMD AAYFGEISIG TPPQNFLVLF DTGSSNLWVP SVYCQTQACT GHTRFNPSQS
     STYSTNGQTF SLQYGSGSLT GFFGYDTLTV QSIQVPNQEF GLSENEPGTN FVYAQFDGIM
     GMAYPSLAMG GATTALQGML QEGALTSPVF SFYLSNQQGS QNGGAVIFGG VDNSLYQGQI
     YWAPVTQELY WQIGIEEFLI GGQASGWCSQ GCQAIVDTGT SLLTVPQQYM SALLQATGAQ
     EDQYGQFFVN CNYIQNLPTF TFIINGVQFP LPPSSYILNN NGYCTVGVEP TYLPSQNGQP
     LWILGDVFLR SYYSVYDMGN NRVGFATAA