ID   PEPC_SORUN              Reviewed;         389 AA.
AC   Q9GMY4;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Gastricsin;
DE            EC=3.4.23.3;
DE   AltName: Full=Pepsinogen C;
DE   Flags: Precursor;
GN   Name=PGC; Synonyms=PGNC;
OS   Sorex unguiculatus (Long-clawed shrew).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Soricidae; Soricinae; Sorex.
OX   NCBI_TaxID=62275;
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; AB047248; BAB11754.1; -; mRNA.
DR   AlphaFoldDB; Q9GMY4; -.
DR   SMR; Q9GMY4; -.
DR   MEROPS; A01.003; -.
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   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_0000026073"
FT   CHAIN           60..389
FT                   /note="Gastricsin"
FT                   /id="PRO_0000026074"
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;  42416 MW;  44E7794541212CD1 CRC64;
     MKWTVVALVC LQLLEAAVVK VPLKKFKSIR ETLREQGLLG EFLRTHPYDP AQKYHFGDFS
     VAYEPMAYLD AAYFGEISIG TPPQNFLVLF DTGSSNLWVP SVYCQSQACT GHARFNPSKS
     STYSTNGQTF SLQYGSGSLT GFFGYDTMTL QNIKVPHQEF GLSQNEPGEN FVYAQFDGIM
     GMAYPTLAMG GATTALQGML QAGALDSPVF SFYLSNQQSS KDGGAVVFGG VDNSLYTGQI
     FWTPVTQELY WQIGVEQFLI GGQATGWCSQ GCQAIVDTGT SLLTVPQQYL SALQQATGAQ
     LDQDGQMVVN CNNIQNLPTL TFVINGVQFP LLPSAYVLNN NGYCTLGVEP TYLPSPTGQP
     LWILGDVFLR SYYSVYDMGN NRVGFATAA