ID   PEPC_CAVPO              Reviewed;         394 AA.
AC   Q64411;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Gastricsin;
DE            EC=3.4.23.3;
DE   AltName: Full=Pepsinogen C;
DE   Flags: Precursor;
GN   Name=PGC;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1644829; DOI=10.1016/s0021-9258(18)42024-8;
RA   Kageyama T., Ichinose M., Tsukada S., Miki K., Kurokawa K., Koiwai O.,
RA   Tanji M., Yakabe E., Athauda S.B., Takahashi K.;
RT   "Gastric procathepsin E and progastricsin from guinea pig. Purification,
RT   molecular cloning of cDNAs, and characterization of enzymatic properties,
RT   with special reference to procathepsin E.";
RL   J. Biol. Chem. 267:16450-16459(1992).
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; M88652; AAA37053.1; -; mRNA.
DR   PIR; B43356; B43356.
DR   RefSeq; NP_001166470.1; NM_001172999.1.
DR   AlphaFoldDB; Q64411; -.
DR   SMR; Q64411; -.
DR   STRING; 10141.ENSCPOP00000006477; -.
DR   MEROPS; A01.003; -.
DR   Ensembl; ENSCPOT00000007255; ENSCPOP00000006477; ENSCPOG00000007183.
DR   GeneID; 100135598; -.
DR   KEGG; cpoc:100135598; -.
DR   CTD; 5225; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   GeneTree; ENSGT00940000160626; -.
DR   HOGENOM; CLU_013253_3_0_1; -.
DR   InParanoid; Q64411; -.
DR   OMA; LSNNGYC; -.
DR   OrthoDB; 1619495at2759; -.
DR   TreeFam; TF314990; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000007183; Expressed in cerebellum and 2 other tissues.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR   GO; GO:0002803; P:positive regulation of antibacterial peptide production; IEA:Ensembl.
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..65
FT                   /note="Activation peptide"
FT                   /id="PRO_0000026054"
FT   CHAIN           66..394
FT                   /note="Gastricsin"
FT                   /id="PRO_0000026055"
FT   DOMAIN          79..391
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        97
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        283
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   DISULFID        110..115
FT                   /evidence="ECO:0000250"
FT   DISULFID        273..277
FT                   /evidence="ECO:0000250"
FT   DISULFID        316..349
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   394 AA;  42996 MW;  114F08E105D49865 CRC64;
     MKWMVVVLLC LPLLEATQIK VPLKKIKSIR EVLREKGLLG DFLKNHKPQH ARKFFRNRLA
     KTGDFSVLYE PMSYMDAAYF GQISLGTPPQ SFQVLFDTGS SNLWVPSVYC SSLACTTHTR
     FNPRDSSTYV ATDQSFSLEY GTGSLTGVFG YDTMTIQDIQ VPKQEFGLSE TEPGSDFVYA
     EFDGILGLGY PGLSEGGATT AMQGLLREGA LSQSLFSVYL GSQQGSDEGQ LILGGVDESL
     YTGDIYWTPV TQELYWQIGI EGFLIDGSAS GWCSRGCQGI VDTGTSLLTV PSDYLSTLVQ
     AIGAEENEYG EYFVSCSSIQ DLPTLTFVIS GVEFPLSPSA YILSGENYCM VGLESTYVSP
     GGGEPVWILG DVFLRSYYSV YDLANNRVGF ATAA