ID   PEPC_CALJA              Reviewed;         388 AA.
AC   Q9N2D3;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Gastricsin;
DE            EC=3.4.23.3;
DE   AltName: Full=Pepsinogen C;
DE   Flags: Precursor;
GN   Name=PGC;
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 17-26, 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: Hydrolyzes a variety of proteins.
CC       {ECO:0000269|PubMed:10788784}.
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   -!- 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; AB038385; BAA90872.1; -; mRNA.
DR   PIR; JC7246; JC7246.
DR   RefSeq; XP_002746573.1; XM_002746527.2.
DR   AlphaFoldDB; Q9N2D3; -.
DR   SMR; Q9N2D3; -.
DR   STRING; 9483.ENSCJAP00000007671; -.
DR   MEROPS; A01.003; -.
DR   GeneID; 100404738; -.
DR   KEGG; cjc:100404738; -.
DR   CTD; 5225; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_013253_3_0_1; -.
DR   InParanoid; Q9N2D3; -.
DR   OMA; LSNNGYC; -.
DR   OrthoDB; 1619495at2759; -.
DR   TreeFam; TF314990; -.
DR   Proteomes; UP000008225; Unplaced.
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   1: Evidence at protein level;
KW   Aspartyl protease; Digestion; Direct protein sequencing; Disulfide bond;
KW   Hydrolase; Protease; Reference proteome; Secreted; Signal; Zymogen.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000269|PubMed:10788784"
FT   PROPEP          17..59
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000026052"
FT   CHAIN           60..388
FT                   /note="Gastricsin"
FT                   /id="PRO_0000026053"
FT   DOMAIN          73..385
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        276
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   DISULFID        104..109
FT                   /evidence="ECO:0000250"
FT   DISULFID        267..271
FT                   /evidence="ECO:0000250"
FT   DISULFID        310..343
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   388 AA;  42503 MW;  0BC48DBD1F7D2D8C CRC64;
     MKWMVVAFIC LQLLEATVVK VPLKKFKSIR ETMKEKGLLW EFLKTHKHDP ARKYRVSDLS
     VSYEPMDYMD AAYFGEISIG TPPQNFLVLF DTGSSNLWVP SVYCQSQACT SHSRFNPSAS
     STYSSNGQTF SLQYGSGSLT GFFGYDTLTV QSIQVPNQEF GLSENEPGTN FVYAQFDGIM
     GLAYPALSMG GATTAMQGML QEGALTSPVF SFYLSNQQGS SGGAVIFGGV DSSLYTGQIY
     WAPVTQELYW QIGIEEFLIG GQASGWCSEG CQAIVDTGTS LLTVPQQYMS AFLEATGAQE
     DEYGQFLVNC DSIQNLPTLT FIINGVEFPL PPSSYILSNN GYCTVGVEPT YLSSQNSQPL
     WILGDVFLRS YYSVFDLGNN RVGFATAA