ID   PEPC_RABIT              Reviewed;         388 AA.
AC   Q9GMY2;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Gastricsin;
DE            EC=3.4.23.3;
DE   AltName: Full=Pepsinogen C;
DE   Flags: Precursor;
GN   Name=PGC; Synonyms=PGNC;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
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; AB047250; BAB11756.1; -; mRNA.
DR   RefSeq; NP_001076103.1; NM_001082634.1.
DR   AlphaFoldDB; Q9GMY2; -.
DR   SMR; Q9GMY2; -.
DR   MEROPS; A01.003; -.
DR   GeneID; 100009323; -.
DR   KEGG; ocu:100009323; -.
DR   CTD; 5225; -.
DR   InParanoid; Q9GMY2; -.
DR   OrthoDB; 1619495at2759; -.
DR   Proteomes; UP000001811; 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   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:0000250"
FT   PROPEP          17..59
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000026067"
FT   CHAIN           60..388
FT                   /note="Gastricsin"
FT                   /id="PRO_0000026068"
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;  42754 MW;  A41CAE09E595E8A4 CRC64;
     MKWLLVALVC LHLLEAAVIK VPLRKFKSIR ETLKEKGLLK EFLNTHKYDP ALKYRFGDFS
     VTYEPMDYLD AAYFGEISIG TPSQNFLVLF DTGSSNLWVP SVYCQSEACT THNRFNPSKS
     STFYTYDQTF SLEYGSGSLT GFFGYDTFTI QNIEVPNQEF GLSETEPGTN FLYAEFDGIM
     GLAYPSLSVG DATPALQGMV QDGTISSSVF SFYLSSQQGT DGGALVLGGV DSSLYTGDIY
     WAPVTRELYW QIGIDEFLIS SEASGWCSQG CQAIVDTGTS LLTVPQEYMS DLLEATGAQE
     NEYGEFLVDC DSTESLPTFT FVINGVEFPL SPSAYILNTD GQCMVGVEAT YLSSQDGEPL
     WILGDVFLRA YYSVFDMANN RVGFAALA