ID   B4DW12_HUMAN            Unreviewed;       151 AA.
AC   B4DW12;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=Gastricsin {ECO:0000256|ARBA:ARBA00023821};
DE            EC=3.4.23.3 {ECO:0000256|ARBA:ARBA00023796};
DE   AltName: Full=Pepsinogen C {ECO:0000256|ARBA:ARBA00033248};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG62874.1};
RN   [1] {ECO:0000313|EMBL:BAG62874.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Stomach {ECO:0000313|EMBL:BAG62874.1};
RA   Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A.,
RA   Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y.,
RA   Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.,
RA   Sugano S., Nomura N., Isogai T.;
RT   "NEDO human cDNA sequencing project focused on splicing variants.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Hydrolyzes a variety of proteins.
CC       {ECO:0000256|ARBA:ARBA00023749}.
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; Evidence={ECO:0000256|ARBA:ARBA00023733};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
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DR   EMBL; AK301325; BAG62874.1; -; mRNA.
DR   AlphaFoldDB; B4DW12; -.
DR   MEROPS; A01.003; -.
DR   PeptideAtlas; B4DW12; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 6.10.140.60; -; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 1.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR012848; Aspartic_peptidase_N.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR47966:SF72; GASTRICSIN; 1.
DR   Pfam; PF07966; A1_Propeptide; 1.
DR   Pfam; PF00026; Asp; 1.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR601461-2}; Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..151
FT                   /note="Gastricsin"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002803348"
FT   DOMAIN          73..151
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   DISULFID        104..109
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   151 AA;  17053 MW;  24F8929FC324C2FA CRC64;
     MKWMVVVLVC LQLLEAAVVK VPLKKFKSIR ETMKEKGLLG EFLRTHKYDP AWKYRFGDLS
     VTYEPMAYMD AAYFGEISIG TPPQNFLVLF DTGSSNLWVP SVYCQSQACT SHSRFNPSES
     STYSTNGQTF SLQYGSGSLT GFFGYDTLDF L
//