ID   H6WAS7_ORENI            Unreviewed;       339 AA.
AC   H6WAS7;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   22-FEB-2023, entry version 44.
DE   SubName: Full=Pepsin {ECO:0000313|EMBL:AEZ51819.1};
DE   Flags: Fragment;
OS   Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX   NCBI_TaxID=8128 {ECO:0000313|EMBL:AEZ51819.1};
RN   [1] {ECO:0000313|EMBL:AEZ51819.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Li B.;
RT   "Molecular cloning of pepsin of Nile tilapia.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; JQ043215; AEZ51819.1; -; mRNA.
DR   AlphaFoldDB; H6WAS7; -.
DR   SMR; H6WAS7; -.
DR   MEROPS; A01.088; -.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.1960; -; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
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:SF22; PEPSIN A-3-RELATED; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 2.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   2: Evidence at transcript level;
KW   Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW   Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454}.
FT   DOMAIN          32..336
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        50
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        232
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        63..68
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   DISULFID        223..227
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   DISULFID        266..299
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AEZ51819.1"
SQ   SEQUENCE   339 AA;  35842 MW;  7024CD8A2EB5911F CRC64;
     VEEGKKTHPY NPAAKFYSSG TESMTNDADL SYYGTISIGT PPQSFSVIFD TGSSNLWVPS
     VYCNSTACEN HNQFNPSQSS TFQWGNQSLS IQYGTGSMTG FLGSDTVEVG GISVANQVFG
     LSQTEASFMT YMQADGILGL AFQSIASDNV VPVFNTMITE GLVSEPIFSV YLSGNSEQGS
     EVVFGGTDST HYTGTITWIP LSSATYWQIN MDSVTINGQT VACSGGCQAI IDTGTSLIVG
     PTTDINNLNS WVGASTDQSG DAIVNCQNIP SMPDVTFTLN GNAFTVPASA YVSQSSSGCM
     TGFGQGGTMQ LWILGDVFIR EYYAVFNAQT QNIGLAKSA
//