ID   A0A087QMX4_APTFO        Unreviewed;       263 AA.
AC   A0A087QMX4;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Embryonic pepsinogen {ECO:0000313|EMBL:KFM02578.1};
DE   Flags: Fragment;
GN   ORFNames=AS27_08013 {ECO:0000313|EMBL:KFM02578.1};
OS   Aptenodytes forsteri (Emperor penguin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC   Aptenodytes.
OX   NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM02578.1, ECO:0000313|Proteomes:UP000053286};
RN   [1] {ECO:0000313|EMBL:KFM02578.1, ECO:0000313|Proteomes:UP000053286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM02578.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) 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; KL225746; KFM02578.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A087QMX4; -.
DR   STRING; 9233.A0A087QMX4; -.
DR   MEROPS; A01.028; -.
DR   Proteomes; UP000053286; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 6.10.140.60; -; 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:SF13; CHYMOSIN; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053286}.
FT   DOMAIN          59..263
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        77
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        259
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        90..95
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   DISULFID        250..254
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFM02578.1"
FT   NON_TER         263
FT                   /evidence="ECO:0000313|EMBL:KFM02578.1"
SQ   SEQUENCE   263 AA;  28793 MW;  CCF8DA42393866C0 CRC64;
     ARLPLERGKK LREVLREKGL LCRFFQHHRY DIGTKFPHVF PNGTEVATEP LLNTLDMEYY
     GTISIGTPPQ DFTVVFDTGS SNLWVPSVSC TSLACQNHQM FNPSQSSTYK STGQNLSIQY
     GTGDMEGIVG SDTITVASLV DTNQLFGLST TEPGQFFVHV KFDGILGLGY PNLAADGIMP
     VFDNLVNESL LEENLFSVYL SRETTGSVVI FGGIDESYFT GSINWISVSY QGYWQISMDS
     IIVNSQEIAC SGGCQAIVDT GTS
//