ID   A0A091NRB4_APAVI        Unreviewed;       376 AA.
AC   A0A091NRB4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   22-FEB-2023, entry version 34.
DE   SubName: Full=Gastricsin {ECO:0000313|EMBL:KFP91896.1};
DE   Flags: Fragment;
GN   ORFNames=N311_06276 {ECO:0000313|EMBL:KFP91896.1};
OS   Apaloderma vittatum (Bar-tailed trogon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Trogoniformes; Trogonidae; Apaloderma.
OX   NCBI_TaxID=57397 {ECO:0000313|EMBL:KFP91896.1, ECO:0000313|Proteomes:UP000054244};
RN   [1] {ECO:0000313|EMBL:KFP91896.1, ECO:0000313|Proteomes:UP000054244}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N311 {ECO:0000313|EMBL:KFP91896.1};
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; KL391855; KFP91896.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091NRB4; -.
DR   Proteomes; UP000054244; 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:SF70; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 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:UP000054244};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..376
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001879048"
FT   DOMAIN          72..376
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   DISULFID        103..108
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   NON_TER         376
FT                   /evidence="ECO:0000313|EMBL:KFP91896.1"
SQ   SEQUENCE   376 AA;  41987 MW;  57AE1D79A9A7C8A2 CRC64;
     MRWLVLGLLC FHLGEGVVRI PLKKSRFLGE VMGEKVVPES FLKNLRGDPG RRYQPSNAVA
     YEPLMNYLDS FYFGEISIGT PPQNFLVLFD TGSANLWVPS IYCQTAACEN HARFNYNLSS
     TFSGTNVTYT LNYGFGDVSV ALGYDTVTIQ NMVVRNQEFG LSLNEPSSPF YYLYFDGILG
     MSYPGVGISG YNTLMENMLQ QDQLAEPVFS FYYSRNPTYD YGGEVILGGI DPQLYYGEIL
     WAPVVQEYYW KIDIEEFSIG PAATGWGSQR WPGVGVPGEF MSAFLQALGA EEDDYGFIVD
     CSNISIMPTL YFAISGTQLS LPPSVYVLNN NGVCTIGVET TYVSSTNGQP LWILGNIFLR
     QYYSIFDMAN NRVGFA
//