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Database: UniProt
Entry: A0A0Q3TEK1_AMAAE
LinkDB: A0A0Q3TEK1_AMAAE
Original site: A0A0Q3TEK1_AMAAE 
ID   A0A0Q3TEK1_AMAAE        Unreviewed;       405 AA.
AC   A0A0Q3TEK1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   22-FEB-2023, entry version 24.
DE   SubName: Full=Gastricsin isoform X2 {ECO:0000313|EMBL:KQL52041.1};
GN   ORFNames=AAES_31993 {ECO:0000313|EMBL:KQL52041.1};
OS   Amazona aestiva (Blue-fronted Amazon parrot).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona.
OX   NCBI_TaxID=12930 {ECO:0000313|EMBL:KQL52041.1, ECO:0000313|Proteomes:UP000051836};
RN   [1] {ECO:0000313|EMBL:KQL52041.1, ECO:0000313|Proteomes:UP000051836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FVVF132 {ECO:0000313|EMBL:KQL52041.1};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQL52041.1}.
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DR   EMBL; LMAW01000447; KQL52041.1; -; Genomic_DNA.
DR   STRING; 12930.A0A0Q3TEK1; -.
DR   Proteomes; UP000051836; 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; 2.60.40.1960; -; 1.
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; 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:SF70; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF07966; A1_Propeptide; 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|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR601461-2};
KW   Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051836};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..405
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006207914"
FT   DOMAIN          72..402
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        90
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        276
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        103..108
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   405 AA;  44949 MW;  912A4566F24F4523 CRC64;
     MKWLVLALVC LQLSEAVVRI KLKKGKSIRE NMKKAGVLED YLRERKHHAA KKXFGEDFVV
     YEPITSHLDS SYFGEISIGD PPQNFTVLFD TGSSNLWVPS TYCRTPACYN HMKFRPGESS
     TFVTNGQSYT LSYGSGALTV LLGYDTLRIQ SITVTNQEXG LSEDEPTQPF YYADFDGILG
     MAYPSLAVGG TPTVLQGMLE QNQLAXPIFS FYFSRNPTYS YGGELILGGV DPQLYYGDIT
     WAPVTQELYW QVAINEFAIG QSRTDWCRQG CQGIVDTGTF LLTVPEEYIE SFLQALGAQL
     TSYGYAVDCN EIQNMPPITF VINGAQLPLP PSAXVLXVRS CSLPEALSPV IPLLQNSGYC
     TLGIEITYLP SQSGQPLWIL GDVFLKEYYT IFDMANNLIG FXPSL
//
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