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
//