ID A0A093C8M4_TAUER Unreviewed; 368 AA.
AC A0A093C8M4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 22-FEB-2023, entry version 31.
DE SubName: Full=Gastricsin {ECO:0000313|EMBL:KFV12300.1};
GN ORFNames=N340_08918 {ECO:0000313|EMBL:KFV12300.1};
OS Tauraco erythrolophus (Red-crested turaco).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Musophagiformes; Musophagidae; Tauraco.
OX NCBI_TaxID=121530 {ECO:0000313|EMBL:KFV12300.1, ECO:0000313|Proteomes:UP000053661};
RN [1] {ECO:0000313|EMBL:KFV12300.1, ECO:0000313|Proteomes:UP000053661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N340 {ECO:0000313|EMBL:KFV12300.1};
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; KL460348; KFV12300.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093C8M4; -.
DR Proteomes; UP000053661; 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:UP000053661};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..368
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001883087"
FT DOMAIN 73..365
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 91
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 267
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 104..110
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 368 AA; 41205 MW; FA16E61EAB4E165F CRC64;
MKWLVLVLVC LQLSEGLVRI KLKKAKSIRE KMKEAGVLED YLKKIKYDPV KKYRFSKDHV
VYEPMTNHLD SSYFGEISIG TPPQNFLVLF DTGSSNLWVP STLCRTLACC EYRNRVAQST
PSTRAYGSLA VVLGYDTLTI QSIKVTNQEF GLSEYEPTEP FYYAEFDGIL GMAYPSLAVG
GTPTALQGML QQNQLAEPIF SFYFSRRPTY SYGGELILGG VDTQLFQGDI VWAPVSRELY
WQVTLDEFVI GQSATGWCSE GCQAVVDTGT GCCSSHNLLF TLSPQYAVDC NKIKNMPTLT
FIINGAELPL HPSSYVSNVY GYCTLGVEAT YLYSLNDQPL WILGDVFLKE YYTIFDMANN
RLGFAVSV
//