ID A0A091H8Y1_9AVES Unreviewed; 400 AA.
AC A0A091H8Y1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Gastricsin {ECO:0000313|EMBL:KFO82692.1};
DE Flags: Fragment;
GN ORFNames=N303_11101 {ECO:0000313|EMBL:KFO82692.1};
OS Cuculus canorus (common cuckoo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO82692.1, ECO:0000313|Proteomes:UP000053760};
RN [1] {ECO:0000313|EMBL:KFO82692.1, ECO:0000313|Proteomes:UP000053760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO82692.1};
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; KL448316; KFO82692.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091H8Y1; -.
DR STRING; 55661.A0A091H8Y1; -.
DR MEROPS; A01.002; -.
DR Proteomes; UP000053760; 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; IPR018222; Nuclear_transport_factor_2_euk.
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; PS50177; NTF2_DOMAIN; 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:UP000053760};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..400
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001874410"
FT DOMAIN 71..400
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT DOMAIN 378..400
FT /note="NTF2"
FT /evidence="ECO:0000259|PROSITE:PS50177"
FT ACT_SITE 89
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 275
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 102..107
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 325..358
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT NON_TER 400
FT /evidence="ECO:0000313|EMBL:KFO82692.1"
SQ SEQUENCE 400 AA; 44702 MW; 9BA550CB177DF1FD CRC64;
MQWLVLVLLC LRLGEGVMRI PLRKAKSVGE RMKEKGVPEM FLKELKGDPG RKYQLSNVAY
EPLTNYLDTF YFGEISIGNP PQNFMVIFDT GSANLWVPST YCRSPACEDH ARFNPNLSSN
FSNIGVTYTL SYGFGDVSVV LGYDTVTIQN IVITNQEFGL TLEEPTQPFY YLEFDGILGM
SYPGVGLRGY NTLLQNMLQQ NQLTEPIFSF YYSRNPTYNY GGEVILGGVD PELYSGEILW
APVVQELYWK IGIEEFSIGS STTGWCNQGC HGIVDTGTFL LTIPQQFMSA FLQALGAEEI
DYNVAPVVLT TRPLFLLLFQ FVVDCNNVPN MPTLYFAISG AQLPLPPSVY VLENNGTCTV
GVETTYVASD SGQPLWILGN IFLRQYYSIF DMANNRVGLA
//
