ID A0A091UFJ7_PHORB Unreviewed; 384 AA.
AC A0A091UFJ7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 22-FEB-2023, entry version 33.
DE SubName: Full=Gastricsin {ECO:0000313|EMBL:KFQ89514.1};
DE Flags: Fragment;
GN ORFNames=N337_08198 {ECO:0000313|EMBL:KFQ89514.1};
OS Phoenicopterus ruber ruber.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Phoenicopteriformes; Phoenicopteridae;
OC Phoenicopterus.
OX NCBI_TaxID=9218 {ECO:0000313|EMBL:KFQ89514.1, ECO:0000313|Proteomes:UP000053700};
RN [1] {ECO:0000313|EMBL:KFQ89514.1, ECO:0000313|Proteomes:UP000053700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N337 {ECO:0000313|EMBL:KFQ89514.1};
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; KK433165; KFQ89514.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091UFJ7; -.
DR MEROPS; A01.002; -.
DR Proteomes; UP000053700; 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; 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:UP000053700};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..384
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001882658"
FT DOMAIN 73..384
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 91
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 277
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 104..109
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 309..342
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT NON_TER 384
FT /evidence="ECO:0000313|EMBL:KFQ89514.1"
SQ SEQUENCE 384 AA; 42900 MW; 50F2FE18CBE6D8C8 CRC64;
MKWLVLALVC LQVSEGLVRV NLKKAKSIRE KMREAGVLED YLKKIKYDPV KKYSFSEDYV
VYEPITNHLD SSYFGEISIG TPPQNFLVLF DTGSSNLWVP STYCQTAACF NHMKFNPNES
SSFTYDGQSY TLSYGSGALT VVLGYDTLRI QSITVTNQAF GLSQDEPTQP FYYAEFDGIL
GMAYPSLAAG EMPTALQGML QQNQLTQPIF SFYFSRKPTY SYGGELILGG VDTRHFRGDI
KWAPVTQKLY WQVALDEFAI GQSATSWCSQ GCQAIVDTGT YLLTVPQQYL NSSLQALGAQ
LTSYGVIDCN EVQNMPTITF VINGARLPLY PSAYVLNSNG YCTLGIEPTY LPSQNGQPLW
ILGDVFLKEY YTVFDMAKNR IGFA
//
