ID A0A091GLR4_BUCRH Unreviewed; 368 AA.
AC A0A091GLR4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=cathepsin E {ECO:0000256|ARBA:ARBA00013240};
DE EC=3.4.23.34 {ECO:0000256|ARBA:ARBA00013240};
DE Flags: Fragment;
GN ORFNames=N320_00863 {ECO:0000313|EMBL:KFO84516.1};
OS Buceros rhinoceros silvestris.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Bucerotiformes; Bucerotidae; Buceros.
OX NCBI_TaxID=175836 {ECO:0000313|EMBL:KFO84516.1, ECO:0000313|Proteomes:UP000054064};
RN [1] {ECO:0000313|EMBL:KFO84516.1, ECO:0000313|Proteomes:UP000054064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N320 {ECO:0000313|EMBL:KFO84516.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Similar to cathepsin D, but slightly broader specificity.;
CC EC=3.4.23.34; Evidence={ECO:0000256|ARBA:ARBA00001898};
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000256|ARBA:ARBA00011748}.
CC -!- SUBCELLULAR LOCATION: Endosome {ECO:0000256|ARBA:ARBA00004177}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KL504960; KFO84516.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091GLR4; -.
DR MEROPS; A01.010; -.
DR Proteomes; UP000054064; Unassembled WGS sequence.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
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:SF26; CATHEPSIN E; 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; 2.
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}; Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000054064}.
FT DOMAIN 56..365
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 74
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 254
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 245..249
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 287..324
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO84516.1"
FT NON_TER 368
FT /evidence="ECO:0000313|EMBL:KFO84516.1"
SQ SEQUENCE 368 AA; 40130 MW; CCD4B267B42487FE CRC64;
RVTLMRHRSL RKVLRDSGQL PHFWKAHRLD MVQYSEDCNV FTEANEPLIS YLDMEYFGQI
SIGTPPQNFT VVFDTGSSNL WLSSLSPVQH ARFQPSQSST YQAIGTPFSI QYGTGSLTGI
IGSDQVVVEG LTVSNQQFAE SVTEPGKAFL DVKFDGVLGL AYPSLAVDGV TPVFDNMMAQ
DLVDLPIFSV YLSSNPESPT GGEVLFGGFD PSHFTGTLNW VPVTQQGYWQ IQLDNIQLGG
AVAFCVNSCQ AIVDTGTSLI TGPTKDIKQL QNYIGATPVD GVYAVECSNL YMMPDLTFTI
NGLPYTLSAQ AYTLLEESDG TTFCSSGFQG LDINPPSGPL WILGDVFIRQ FYSVFDRGNN
RVGLAPAV
//
