ID A0A093H4V1_GAVST Unreviewed; 320 AA.
AC A0A093H4V1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=cathepsin E {ECO:0000256|ARBA:ARBA00013240};
DE EC=3.4.23.34 {ECO:0000256|ARBA:ARBA00013240};
DE Flags: Fragment;
GN ORFNames=N328_03996 {ECO:0000313|EMBL:KFV49693.1};
OS Gavia stellata (Red-throated diver) (Colymbus stellatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gaviiformes; Gaviidae; Gavia.
OX NCBI_TaxID=37040 {ECO:0000313|EMBL:KFV49693.1, ECO:0000313|Proteomes:UP000054313};
RN [1] {ECO:0000313|EMBL:KFV49693.1, ECO:0000313|Proteomes:UP000054313}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N328 {ECO:0000313|EMBL:KFV49693.1};
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; KK617954; KFV49693.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093H4V1; -.
DR MEROPS; A01.010; -.
DR Proteomes; UP000054313; 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; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
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; 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|PIRSR:PIRSR601461-2};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000054313}.
FT DOMAIN 2..317
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 20
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 205
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 33..38
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 196..200
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 238..276
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV49693.1"
FT NON_TER 320
FT /evidence="ECO:0000313|EMBL:KFV49693.1"
SQ SEQUENCE 320 AA; 34063 MW; DD8D2BF960ED719F CRC64;
EYFGQISIGT PPQNFTVVFD TGSSNLWVPS VYCVSKACAK HTKFQPSESS TYQAIGTPFS
IQYGTGSLMG VIGSDQVVVE GLTVSNQQFA ESVSEPGKTF LDAEFDGILG LAYPSLAVDG
VTPVFDNMMA QNLVELPMFS VYMSTNPESS LGGELLFGGF DPSRFTGTLN WVPVTQQGYW
QIQLDNIQLD GTVAFCVNGC QAIVDTGTSL ITGPTKDIKE LQSYIGATPV DGEPTASCTA
PAVTIPACFH VHEALGFVPS LALLLPQENS DGMAFCISGF QGMDTAPPAG PLWILGDVFI
RQFYSVFDRG NNRVGLAPAV
//