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Database: UniProt
Entry: A0A093H4V1_GAVST
LinkDB: A0A093H4V1_GAVST
Original site: A0A093H4V1_GAVST 
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}.
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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
//
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