ID A0A091K8W3_COLST Unreviewed; 373 AA.
AC A0A091K8W3;
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=N325_08235 {ECO:0000313|EMBL:KFP32776.1};
OS Colius striatus (Speckled mousebird).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Coliiformes; Coliidae; Colius.
OX NCBI_TaxID=57412 {ECO:0000313|EMBL:KFP32776.1, ECO:0000313|Proteomes:UP000053615};
RN [1] {ECO:0000313|EMBL:KFP32776.1, ECO:0000313|Proteomes:UP000053615}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N325 {ECO:0000313|EMBL:KFP32776.1};
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; KK547468; KFP32776.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091K8W3; -.
DR MEROPS; A01.010; -.
DR Proteomes; UP000053615; 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:UP000053615}.
FT DOMAIN 56..370
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 74
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 259
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 87..92
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 250..254
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP32776.1"
FT NON_TER 373
FT /evidence="ECO:0000313|EMBL:KFP32776.1"
SQ SEQUENCE 373 AA; 40601 MW; 7F987E20EA19FCDF CRC64;
RVTLVRHRSL RKSLRDRGQL SHFWKAHRLN MVQYSEDCSA FTEANEPLIN YLDMEYFGQI
SIGTPPQNFT VIFDTGSSNL WVPSVYCVSK ACDAHTKFQP SQSSTYQAIG IPFSIQYGTG
SLTGVIGSDQ VVIEGLTVSN QQFAESVSEP GKAFLDAEFD GVLGLAYPSL AVDGITPVFD
NMMAQNLVEL PMFSVYMSTN PESSLGGELL FGGFDPSRFT GTLNWVPVTQ QGYWQIQLDN
IQLAGSVAFC ENGCQAIVDT GTSLITGPTK DIKELQSSIG ATPVDGEYAV ECSNLSIMPN
VTFTINGLPY TLSAQAYTLM EYSDGMAFCT SGFQGMDIAP PAGPLWILGD VFIRQFYSVF
DRGNNRVGLA PAV
//
