ID H0X8A6_OTOGA Unreviewed; 393 AA.
AC H0X8A6;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE RecName: Full=Cathepsin E {ECO:0000256|ARBA:ARBA00015580};
DE EC=3.4.23.34 {ECO:0000256|ARBA:ARBA00013240};
GN Name=CTSE {ECO:0000313|Ensembl:ENSOGAP00000011698.2};
OS Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC Galagidae; Otolemur.
OX NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000011698.2, ECO:0000313|Proteomes:UP000005225};
RN [1] {ECO:0000313|Proteomes:UP000005225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA Walker B.J., Sharpe T., Hall G.;
RT "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby).";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSOGAP00000011698.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- FUNCTION: May have a role in immune function. Probably involved in the
CC processing of antigenic peptides during MHC class II-mediated antigen
CC presentation. May play a role in activation-induced lymphocyte
CC depletion in the thymus, and in neuronal degeneration and glial cell
CC activation in the brain. {ECO:0000256|ARBA:ARBA00024985}.
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; AAQR03088841; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03088842; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H0X8A6; -.
DR Ensembl; ENSOGAT00000013062.2; ENSOGAP00000011698.2; ENSOGAG00000013057.2.
DR GeneTree; ENSGT00940000161300; -.
DR HOGENOM; CLU_013253_3_0_1; -.
DR Proteomes; UP000005225; 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; 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; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
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:UP000005225};
KW Signal {ECO:0000256|SAM:SignalP}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..393
FT /note="Cathepsin E"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003545275"
FT DOMAIN 76..390
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 94
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 281
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 107..112
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 272..276
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 315..350
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 393 AA; 43837 MW; 405E4BE1E612BBBB CRC64;
MHLLLLLVLL HLEQAQGSLH RVPLTRYPSL RKKLQEPDQL SEFCKSLDLE MTQQNNSCLM
ALAVKEPLTN YLDVEYFGNI SIGSPPQNFT VCFDTGSPDF WVPSAFCKSR ACKKHAKFCP
SQSNTHTRLE GKTFSIQYGT GSCSGIIGVD RVSVGGLTVP NQPFGEALKE PGKVFAHVQF
DGIMGLSYPS LAEDGMTPVF DNMITQKLVD QPIFSIYMSS TNQKGGKGSE LIFGGYDHSH
FTGRLNWVPV SKQEYWQIKV DKIRVGRSVM LCSKGCQAIV DTGTSSITGP SDDIRQLQKA
IRAVRRKNGD YTVRCNKLKV MPDVTIVIKG VSYTLKPTAY TLRSQGKKFC RTGFEEFDIS
DDEPLWILGN VFIRQFYSVF DRGNNRVGLA RAV
//