ID L5MFU3_MYODS Unreviewed; 396 AA.
AC L5MFU3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Cathepsin E {ECO:0000256|ARBA:ARBA00015580};
DE EC=3.4.23.34 {ECO:0000256|ARBA:ARBA00013240};
GN ORFNames=MDA_GLEAN10010771 {ECO:0000313|EMBL:ELK37212.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK37212.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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}.
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; KB100879; ELK37212.1; -; Genomic_DNA.
DR RefSeq; XP_006754458.1; XM_006754395.2.
DR AlphaFoldDB; L5MFU3; -.
DR MEROPS; A01.010; -.
DR GeneID; 102753719; -.
DR KEGG; myd:102753719; -.
DR CTD; 1510; -.
DR eggNOG; KOG1339; Eukaryota.
DR OrthoDB; 1120702at2759; -.
DR Proteomes; UP000010556; 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 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:UP000010556};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..396
FT /note="Cathepsin E"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003971222"
FT DOMAIN 78..392
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 96
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 281
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 109..114
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 272..276
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 314..351
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 396 AA; 42992 MW; 7AE8858AD60D79E3 CRC64;
MKSLLLLLLL LPDLVRALGP LHRVPLRRRQ SLRKKLRARG QLSEFWKSQH LDMIQFTESC
TMDQSVNEPL VNYLDMEYFG TISIGSPPQN FTVIFDTGSS NLWVPSVYCT SPACKTHPRF
SPSQSSTYSS PGSHFFIQYG TGSLSGVIGE DQVSVEGLTV VGQQFGESVT EPGQTFVDAE
FDGILGLGYP SLAVGGVTPV FDNMMAQNLV DVPMFSVYMS SDPEGGAGSE LIFGGYDHSH
FSGSLNWVPV TKQGYWQIAL DTIQVGGAVM FCSEGCQAIV DTGTSLITGP PAEIKQLQKA
IGAEPVDGEY AVECDNLNVM PDVTFTINGV PYTLQPTAYT LLDFVDGMEF CSSGFQGLDI
QPPAGPLWIL GDVFIRQFYS VFDRGDNRVG LAPAVP
//
