ID G3HAY9_CRIGR Unreviewed; 388 AA.
AC G3HAY9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Cathepsin E {ECO:0000256|ARBA:ARBA00015580};
DE EC=3.4.23.34 {ECO:0000256|ARBA:ARBA00013240};
GN ORFNames=I79_007601 {ECO:0000313|EMBL:EGV92814.1};
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029 {ECO:0000313|EMBL:EGV92814.1, ECO:0000313|Proteomes:UP000001075};
RN [1] {ECO:0000313|Proteomes:UP000001075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX PubMed=21804562; DOI=10.1038/nbt.1932;
RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA Famili I., Palsson B.O., Wang J.;
RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL Nat. Biotechnol. 29:735-741(2011).
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; JH000259; EGV92814.1; -; Genomic_DNA.
DR AlphaFoldDB; G3HAY9; -.
DR STRING; 10029.G3HAY9; -.
DR MEROPS; A01.010; -.
DR PaxDb; 10029-XP_007609139-1; -.
DR eggNOG; KOG1339; Eukaryota.
DR InParanoid; G3HAY9; -.
DR Proteomes; UP000001075; 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; 2.60.40.1960; -; 1.
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:UP000001075};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..388
FT /note="Cathepsin E"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003443944"
FT DOMAIN 78..384
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 96
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 273
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 109..114
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 264..268
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 388 AA; 42203 MW; D0A55FC27750B2C4 CRC64;
MKSLLALLLV LLDLGQAYGA IHRVPLRKHQ SIRKKLRARG KLSDFWKSQN LDMIQFSESC
KMDQSTNEPL INYLDVEYFG TISIGSPPQN FTVIFDTGSS NLWVPSVYCT SPACRKLRKE
DLAFIGTGTQ ESENLIQRTF VQFSLQVEGL TVDGQQFGES VKEPGQTFVN AEFDGILGLG
YPSLAVGGVT PVFDNMMAQN LVDLPIFSVY MSSDPQGGSG SELTFGGFDP SHFSGNLNWI
PVTKQGYWQI ALDGVQVGDT VMFCSEGCQA IVDTGTSLIT GPSHKIKQLQ EAIGATPMDG
EYAVDCANLN TMPNVAFILN GVSYTLSPTA YILPDLVDGM QFCGSGFQGL DIQPPSGPLW
ILGDVFIRQF YAVFDRGNNQ VGLAPAVP
//
