ID A0A091SJ45_9GRUI Unreviewed; 373 AA.
AC A0A091SJ45;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=cathepsin E {ECO:0000256|ARBA:ARBA00013240};
DE EC=3.4.23.34 {ECO:0000256|ARBA:ARBA00013240};
DE Flags: Fragment;
GN ORFNames=N332_09021 {ECO:0000313|EMBL:KFQ40270.1};
OS Mesitornis unicolor (brown roatelo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Mesitornithidae; Mesitornis.
OX NCBI_TaxID=54374 {ECO:0000313|EMBL:KFQ40270.1, ECO:0000313|Proteomes:UP000053369};
RN [1] {ECO:0000313|EMBL:KFQ40270.1, ECO:0000313|Proteomes:UP000053369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N332 {ECO:0000313|EMBL:KFQ40270.1};
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; KK821488; KFQ40270.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091SJ45; -.
DR MEROPS; A01.010; -.
DR Proteomes; UP000053369; 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; 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:UP000053369}.
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:KFQ40270.1"
FT NON_TER 373
FT /evidence="ECO:0000313|EMBL:KFQ40270.1"
SQ SEQUENCE 373 AA; 40616 MW; 8CCC317359A37C6B CRC64;
RVTLTRHRSL RKTLRARGQL SHFWKAHGLN MVQYSQDCTA FTEANEPLIT YLDLEYFGQI
SIGTPPQNFT VVFDTGSSNL WVPSVYCVSK ACTEHSRFQP SQSSTYQPIG TPFSIQYGTG
SLTGVIGSDQ VVVEGLTISN QQFAESVSEP GKAFLDAEFD GILGLAYPSL AVDGVTPVFD
NMMAQNLVEL PMFSVYLSSN PESSLGGELL FGGFDPSRFT GTLNWVPVTQ QGYWQIQLDN
IQLGGTVVFC ANGCQAIVDT GTSLVTGPTK DIKELQGYIG AMSVDGEFAV ECSNMNVMPD
VTFTINGLPY TLSAQAYTLM EYNDNMAFCT SGFQGLDITP PAGPLWILGD VFIRQFYSVF
DRGNNRVGLA PAV
//