ID V8PCR8_OPHHA Unreviewed; 392 AA.
AC V8PCR8;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=cathepsin E {ECO:0000256|ARBA:ARBA00013240};
DE EC=3.4.23.34 {ECO:0000256|ARBA:ARBA00013240};
GN Name=CTSE {ECO:0000313|EMBL:ETE71687.1};
GN ORFNames=L345_02489 {ECO:0000313|EMBL:ETE71687.1};
OS Ophiophagus hannah (King cobra) (Naja hannah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE71687.1, ECO:0000313|Proteomes:UP000018936};
RN [1] {ECO:0000313|EMBL:ETE71687.1, ECO:0000313|Proteomes:UP000018936}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Blood {ECO:0000313|EMBL:ETE71687.1};
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETE71687.1}.
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DR EMBL; AZIM01000327; ETE71687.1; -; Genomic_DNA.
DR AlphaFoldDB; V8PCR8; -.
DR MEROPS; A01.010; -.
DR Proteomes; UP000018936; 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:UP000018936};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..392
FT /note="cathepsin E"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004771378"
FT DOMAIN 74..388
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 92
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 277
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 105..110
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 268..272
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 392 AA; 43568 MW; ACC78D18A47C24FB CRC64;
MNWLIFLMFN IWMTSGLQRV TLKRHRSLRQ ILRERGQLPQ FWKKYKIDMI QYTQDCSVFK
ETNEPLLNYL DVEYFGQISI GNPPQNFTVL FDTGSSNLWV PSIYCVSKAC VEHSRFHPSQ
SSTYTEVGTP FSIHYGTGSL TGIIGMDQVT VEGLTIVNQQ FAESVSEPGN TFLDSEFDGI
LGLAYPSLAV DGVTPVFDNM MAQNLVDLPI FSVYMNRNPY SSVGGELIFG GYDEAYFSGN
LNWIPVTKQG YWQILLDNIQ VGGNVAFCAD GCQAIVDTGT SLITGPSEDI KQMQTLIGAE
PMDGEYAVEC NYLNVMPLVT FTINGNSYPL TPEAYTVMVN SDGMNLCTSG FQSLDIETAD
GPLWILGDVF IGQYYSVFDR GNNRVGLAPI VS
//
