ID A0A093BI66_CHAPE Unreviewed; 373 AA.
AC A0A093BI66;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=cathepsin E {ECO:0000256|ARBA:ARBA00013240};
DE EC=3.4.23.34 {ECO:0000256|ARBA:ARBA00013240};
DE Flags: Fragment;
GN ORFNames=M959_05003 {ECO:0000313|EMBL:KFU89492.1};
OS Chaetura pelagica (Chimney swift) (Hirundo pelagica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes; Apodidae;
OC Apodinae; Chaetura.
OX NCBI_TaxID=8897 {ECO:0000313|EMBL:KFU89492.1, ECO:0000313|Proteomes:UP000031515};
RN [1] {ECO:0000313|EMBL:KFU89492.1, ECO:0000313|Proteomes:UP000031515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M959 {ECO:0000313|EMBL:KFU89492.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000031515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=25504712; DOI=10.1126/science.1251385;
RG Avian Genome Consortium;
RA Zhang G., Li C., Li Q., Li B., Larkin D.M., Lee C., Storz J.F., Antunes A.,
RA Greenwold M.J., Meredith R.W., Odeen A., Cui J., Zhou Q., Xu L., Pan H.,
RA Wang Z., Jin L., Zhang P., Hu H., Yang W., Hu J., Xiao J., Yang Z., Liu Y.,
RA Xie Q., Yu H., Lian J., Wen P., Zhang F., Li H., Zeng Y., Xiong Z., Liu S.,
RA Zhou L., Huang Z., An N., Wang J., Zheng Q., Xiong Y., Wang G., Wang B.,
RA Wang J., Fan Y., da Fonseca R.R., Alfaro-Nunez A., Schubert M., Orlando L.,
RA Mourier T., Howard J.T., Ganapathy G., Pfenning A., Whitney O., Rivas M.V.,
RA Hara E., Smith J., Farre M., Narayan J., Slavov G., Romanov M.N.,
RA Borges R., Machado J.P., Khan I., Springer M.S., Gatesy J., Hoffmann F.G.,
RA Opazo J.C., Hastad O., Sawyer R.H., Kim H., Kim K.W., Kim H.J., Cho S.,
RA Li N., Huang Y., Bruford M.W., Zhan X., Dixon A., Bertelsen M.F.,
RA Derryberry E., Warren W., Wilson R.K., Li S., Ray D.A., Green R.E.,
RA O'Brien S.J., Griffin D., Johnson W.E., Haussler D., Ryder O.A.,
RA Willerslev E., Graves G.R., Alstrom P., Fjeldsa J., Mindell D.P.,
RA Edwards S.V., Braun E.L., Rahbek C., Burt D.W., Houde P., Zhang Y.,
RA Yang H., Wang J., Jarvis E.D., Gilbert M.T., Wang J.;
RT "Comparative genomics reveals insights into avian genome evolution and
RT adaptation.";
RL Science 346:1311-1320(2014).
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; KN126421; KFU89492.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093BI66; -.
DR MEROPS; A01.010; -.
DR Proteomes; UP000031515; 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; 2.40.70.10; 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:UP000031515}.
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 DISULFID 292..329
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFU89492.1"
FT NON_TER 373
FT /evidence="ECO:0000313|EMBL:KFU89492.1"
SQ SEQUENCE 373 AA; 40437 MW; D3CBE23EC1911EC4 CRC64;
RVALTRQRSL RQSLRDRGQL SHFWEAHRLD RLRYGEDCTA FSTANEPLIN YLDVEYFGQI
SIGTPPQNFT VVFDTGSSNL WVPSVYCISK ACAVHAKFHP SQSSTYQMVG TPFSIQYGTG
SLTGVIGSDQ VAIQGLTVNN QQFAESISEP GKTFLDAAFD GVLGLGYPSL AVGGITPVFD
NMMAQNLVEL PMFSVYLSKN AEVSRGGELL FGGFDPSHFT GTLNWVPVTR QGYWQIQLDN
IQVGGTVAFC ANGCQAIVDT GTSLINGPSK DVKELQNYIG ATPVDGVCTV DCNNLGVMPD
VTFTINGLPH TLSAQAYTLM EYIDGTTICT SGFQGSDVPP PTGPLWILGD VFIRQFYSVF
DRGNNRVGFA PAI
//
