ID   A0A7I2V480_HUMAN        Unreviewed;       363 AA.
AC   A0A7I2V480;
DT   07-APR-2021, integrated into UniProtKB/TrEMBL.
DT   07-APR-2021, sequence version 1.
DT   14-DEC-2022, entry version 7.
DE   RecName: Full=Cathepsin E {ECO:0000256|ARBA:ARBA00015580};
DE            EC=3.4.23.34 {ECO:0000256|ARBA:ARBA00013240};
GN   Name=CTSE {ECO:0000313|Ensembl:ENSP00000503796.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000503796.1, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000503796.1, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H.,
RA   Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C.,
RA   Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R.,
RA   Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A.,
RA   Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.,
RA   Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.,
RA   Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R.,
RA   Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D.,
RA   Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A.,
RA   Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S., McLaren S., Milne S.,
RA   Mistry S., Moore M.J., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A.,
RA   Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S.,
RA   Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G.,
RA   Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S.,
RA   Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A.,
RA   Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L.,
RA   Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z.,
RA   Coulson A., Vaudin M., Sulston J.E., Durbin R., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   Beck S., Rogers J., Bentley D.R., Banerjee R., Bryant S.P., Burford D.C.,
RA   Burrill W.D., Clegg S.M., Dhami P., Dovey O., Faulkner L.M., Gribble S.M.,
RA   Langford C.F., Pandian R.D., Porter K.M., Prigmore E.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [2] {ECO:0000313|Ensembl:ENSP00000503796.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2022) to UniProtKB.
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; BX571818; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; FO535328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A7I2V480; -.
DR   SMR; A0A7I2V480; -.
DR   Ensembl; ENST00000678712.1; ENSP00000503796.1; ENSG00000196188.12.
DR   HGNC; HGNC:2530; CTSE.
DR   GeneTree; ENSGT00940000161300; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   Bgee; ENSG00000196188; Expressed in jejunal mucosa and 114 other tissues.
DR   GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016540; P:protein autoprocessing; IEA:InterPro.
DR   Gene3D; 2.40.70.10; -; 3.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR012848; Aspartic_peptidase_N.
DR   InterPro; IPR033145; Cathepsin_E.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 2.
DR   PANTHER; PTHR47966:SF26; CATHEPSIN E; 2.
DR   Pfam; PF07966; A1_Propeptide; 1.
DR   Pfam; PF00026; Asp; 2.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 2.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   1: Evidence at protein level;
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   Proteomics identification {ECO:0007829|PeptideAtlas:A0A7I2V480,
KW   ECO:0007829|ProteomicsDB:A0A7I2V480};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Signal {ECO:0000256|SAM:SignalP}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..363
FT                   /note="Cathepsin E"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5029632412"
FT   DOMAIN          78..363
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"
SQ   SEQUENCE   363 AA;  39219 MW;  CA3C91570A2B02D4 CRC64;
     MKTLLLLLLV LLELGEAQGS LHRVPLRRHP SLKKKLRARS QLSEFWKSHN LDMIQFTESC
     SMDQSAKEPL INYLDMEYFG TISIGSPPQN FTVIFDTGSS NLWVPSVYCT SPACKTHSRF
     QPSQSSTYSQ PGQSFSIQYG TGSLSGIIGA DQVSVEGLTV VGQQFGESVT EPGQTFVDAE
     FDGILGLGYP SLAVGGVTPV FDNMMAQNLV DLPMFSVYMS SNPEGGAGSE LIFGGYDHSH
     FSGSLNWVPV TKQAYWQIAL DNIQVGGTVM FCSEGCQAIV DTGTSLITGP SDKIKQLQNA
     IGAAPVDGED FVDGMQFCSS GFQGLDIHPP AGPLWILGDV FIRQFYSVFD RGNNRVGLAP
     AVP
//