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 //