CATE_RAT
ID CATE_RAT Reviewed; 398 AA.
AC P16228; Q63701;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 3.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Cathepsin E;
DE EC=3.4.23.34;
DE Flags: Precursor;
GN Name=Ctse;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANT SER-114.
RC TISSUE=Spleen;
RX PubMed=7574663; DOI=10.1006/abbi.1995.1441;
RA Okamoto K., Yu H., Misumi Y., Ikehara Y., Yamamoto K.;
RT "Isolation and sequencing of two cDNA clones encoding rat spleen cathepsin
RT E and analysis of the activation of purified procathepsin E.";
RL Arch. Biochem. Biophys. 322:103-111(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 59-110, AND GLYCOSYLATION.
RX PubMed=2105725; DOI=10.1016/0006-291x(90)90914-9;
RA Yonezawa S., Takahashi T., Ichinose M., Miki K., Tanaka J., Gasa S.;
RT "Structural studies of rat cathepsin E: amino-terminal structure and
RT carbohydrate units of mature enzyme.";
RL Biochem. Biophys. Res. Commun. 166:1032-1038(1990).
RN [4]
RP GLYCOSYLATION.
RX PubMed=8346912; DOI=10.1006/abbi.1993.1361;
RA Takeda-Ezaki M., Yamamoto K.;
RT "Isolation and biochemical characterization of procathepsin E from human
RT erythrocyte membranes.";
RL Arch. Biochem. Biophys. 304:352-358(1993).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=8339772; DOI=10.1006/exnr.1993.1088;
RA Nakanishi H., Tsukuba T., Kondou T., Tanaka T., Yamamoto K.;
RT "Transient forebrain ischemia induces increased expression and specific
RT localization of cathepsins E and D in rat hippocampus and neostriatum.";
RL Exp. Neurol. 121:215-223(1993).
RN [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=8491674; DOI=10.1007/bf00269138;
RA Finzi G., Cornaggia M., Capella C., Fiocca R., Bosi F., Solcia E.,
RA Samloff I.M.;
RT "Cathepsin E in follicle associated epithelium of intestine and tonsils:
RT localization to M cells and possible role in antigen processing.";
RL Histochemistry 99:201-211(1993).
RN [7]
RP CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=8157122; DOI=10.1006/exnr.1994.1048;
RA Nakanishi H., Tominaga K., Amano T., Hirotsu I., Inoue T., Yamamoto K.;
RT "Age-related changes in activities and localizations of cathepsins D, E, B,
RT and L in the rat brain tissues.";
RL Exp. Neurol. 126:119-128(1994).
RN [8]
RP TISSUE SPECIFICITY, AND DEXAMETHASONE ADMINISTRATION.
RX PubMed=8809073; DOI=10.1006/abbi.1996.0401;
RA Nishishita K., Sakai H., Sakai E., Kato Y., Yamamoto K.;
RT "Age-related and dexamethasone-induced changes in cathepsins E and D in rat
RT thymic and splenic cells.";
RL Arch. Biochem. Biophys. 333:349-358(1996).
RN [9]
RP SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION.
RX PubMed=9572291; DOI=10.1046/j.1471-4159.1998.70052045.x;
RA Sastradipura D.F., Nakanishi H., Tsukuba T., Nishishita K., Sakai H.,
RA Kato Y., Gotow T., Uchiyama Y., Yamamoto K.;
RT "Identification of cellular compartments involved in processing of
RT cathepsin E in primary cultures of rat microglia.";
RL J. Neurochem. 70:2045-2056(1998).
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 (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Similar to cathepsin D, but slightly broader specificity.;
CC EC=3.4.23.34; Evidence={ECO:0000269|PubMed:8157122};
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:9572291}.
CC -!- SUBCELLULAR LOCATION: Endosome {ECO:0000269|PubMed:8491674,
CC ECO:0000269|PubMed:9572291}. Note=The proenzyme is localized to the
CC endoplasmic reticulum and Golgi apparatus, while the mature enzyme is
CC localized to the endosome.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P16228-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P16228-2; Sequence=VSP_005224;
CC -!- TISSUE SPECIFICITY: Expressed abundantly in lymphocytes and macrophages
CC of the thymus and spleen, and in the M cells of the intestine. In the
CC brain, expression is limited to reactive microglial cells, the large
CC pyrimidial neurons in the cerebral cortex, the CA1 and CA3 pyrimidial
CC neurons of the hippocampus, the large neurons of the neostriatum, and
CC the Purkinje neurons of the cerebellum. {ECO:0000269|PubMed:8157122,
CC ECO:0000269|PubMed:8339772, ECO:0000269|PubMed:8491674,
CC ECO:0000269|PubMed:8809073, ECO:0000269|PubMed:9572291}.
CC -!- DEVELOPMENTAL STAGE: Expression increases in all brain regions examined
CC with age, and increases markedly in reactive microglial cells amd CA1
CC pyrimidial neurons following ischemic injury. In the thymus expression
CC increased steadily up to 8 weeks of age before decreasing to a much
CC lower level by 52 weeks. Expression levels in the spleen and stomach do
CC not appear to vary with age. {ECO:0000269|PubMed:8157122}.
CC -!- PTM: Glycosylated. The nature of the carbohydrate chain varies between
CC cell types. In brain microglia, the proenzyme contains a high mannose-
CC type oligosaccharide, while the mature enzyme contains a complex-type
CC oligosaccharide. In stomach and spleen, the mature enzyme contains a
CC high mannose-type oligosaccharide. In erythrocyte membranes, the mature
CC enzyme contains a complex-type oligosaccharide.
CC {ECO:0000269|PubMed:2105725, ECO:0000269|PubMed:8346912,
CC ECO:0000269|PubMed:9572291}.
CC -!- MISCELLANEOUS: Administration of dexamethasone results in the
CC conversion of the proenzyme to the mature form in thymocytes.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; D38104; BAA07285.1; -; mRNA.
DR EMBL; D45187; BAA08128.1; -; mRNA.
DR EMBL; BC062002; AAH62002.1; -; mRNA.
DR PIR; A34657; A34657.
DR PIR; S66465; S66465.
DR PIR; S66466; S66466.
DR RefSeq; NP_037070.1; NM_012938.1.
DR RefSeq; XP_006249810.1; XM_006249748.2. [P16228-1]
DR RefSeq; XP_006249811.1; XM_006249749.2. [P16228-1]
DR RefSeq; XP_017454166.1; XM_017598677.1. [P16228-1]
DR AlphaFoldDB; P16228; -.
DR SMR; P16228; -.
DR STRING; 10116.ENSRNOP00000048353; -.
DR MEROPS; A01.010; -.
DR GlyGen; P16228; 1 site.
DR PaxDb; P16228; -.
DR Ensembl; ENSRNOT00000009241; ENSRNOP00000009242; ENSRNOG00000006963. [P16228-2]
DR Ensembl; ENSRNOT00000048391; ENSRNOP00000048353; ENSRNOG00000006963. [P16228-1]
DR GeneID; 25424; -.
DR KEGG; rno:25424; -.
DR UCSC; RGD:2446; rat. [P16228-1]
DR CTD; 1510; -.
DR RGD; 2446; Ctse.
DR eggNOG; KOG1339; Eukaryota.
DR GeneTree; ENSGT00940000161300; -.
DR HOGENOM; CLU_013253_3_0_1; -.
DR InParanoid; P16228; -.
DR OMA; GVECANL; -.
DR OrthoDB; 1619495at2759; -.
DR PhylomeDB; P16228; -.
DR TreeFam; TF314990; -.
DR BRENDA; 3.4.23.34; 5301.
DR Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR PRO; PR:P16228; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000006963; Expressed in stomach and 17 other tissues.
DR Genevisible; P16228; RN.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0008233; F:peptidase activity; ISO:RGD.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IDA:UniProtKB.
DR GO; GO:0016540; P:protein autoprocessing; IMP:RGD.
DR GO; GO:0006508; P:proteolysis; ISO:RGD.
DR Gene3D; 2.40.70.10; -; 2.
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; PTHR47966; 1.
DR PANTHER; PTHR47966:SF26; PTHR47966:SF26; 1.
DR Pfam; PF07966; A1_Propeptide; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Aspartyl protease; Autocatalytic cleavage;
KW Direct protein sequencing; Disulfide bond; Endosome; Glycoprotein;
KW Hydrolase; Protease; Reference proteome; Signal; Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000250"
FT PROPEP 22..58
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:2105725"
FT /id="PRO_0000025980"
FT CHAIN 59..398
FT /note="Cathepsin E"
FT /id="PRO_0000025981"
FT DOMAIN 80..394
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 98
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 283
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 62
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 111..116
FT /evidence="ECO:0000250"
FT DISULFID 274..278
FT /evidence="ECO:0000250"
FT VAR_SEQ 312..344
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7574663"
FT /id="VSP_005224"
FT VARIANT 114
FT /note="P -> S"
FT /evidence="ECO:0000269|PubMed:7574663"
FT CONFLICT 55
FT /note="M -> V (in Ref. 2; AAH62002)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="E -> N (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 83..84
FT /note="TV -> SR (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 398 AA; 43021 MW; 25F123E67C46EB5F CRC64;
MKPLFVLLLL LLLLDLAQAQ GVLHRVPLRR HQSLRKKLRA QGQLSDFWRS HNLDMIEFSE
SCNVDKGINE PLINYLDMEY FGTVSIGSPS QNFTVIFDTG SSNLWVPSVY CTSPACKAHP
VFHPSQSSTY MEVGNHFSIQ YGTGSLTGII GADQVSVEGL TVEGQQFGES VKEPGQTFVN
AEFDGILGLG YPSLAVGGVT PVFDNMMAQN LVALPMFSVY LSSDPQGGSG SELTFGGYDP
SHFSGSLNWI PVTKQGYWQI ALDGIQVGDT VMFCSEGCQA IVDTGTSLIT GPPKKIKQLQ
EAIGATPMDG EYAVDCATLN MMPNVTFLIN GVSYTLSPTA YILPDLVDGM QFCGSGFQGL
DIQPPAGPLW ILGDVFIRKF YSVFDRGNNQ VGLAPAVP
