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Cathepsin E (EC 3.4.23.34)

 CATE_RAT                Reviewed;         398 AA.
P16228; Q63701;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
15-JUL-1998, sequence version 3.
22-NOV-2017, entry version 158.
RecName: Full=Cathepsin E;
EC=3.4.23.34;
Flags: Precursor;
Name=Ctse;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANT SER-114.
TISSUE=Spleen;
PubMed=7574663; DOI=10.1006/abbi.1995.1441;
Okamoto K., Yu H., Misumi Y., Ikehara Y., Yamamoto K.;
"Isolation and sequencing of two cDNA clones encoding rat spleen
cathepsin E and analysis of the activation of purified procathepsin
E.";
Arch. Biochem. Biophys. 322:103-111(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Prostate;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PROTEIN SEQUENCE OF 59-110, AND GLYCOSYLATION.
PubMed=2105725; DOI=10.1016/0006-291X(90)90914-9;
Yonezawa S., Takahashi T., Ichinose M., Miki K., Tanaka J., Gasa S.;
"Structural studies of rat cathepsin E: amino-terminal structure and
carbohydrate units of mature enzyme.";
Biochem. Biophys. Res. Commun. 166:1032-1038(1990).
[4]
GLYCOSYLATION.
PubMed=8346912; DOI=10.1006/abbi.1993.1361;
Takeda-Ezaki M., Yamamoto K.;
"Isolation and biochemical characterization of procathepsin E from
human erythrocyte membranes.";
Arch. Biochem. Biophys. 304:352-358(1993).
[5]
TISSUE SPECIFICITY.
PubMed=8339772; DOI=10.1006/exnr.1993.1088;
Nakanishi H., Tsukuba T., Kondou T., Tanaka T., Yamamoto K.;
"Transient forebrain ischemia induces increased expression and
specific localization of cathepsins E and D in rat hippocampus and
neostriatum.";
Exp. Neurol. 121:215-223(1993).
[6]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=8491674; DOI=10.1007/BF00269138;
Finzi G., Cornaggia M., Capella C., Fiocca R., Bosi F., Solcia E.,
Samloff I.M.;
"Cathepsin E in follicle associated epithelium of intestine and
tonsils: localization to M cells and possible role in antigen
processing.";
Histochemistry 99:201-211(1993).
[7]
CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=8157122; DOI=10.1006/exnr.1994.1048;
Nakanishi H., Tominaga K., Amano T., Hirotsu I., Inoue T.,
Yamamoto K.;
"Age-related changes in activities and localizations of cathepsins D,
E, B, and L in the rat brain tissues.";
Exp. Neurol. 126:119-128(1994).
[8]
TISSUE SPECIFICITY, AND DEXAMETHASONE ADMINISTRATION.
PubMed=8809073; DOI=10.1006/abbi.1996.0401;
Nishishita K., Sakai H., Sakai E., Kato Y., Yamamoto K.;
"Age-related and dexamethasone-induced changes in cathepsins E and D
in rat thymic and splenic cells.";
Arch. Biochem. Biophys. 333:349-358(1996).
[9]
SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION.
PubMed=9572291;
Sastradipura D.F., Nakanishi H., Tsukuba T., Nishishita K., Sakai H.,
Kato Y., Gotow T., Uchiyama Y., Yamamoto K.;
"Identification of cellular compartments involved in processing of
cathepsin E in primary cultures of rat microglia.";
J. Neurochem. 70:2045-2056(1998).
-!- FUNCTION: May have a role in immune function. Probably involved in
the processing of antigenic peptides during MHC class II-mediated
antigen presentation. May play a role in activation-induced
lymphocyte depletion in the thymus, and in neuronal degeneration
and glial cell activation in the brain (By similarity).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: Similar to cathepsin D, but slightly broader
specificity. {ECO:0000269|PubMed:8157122}.
-!- SUBUNIT: Homodimer; disulfide-linked.
{ECO:0000269|PubMed:9572291}.
-!- SUBCELLULAR LOCATION: Endosome {ECO:0000269|PubMed:8491674,
ECO:0000269|PubMed:9572291}. Note=The proenzyme is localized to
the endoplasmic reticulum and Golgi apparatus, while the mature
enzyme is localized to the endosome.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P16228-1; Sequence=Displayed;
Name=2;
IsoId=P16228-2; Sequence=VSP_005224;
-!- TISSUE SPECIFICITY: Expressed abundantly in lymphocytes and
macrophages of the thymus and spleen, and in the M cells of the
intestine. In the brain, expression is limited to reactive
microglial cells, the large pyrimidial neurons in the cerebral
cortex, the CA1 and CA3 pyrimidial neurons of the hippocampus, the
large neurons of the neostriatum, and the Purkinje neurons of the
cerebellum. {ECO:0000269|PubMed:8157122,
ECO:0000269|PubMed:8339772, ECO:0000269|PubMed:8491674,
ECO:0000269|PubMed:8809073, ECO:0000269|PubMed:9572291}.
-!- DEVELOPMENTAL STAGE: Expression increases in all brain regions
examined with age, and increases markedly in reactive microglial
cells amd CA1 pyrimidial neurons following ischemic injury. In the
thymus expression increased steadily up to 8 weeks of age before
decreasing to a much lower level by 52 weeks. Expression levels in
the spleen and stomach do not appear to vary with age.
{ECO:0000269|PubMed:8157122}.
-!- PTM: Glycosylated. The nature of the carbohydrate chain varies
between cell types. In brain microglia, the proenzyme contains a
high mannose-type oligosaccharide, while the mature enzyme
contains a complex-type oligosaccharide. In stomach and spleen,
the mature enzyme contains a high mannose-type oligosaccharide. In
erythrocyte membranes, the mature enzyme contains a complex-type
oligosaccharide. {ECO:0000269|PubMed:2105725,
ECO:0000269|PubMed:8346912, ECO:0000269|PubMed:9572291}.
-!- MISCELLANEOUS: Administration of dexamethasone results in the
conversion of the proenzyme to the mature form in thymocytes.
-!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; D38104; BAA07285.1; -; mRNA.
EMBL; D45187; BAA08128.1; -; mRNA.
EMBL; BC062002; AAH62002.1; -; mRNA.
PIR; A34657; A34657.
PIR; S66465; S66465.
PIR; S66466; S66466.
RefSeq; NP_037070.1; NM_012938.1.
RefSeq; XP_006249810.1; XM_006249748.2. [P16228-1]
RefSeq; XP_006249811.1; XM_006249749.2. [P16228-1]
RefSeq; XP_017454166.1; XM_017598677.1. [P16228-1]
UniGene; Rn.92738; -.
ProteinModelPortal; P16228; -.
SMR; P16228; -.
STRING; 10116.ENSRNOP00000048353; -.
MEROPS; A01.010; -.
PaxDb; P16228; -.
PRIDE; P16228; -.
Ensembl; ENSRNOT00000009241; ENSRNOP00000009242; ENSRNOG00000006963. [P16228-2]
Ensembl; ENSRNOT00000048391; ENSRNOP00000048353; ENSRNOG00000006963. [P16228-1]
GeneID; 25424; -.
KEGG; rno:25424; -.
UCSC; RGD:2446; rat. [P16228-1]
CTD; 1510; -.
RGD; 2446; Ctse.
eggNOG; KOG1339; Eukaryota.
eggNOG; ENOG410XNV7; LUCA.
GeneTree; ENSGT00760000118929; -.
HOGENOM; HOG000197681; -.
HOVERGEN; HBG000482; -.
InParanoid; P16228; -.
KO; K01382; -.
OMA; KEPGQTF; -.
OrthoDB; EOG091G0JP7; -.
PhylomeDB; P16228; -.
TreeFam; TF314990; -.
BRENDA; 3.4.23.34; 5301.
PRO; PR:P16228; -.
Proteomes; UP000002494; Chromosome 13.
Bgee; ENSRNOG00000006963; -.
Genevisible; P16228; RN.
GO; GO:0005768; C:endosome; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0004190; F:aspartic-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IDA:UniProtKB.
GO; GO:0016540; P:protein autoprocessing; IMP:RGD.
GO; GO:0030163; P:protein catabolic process; IBA:GO_Central.
Gene3D; 2.40.70.10; -; 2.
InterPro; IPR001461; Aspartic_peptidase_A1.
InterPro; IPR001969; Aspartic_peptidase_AS.
InterPro; IPR012848; Aspartic_peptidase_N.
InterPro; IPR033145; Cathepsin_E.
InterPro; IPR033121; PEPTIDASE_A1.
InterPro; IPR021109; Peptidase_aspartic_dom_sf.
PANTHER; PTHR13683; PTHR13683; 1.
PANTHER; PTHR13683:SF81; PTHR13683:SF81; 1.
Pfam; PF07966; A1_Propeptide; 1.
Pfam; PF00026; Asp; 1.
PRINTS; PR00792; PEPSIN.
SUPFAM; SSF50630; SSF50630; 1.
PROSITE; PS00141; ASP_PROTEASE; 2.
PROSITE; PS51767; PEPTIDASE_A1; 1.
1: Evidence at protein level;
Alternative splicing; Aspartyl protease; Autocatalytic cleavage;
Complete proteome; Direct protein sequencing; Disulfide bond;
Endosome; Glycoprotein; Hydrolase; Polymorphism; Protease;
Reference proteome; Signal; Zymogen.
SIGNAL 1 21 {ECO:0000250}.
PROPEP 22 58 Activation peptide.
{ECO:0000269|PubMed:2105725}.
/FTId=PRO_0000025980.
CHAIN 59 398 Cathepsin E.
/FTId=PRO_0000025981.
DOMAIN 80 394 Peptidase A1. {ECO:0000255|PROSITE-
ProRule:PRU01103}.
ACT_SITE 98 98 {ECO:0000255|PROSITE-ProRule:PRU10094}.
ACT_SITE 283 283 {ECO:0000255|PROSITE-ProRule:PRU10094}.
CARBOHYD 92 92 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
DISULFID 62 62 Interchain. {ECO:0000305}.
DISULFID 111 116 {ECO:0000250}.
DISULFID 274 278 {ECO:0000250}.
VAR_SEQ 312 344 Missing (in isoform 2).
{ECO:0000303|PubMed:7574663}.
/FTId=VSP_005224.
VARIANT 114 114 P -> S. {ECO:0000269|PubMed:7574663}.
CONFLICT 55 55 M -> V (in Ref. 2; AAH62002).
{ECO:0000305}.
CONFLICT 79 79 E -> N (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 83 84 TV -> SR (in Ref. 3; AA sequence).
{ECO:0000305}.
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


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