CATEB_XENLA
ID CATEB_XENLA Reviewed; 397 AA.
AC Q805F2;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Cathepsin E-B;
DE EC=3.4.23.34;
DE Flags: Precursor;
GN Name=ctse-b; Synonyms=ce2;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000312|EMBL:BAC57454.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=14561724; DOI=10.1093/jb/mvg156;
RA Ikuzawa M., Yasumasu S., Inokuchi T., Kobayashi K., Nomura K., Iuchi I.;
RT "Differential expression of two cathepsin Es during metamorphosis-
RT associated remodeling of the larval to adult type epithelium in Xenopus
RT stomach.";
RL J. Biochem. 134:385-394(2003).
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 (By similarity). {ECO:0000250|UniProtKB:P14091}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Similar to cathepsin D, but slightly broader specificity.;
CC EC=3.4.23.34; Evidence={ECO:0000250|UniProtKB:Q805F3};
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250|UniProtKB:Q805F3}.
CC -!- SUBCELLULAR LOCATION: Endosome {ECO:0000250}. Note=The proenzyme is
CC localized to the endoplasmic reticulum and Golgi apparatus, while the
CC mature enzyme is localized to the endosome. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in the anterior and
CC posterior adult stomach and at much lower levels in the larval foregut.
CC {ECO:0000269|PubMed:14561724}.
CC -!- DEVELOPMENTAL STAGE: Expression levels are low in surface mucous cells
CC and manicotto gland cells of the foregut epithelium of pro-metamorphic
CC tadpoles. During metamorphosis, expression levels rise markedly in
CC proliferating adult epithelial primordia. In the adult stomach,
CC expression was strongest in oxynticopeptic cells, but was also detected
CC at a lower level in surface mucose cells.
CC {ECO:0000269|PubMed:14561724}.
CC -!- PTM: Glycosylated. Contains high mannose-type oligosaccharide (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; AB080685; BAC57454.1; -; mRNA.
DR RefSeq; NP_001079044.1; NM_001085575.1.
DR AlphaFoldDB; Q805F2; -.
DR SMR; Q805F2; -.
DR MEROPS; A01.010; -.
DR GeneID; 373573; -.
DR KEGG; xla:373573; -.
DR CTD; 373573; -.
DR Xenbase; XB-GENE-6253064; ctse.S.
DR OMA; CERAVVW; -.
DR OrthoDB; 1619495at2759; -.
DR Proteomes; UP000186698; Chromosome 2S.
DR Bgee; 373573; Expressed in stomach and 6 other tissues.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; ISS:UniProtKB.
DR GO; GO:0016540; P:protein autoprocessing; IEA:InterPro.
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 2: Evidence at transcript level;
KW Aspartyl protease; Disulfide bond; Endosome; Glycoprotein; Hydrolase;
KW Protease; Reference proteome; Signal; Zymogen.
FT SIGNAL 1..16
FT /evidence="ECO:0000250|UniProtKB:Q805F3"
FT PROPEP 17..49
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:Q805F3"
FT /id="PRO_0000025986"
FT CHAIN 50..397
FT /note="Cathepsin E-B"
FT /id="PRO_0000025987"
FT DOMAIN 74..385
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 92
FT /evidence="ECO:0000250|UniProtKB:P00790,
FT ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 277
FT /evidence="ECO:0000250|UniProtKB:P00790,
FT ECO:0000255|PROSITE-ProRule:PRU10094"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 105..110
FT /evidence="ECO:0000250|UniProtKB:P00790"
FT DISULFID 268..272
FT /evidence="ECO:0000250|UniProtKB:P00790"
FT DISULFID 310..344
FT /evidence="ECO:0000250|UniProtKB:P00790"
SQ SEQUENCE 397 AA; 43002 MW; BF5CE987689046CC CRC64;
MRQILVLLLF VTLVYGLIRV PLKRQKSIRK TPKEKGKLSH VWTQQGIDMV QYTDSCNNDQ
APSEPLINYM DVQYFGEISI GTPPQNFTVI FDTGSSNLWV PSVYCISPAC AQHNRFQPQL
SSTYESNGNN FSLQYGTGSL SGVIGIDSVT VEGILVQNQQ FGESVSEPGS TFVDASFDGI
LGLGYPSIAV GGCTPVFDNM IAQNLVELPM FSVYMSRDPN SPVGGELVFG GFDASRFSGQ
LNWVPVTNQG YWQIQLDNIQ INGEVVFCSG GCQAIVDTGT SMITGPSSDI VQLQSIIGAS
AANGDYEVDC TVLNKMPTMT FTINGIGYQM TPQQYTLQDD DGVCSSGFQG LDISPPAGPL
WILGDVFIGQ YYSVFDRGNN RVGLAPVVPY PPLMNGV
