CATEA_XENLA
ID CATEA_XENLA Reviewed; 397 AA.
AC Q805F3;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Cathepsin E-A;
DE EC=3.4.23.34;
DE Flags: Precursor;
GN Name=ctse-a; Synonyms=ce1;
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:BAC57453.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-25 AND 53-59, CATALYTIC
RP ACTIVITY, SUBUNIT, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP GLYCOSYLATION.
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:0000269|PubMed:14561724};
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:14561724}.
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 larval foregut and
CC the anterior and posterior adult stomach.
CC {ECO:0000269|PubMed:14561724}.
CC -!- DEVELOPMENTAL STAGE: Expression levels are high in surface mucous cells
CC and manicotto gland cells of the foregut epithelium of pro-metamorphic
CC tadpoles. During metamorphosis, expression levels decrease markedly in
CC larval epithelial cells but are high in proliferating adult epithelial
CC primordia. In the adult stomach, expression was strongest in
CC oxynticopeptic cells, but was also detected at a lower level in surface
CC mucose cells. {ECO:0000269|PubMed:14561724}.
CC -!- PTM: Glycosylated. Contains high mannose-type oligosaccharide.
CC {ECO:0000269|PubMed:14561724}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; AB080684; BAC57453.1; -; mRNA.
DR RefSeq; NP_001079043.1; NM_001085574.1.
DR AlphaFoldDB; Q805F3; -.
DR SMR; Q805F3; -.
DR MEROPS; A01.010; -.
DR GeneID; 373572; -.
DR KEGG; xla:373572; -.
DR CTD; 373572; -.
DR Xenbase; XB-GENE-947868; ctse.L.
DR OMA; GVECANL; -.
DR OrthoDB; 1619495at2759; -.
DR Proteomes; UP000186698; Chromosome 2L.
DR Bgee; 373572; Expressed in stomach and 14 other tissues.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IDA: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; IPR018222; Nuclear_transport_factor_2_euk.
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 Aspartyl protease; Direct protein sequencing; Disulfide bond; Endosome;
KW Glycoprotein; Hydrolase; Protease; Reference proteome; Signal; Zymogen.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:14561724"
FT PROPEP 17..52
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:14561724"
FT /id="PRO_0000025984"
FT CHAIN 53..397
FT /note="Cathepsin E-A"
FT /id="PRO_0000025985"
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; 42907 MW; 3DA99B6866E84611 CRC64;
MRQILVLLLF ATLVYGLIRV PLKRQKSIRK TLKEKGKLSH IWTQQGIDMV QYTDSCSNDQ
APSEPLINYM DVEYFGEISV GTPPQNFTVI FDTGSSNLWV PSVYCISQAC AQHDRFQPQL
SSTYESNGNN FSLQYGTGSL SGVIGIDAVT VEGILVQNQQ FGESVSEPGS TFVDAEFDGI
LGLGYPSIAV GDCTPVFDNM IAQNLVELPM FSVYMSRNPN SAVGGELVFG GFDASRFSGQ
LNWVPVTNQG YWQIQLDNVQ INGEVLFCSG GCQAIVDTGT SLITGPSSDI VQLQNIIGAS
AANGDYEVDC SVLNEMPTVT FTINGIGYQM TPQQYTLQDG GGVCSSGFQG LDIPPPAGPL
WILGDVFIGQ YYSVFDRGNN RVGLAPVVPY PPLKNGV
