Full text data of CTSE
CTSE
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Cathepsin E; 3.4.23.34; Cathepsin E form I; Cathepsin E form II; Flags: Precursor
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Cathepsin E; 3.4.23.34; Cathepsin E form I; Cathepsin E form II; Flags: Precursor
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P14091
ID CATE_HUMAN Reviewed; 401 AA.
AC P14091; Q5TZ01; Q5TZ02; Q9NY58; Q9UCE3; Q9UCE4;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
read moreDT 29-MAR-2004, sequence version 2.
DT 22-JAN-2014, entry version 155.
DE RecName: Full=Cathepsin E;
DE EC=3.4.23.34;
DE Contains:
DE RecName: Full=Cathepsin E form I;
DE Contains:
DE RecName: Full=Cathepsin E form II;
DE Flags: Precursor;
GN Name=CTSE;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Gastric mucosa;
RX PubMed=2674141;
RA Azuma T., Pals G., Mohandas T.K., Couvreur J.M., Taggart R.T.;
RT "Human gastric cathepsin E. Predicted sequence, localization to
RT chromosome 1, and sequence homology with other aspartic proteinases.";
RL J. Biol. Chem. 264:16748-16753(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=1370478;
RA Azuma T., Liu W.G., Vander Laan D.J., Bowcock A.M., Taggart R.T.;
RT "Human gastric cathepsin E gene. Multiple transcripts result from
RT alternative polyadenylation of the primary transcripts of a single
RT gene locus at 1q31-q32.";
RL J. Biol. Chem. 267:1609-1614(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), SUBCELLULAR LOCATION,
RP AND GLYCOSYLATION.
RC TISSUE=Intestine;
RX PubMed=7983070;
RA Finley E.M., Kornfeld S.;
RT "Subcellular localization and targeting of cathepsin E.";
RL J. Biol. Chem. 269:31259-31266(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Gastric adenocarcinoma;
RX PubMed=12531480; DOI=10.1016/S0167-4781(02)00595-X;
RA Tatnell P.J., Cook M., Kay J.;
RT "An alternatively spliced variant of cathepsin E in human gastric
RT adenocarcinoma cells.";
RL Biochim. Biophys. Acta 1625:203-206(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Stomach;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA 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.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA 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.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., 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.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 20-38 AND 54-76, BIOPHYSICOCHEMICAL PROPERTIES,
RP AUTOCATALYTIC CLEAVAGE, AND GLYCOSYLATION.
RC TISSUE=Erythrocyte;
RX PubMed=8346912; DOI=10.1006/abbi.1993.1361;
RA Takeda-Ezaki M., Yamamoto K.;
RT "Isolation and biochemical characterization of procathepsin E from
RT human erythrocyte membranes.";
RL Arch. Biochem. Biophys. 304:352-358(1993).
RN [10]
RP PROTEIN SEQUENCE OF 54-68; 77-95; 141-154; 280-290 AND 394-401, AND
RP GLYCOSYLATION.
RC TISSUE=Gastric mucosa;
RX PubMed=2334440; DOI=10.1016/0006-291X(90)92403-M;
RA Athauda S.B.P., Matsuzaki O., Kgeyama T., Takahashi K.;
RT "Structural evidence for two isozymic forms and the carbohydrate
RT attachment site of human gastric cathepsin E.";
RL Biochem. Biophys. Res. Commun. 168:878-885(1990).
RN [11]
RP CATALYTIC ACTIVITY, SUBUNIT, DISULFIDE BONDS, AND MUTAGENESIS OF
RP CYS-60.
RX PubMed=7789521; DOI=10.1016/0014-5793(95)00501-Y;
RA Fowler S.D., Kay J., Dunn B.M., Tatnell P.J.;
RT "Monomeric human cathepsin E.";
RL FEBS Lett. 366:72-74(1995).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=8765029; DOI=10.1002/eji.1830260826;
RA Sealy L., Mota F., Rayment N., Tatnell P.J., Kay J., Chain B.;
RT "Regulation of cathepsin E expression during human B cell
RT differentiation in vitro.";
RL Eur. J. Immunol. 26:1838-1843(1996).
RN [13]
RP TISSUE SPECIFICITY.
RX PubMed=11322887; DOI=10.1046/j.1432-1327.2001.02159.x;
RA Cook M., Caswell R.C., Richards R.J., Kay J., Tatnell P.J.;
RT "Regulation of human and mouse procathepsin E gene expression.";
RL Eur. J. Biochem. 268:2658-2668(2001).
CC -!- FUNCTION: May have a role in immune function. Probably involved in
CC the processing of antigenic peptides during MHC class II-mediated
CC antigen presentation. May play a role in activation-induced
CC lymphocyte depletion in the thymus, and in neuronal degeneration
CC and glial cell activation in the brain.
CC -!- CATALYTIC ACTIVITY: Similar to cathepsin D, but slightly broader
CC specificity.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.06 mM for hemoglobin;
CC KM=0.13 mM for Pro-Pro-Thr-Ile-Phe-Phe(4-NO2)-Arg-Leu;
CC KM=0.04 mM for Lys-Pro-Ile-Glu-Phe-Phe(4-NO2)-Arg-Leu;
CC -!- SUBUNIT: Homodimer; disulfide-linked.
CC -!- SUBCELLULAR LOCATION: Endosome. Note=The proenzyme is localized to
CC the endoplasmic reticulum and Golgi apparatus, while the mature
CC enzyme is localized to the endosome.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=3;
CC IsoId=P14091-3; Sequence=Displayed;
CC Name=1;
CC IsoId=P14091-1; Sequence=VSP_009729;
CC Name=2;
CC IsoId=P14091-2; Sequence=VSP_009729, VSP_009730, VSP_009731;
CC -!- TISSUE SPECIFICITY: Expressed abundantly in the stomach, the Clara
CC cells of the lung and activated B-lymphocytes, and at lower levels
CC in lymph nodes, skin and spleen. Not expressed in resting B-
CC lymphocytes.
CC -!- PTM: Glycosylated. The nature of the carbohydrate chain varies
CC between cell types. In fibroblasts, the proenzyme contains a high
CC mannose-type oligosaccharide, while the mature enzyme contains a
CC complex-type oligosaccharide. In erythrocyte membranes, both the
CC proenzyme and mature enzyme contain a complex-type
CC oligosaccharide.
CC -!- PTM: Two forms are produced by autocatalytic cleavage, form I
CC begins at Ile-54, form II begins at Thr-57.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
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DR EMBL; J05036; AAA52130.1; -; mRNA.
DR EMBL; M84424; AAA52300.1; -; Genomic_DNA.
DR EMBL; M84413; AAA52300.1; JOINED; Genomic_DNA.
DR EMBL; M84417; AAA52300.1; JOINED; Genomic_DNA.
DR EMBL; M84418; AAA52300.1; JOINED; Genomic_DNA.
DR EMBL; M84419; AAA52300.1; JOINED; Genomic_DNA.
DR EMBL; M84420; AAA52300.1; JOINED; Genomic_DNA.
DR EMBL; M84421; AAA52300.1; JOINED; Genomic_DNA.
DR EMBL; M84422; AAA52300.1; JOINED; Genomic_DNA.
DR EMBL; AJ250716; CAB82849.1; -; mRNA.
DR EMBL; AJ250717; CAB82850.1; -; mRNA.
DR EMBL; AK292057; BAF84746.1; -; mRNA.
DR EMBL; BX571818; CAH73264.1; -; Genomic_DNA.
DR EMBL; BX571818; CAH73265.1; -; Genomic_DNA.
DR EMBL; CH471067; EAW91592.1; -; Genomic_DNA.
DR EMBL; CH471067; EAW91593.1; -; Genomic_DNA.
DR EMBL; BC042537; AAH42537.1; -; mRNA.
DR PIR; A42038; A34401.
DR RefSeq; NP_001901.1; NM_001910.3.
DR RefSeq; NP_683865.1; NM_148964.2.
DR UniGene; Hs.644082; -.
DR PDB; 1LCG; Model; -; A=1-401.
DR PDB; 1TZS; X-ray; 2.35 A; A=54-401, P=19-53.
DR PDBsum; 1LCG; -.
DR PDBsum; 1TZS; -.
DR ProteinModelPortal; P14091; -.
DR SMR; P14091; 21-400.
DR IntAct; P14091; 2.
DR MINT; MINT-1388890; -.
DR STRING; 9606.ENSP00000350911; -.
DR BindingDB; P14091; -.
DR ChEMBL; CHEMBL3092; -.
DR GuidetoPHARMACOLOGY; 2346; -.
DR MEROPS; A01.010; -.
DR PhosphoSite; P14091; -.
DR DMDM; 46397366; -.
DR PaxDb; P14091; -.
DR PRIDE; P14091; -.
DR DNASU; 1510; -.
DR Ensembl; ENST00000358184; ENSP00000350911; ENSG00000196188.
DR Ensembl; ENST00000360218; ENSP00000353350; ENSG00000196188.
DR Ensembl; ENST00000581049; ENSP00000463969; ENSG00000264606.
DR Ensembl; ENST00000583663; ENSP00000463953; ENSG00000264606.
DR GeneID; 1510; -.
DR KEGG; hsa:1510; -.
DR CTD; 1510; -.
DR GeneCards; GC01P206319; -.
DR HGNC; HGNC:2530; CTSE.
DR HPA; HPA008021; -.
DR MIM; 116890; gene.
DR neXtProt; NX_P14091; -.
DR PharmGKB; PA27030; -.
DR eggNOG; NOG248684; -.
DR HOGENOM; HOG000197681; -.
DR HOVERGEN; HBG000482; -.
DR InParanoid; P14091; -.
DR KO; K01382; -.
DR Reactome; REACT_6900; Immune System.
DR SABIO-RK; P14091; -.
DR EvolutionaryTrace; P14091; -.
DR GeneWiki; Cathepsin_E; -.
DR GenomeRNAi; 1510; -.
DR NextBio; 6251; -.
DR PMAP-CutDB; P14091; -.
DR PRO; PR:P14091; -.
DR ArrayExpress; P14091; -.
DR Bgee; P14091; -.
DR CleanEx; HS_CTSE; -.
DR Genevestigator; P14091; -.
DR GO; GO:0005768; C:endosome; IDA: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; IDA:UniProtKB.
DR GO; GO:0007586; P:digestion; TAS:ProtInc.
DR GO; GO:0016540; P:protein autoprocessing; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR012848; Aspartic_peptidase_N.
DR InterPro; IPR021109; Peptidase_aspartic_dom.
DR PANTHER; PTHR13683; PTHR13683; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Aspartyl protease;
KW Autocatalytic cleavage; Complete proteome; Direct protein sequencing;
KW Disulfide bond; Endosome; Glycoprotein; Hydrolase; Polymorphism;
KW Protease; Reference proteome; Signal; Zymogen.
FT SIGNAL 1 19
FT PROPEP 20 53 Activation peptide.
FT /FTId=PRO_0000025974.
FT CHAIN 54 401 Cathepsin E form I.
FT /FTId=PRO_0000025975.
FT CHAIN 57 401 Cathepsin E form II.
FT /FTId=PRO_0000354668.
FT ACT_SITE 96 96 By similarity.
FT ACT_SITE 286 286 By similarity.
FT CARBOHYD 90 90 N-linked (GlcNAc...).
FT DISULFID 60 60 Interchain.
FT DISULFID 109 114 By similarity.
FT DISULFID 277 281 By similarity.
FT DISULFID 319 356 By similarity.
FT VAR_SEQ 155 159 Missing (in isoform 1 and isoform 2).
FT /FTId=VSP_009729.
FT VAR_SEQ 268 368 IQVGGTVMFCSEGCQAIVDTGTSLITGPSDKIKQLQNAIGA
FT APVDGEYAVECANLNVMPDVTFTINGVPYTLSPTAYTLLDF
FT VDGMQFCSSGFQGLDIHPP -> MLWSVPTLTSCRMSPSPL
FT TESPIPSAQLPTPYWTSWMECSSAAVAFKDLTSTLQLGPSG
FT SWGMSSFDSFTQSLTVGITVWDWPQQSPKEGPCVCACLSDR
FT P (in isoform 2).
FT /FTId=VSP_009730.
FT VAR_SEQ 369 401 Missing (in isoform 2).
FT /FTId=VSP_009731.
FT VARIANT 82 82 I -> V (in dbSNP:rs57621203).
FT /FTId=VAR_061731.
FT VARIANT 329 329 T -> I (in dbSNP:rs6503).
FT /FTId=VAR_014572.
FT MUTAGEN 60 60 C->A: Abolishes homodimerization.
FT STRAND 22 25
FT HELIX 71 73
FT STRAND 74 76
FT STRAND 79 84
FT TURN 85 88
FT STRAND 89 96
FT STRAND 102 106
FT HELIX 112 114
FT HELIX 122 124
FT STRAND 134 141
FT STRAND 143 154
FT STRAND 163 173
FT HELIX 179 183
FT STRAND 187 191
FT HELIX 195 197
FT HELIX 199 201
FT HELIX 205 211
FT STRAND 216 223
FT STRAND 235 238
FT HELIX 243 245
FT STRAND 251 254
FT TURN 258 261
FT STRAND 262 270
FT STRAND 273 276
FT STRAND 281 285
FT STRAND 290 294
FT HELIX 296 306
FT STRAND 312 317
FT HELIX 319 324
FT STRAND 328 332
FT STRAND 335 339
FT TURN 341 343
FT STRAND 344 346
FT STRAND 356 362
FT TURN 367 369
FT STRAND 373 375
FT HELIX 377 382
FT STRAND 383 388
FT TURN 389 392
FT STRAND 393 399
SQ SEQUENCE 401 AA; 43312 MW; 46A2BA35266032CB CRC64;
MKTLLLLLLV LLELGEAQGS LHRVPLRRHP SLKKKLRARS QLSEFWKSHN LDMIQFTESC
SMDQSAKEPL INYLDMEYFG TISIGSPPQN FTVIFDTGSS NLWVPSVYCT SPACKTHSRF
QPSQSSTYSQ PGQSFSIQYG TGSLSGIIGA DQVSAFATQV EGLTVVGQQF GESVTEPGQT
FVDAEFDGIL GLGYPSLAVG GVTPVFDNMM AQNLVDLPMF SVYMSSNPEG GAGSELIFGG
YDHSHFSGSL NWVPVTKQAY WQIALDNIQV GGTVMFCSEG CQAIVDTGTS LITGPSDKIK
QLQNAIGAAP VDGEYAVECA NLNVMPDVTF TINGVPYTLS PTAYTLLDFV DGMQFCSSGF
QGLDIHPPAG PLWILGDVFI RQFYSVFDRG NNRVGLAPAV P
//
ID CATE_HUMAN Reviewed; 401 AA.
AC P14091; Q5TZ01; Q5TZ02; Q9NY58; Q9UCE3; Q9UCE4;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
read moreDT 29-MAR-2004, sequence version 2.
DT 22-JAN-2014, entry version 155.
DE RecName: Full=Cathepsin E;
DE EC=3.4.23.34;
DE Contains:
DE RecName: Full=Cathepsin E form I;
DE Contains:
DE RecName: Full=Cathepsin E form II;
DE Flags: Precursor;
GN Name=CTSE;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Gastric mucosa;
RX PubMed=2674141;
RA Azuma T., Pals G., Mohandas T.K., Couvreur J.M., Taggart R.T.;
RT "Human gastric cathepsin E. Predicted sequence, localization to
RT chromosome 1, and sequence homology with other aspartic proteinases.";
RL J. Biol. Chem. 264:16748-16753(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=1370478;
RA Azuma T., Liu W.G., Vander Laan D.J., Bowcock A.M., Taggart R.T.;
RT "Human gastric cathepsin E gene. Multiple transcripts result from
RT alternative polyadenylation of the primary transcripts of a single
RT gene locus at 1q31-q32.";
RL J. Biol. Chem. 267:1609-1614(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), SUBCELLULAR LOCATION,
RP AND GLYCOSYLATION.
RC TISSUE=Intestine;
RX PubMed=7983070;
RA Finley E.M., Kornfeld S.;
RT "Subcellular localization and targeting of cathepsin E.";
RL J. Biol. Chem. 269:31259-31266(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Gastric adenocarcinoma;
RX PubMed=12531480; DOI=10.1016/S0167-4781(02)00595-X;
RA Tatnell P.J., Cook M., Kay J.;
RT "An alternatively spliced variant of cathepsin E in human gastric
RT adenocarcinoma cells.";
RL Biochim. Biophys. Acta 1625:203-206(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Stomach;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA 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.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA 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.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., 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.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 20-38 AND 54-76, BIOPHYSICOCHEMICAL PROPERTIES,
RP AUTOCATALYTIC CLEAVAGE, AND GLYCOSYLATION.
RC TISSUE=Erythrocyte;
RX PubMed=8346912; DOI=10.1006/abbi.1993.1361;
RA Takeda-Ezaki M., Yamamoto K.;
RT "Isolation and biochemical characterization of procathepsin E from
RT human erythrocyte membranes.";
RL Arch. Biochem. Biophys. 304:352-358(1993).
RN [10]
RP PROTEIN SEQUENCE OF 54-68; 77-95; 141-154; 280-290 AND 394-401, AND
RP GLYCOSYLATION.
RC TISSUE=Gastric mucosa;
RX PubMed=2334440; DOI=10.1016/0006-291X(90)92403-M;
RA Athauda S.B.P., Matsuzaki O., Kgeyama T., Takahashi K.;
RT "Structural evidence for two isozymic forms and the carbohydrate
RT attachment site of human gastric cathepsin E.";
RL Biochem. Biophys. Res. Commun. 168:878-885(1990).
RN [11]
RP CATALYTIC ACTIVITY, SUBUNIT, DISULFIDE BONDS, AND MUTAGENESIS OF
RP CYS-60.
RX PubMed=7789521; DOI=10.1016/0014-5793(95)00501-Y;
RA Fowler S.D., Kay J., Dunn B.M., Tatnell P.J.;
RT "Monomeric human cathepsin E.";
RL FEBS Lett. 366:72-74(1995).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=8765029; DOI=10.1002/eji.1830260826;
RA Sealy L., Mota F., Rayment N., Tatnell P.J., Kay J., Chain B.;
RT "Regulation of cathepsin E expression during human B cell
RT differentiation in vitro.";
RL Eur. J. Immunol. 26:1838-1843(1996).
RN [13]
RP TISSUE SPECIFICITY.
RX PubMed=11322887; DOI=10.1046/j.1432-1327.2001.02159.x;
RA Cook M., Caswell R.C., Richards R.J., Kay J., Tatnell P.J.;
RT "Regulation of human and mouse procathepsin E gene expression.";
RL Eur. J. Biochem. 268:2658-2668(2001).
CC -!- FUNCTION: May have a role in immune function. Probably involved in
CC the processing of antigenic peptides during MHC class II-mediated
CC antigen presentation. May play a role in activation-induced
CC lymphocyte depletion in the thymus, and in neuronal degeneration
CC and glial cell activation in the brain.
CC -!- CATALYTIC ACTIVITY: Similar to cathepsin D, but slightly broader
CC specificity.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.06 mM for hemoglobin;
CC KM=0.13 mM for Pro-Pro-Thr-Ile-Phe-Phe(4-NO2)-Arg-Leu;
CC KM=0.04 mM for Lys-Pro-Ile-Glu-Phe-Phe(4-NO2)-Arg-Leu;
CC -!- SUBUNIT: Homodimer; disulfide-linked.
CC -!- SUBCELLULAR LOCATION: Endosome. Note=The proenzyme is localized to
CC the endoplasmic reticulum and Golgi apparatus, while the mature
CC enzyme is localized to the endosome.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=3;
CC IsoId=P14091-3; Sequence=Displayed;
CC Name=1;
CC IsoId=P14091-1; Sequence=VSP_009729;
CC Name=2;
CC IsoId=P14091-2; Sequence=VSP_009729, VSP_009730, VSP_009731;
CC -!- TISSUE SPECIFICITY: Expressed abundantly in the stomach, the Clara
CC cells of the lung and activated B-lymphocytes, and at lower levels
CC in lymph nodes, skin and spleen. Not expressed in resting B-
CC lymphocytes.
CC -!- PTM: Glycosylated. The nature of the carbohydrate chain varies
CC between cell types. In fibroblasts, the proenzyme contains a high
CC mannose-type oligosaccharide, while the mature enzyme contains a
CC complex-type oligosaccharide. In erythrocyte membranes, both the
CC proenzyme and mature enzyme contain a complex-type
CC oligosaccharide.
CC -!- PTM: Two forms are produced by autocatalytic cleavage, form I
CC begins at Ile-54, form II begins at Thr-57.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC -----------------------------------------------------------------------
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CC Distributed under the Creative Commons Attribution-NoDerivs License
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DR EMBL; J05036; AAA52130.1; -; mRNA.
DR EMBL; M84424; AAA52300.1; -; Genomic_DNA.
DR EMBL; M84413; AAA52300.1; JOINED; Genomic_DNA.
DR EMBL; M84417; AAA52300.1; JOINED; Genomic_DNA.
DR EMBL; M84418; AAA52300.1; JOINED; Genomic_DNA.
DR EMBL; M84419; AAA52300.1; JOINED; Genomic_DNA.
DR EMBL; M84420; AAA52300.1; JOINED; Genomic_DNA.
DR EMBL; M84421; AAA52300.1; JOINED; Genomic_DNA.
DR EMBL; M84422; AAA52300.1; JOINED; Genomic_DNA.
DR EMBL; AJ250716; CAB82849.1; -; mRNA.
DR EMBL; AJ250717; CAB82850.1; -; mRNA.
DR EMBL; AK292057; BAF84746.1; -; mRNA.
DR EMBL; BX571818; CAH73264.1; -; Genomic_DNA.
DR EMBL; BX571818; CAH73265.1; -; Genomic_DNA.
DR EMBL; CH471067; EAW91592.1; -; Genomic_DNA.
DR EMBL; CH471067; EAW91593.1; -; Genomic_DNA.
DR EMBL; BC042537; AAH42537.1; -; mRNA.
DR PIR; A42038; A34401.
DR RefSeq; NP_001901.1; NM_001910.3.
DR RefSeq; NP_683865.1; NM_148964.2.
DR UniGene; Hs.644082; -.
DR PDB; 1LCG; Model; -; A=1-401.
DR PDB; 1TZS; X-ray; 2.35 A; A=54-401, P=19-53.
DR PDBsum; 1LCG; -.
DR PDBsum; 1TZS; -.
DR ProteinModelPortal; P14091; -.
DR SMR; P14091; 21-400.
DR IntAct; P14091; 2.
DR MINT; MINT-1388890; -.
DR STRING; 9606.ENSP00000350911; -.
DR BindingDB; P14091; -.
DR ChEMBL; CHEMBL3092; -.
DR GuidetoPHARMACOLOGY; 2346; -.
DR MEROPS; A01.010; -.
DR PhosphoSite; P14091; -.
DR DMDM; 46397366; -.
DR PaxDb; P14091; -.
DR PRIDE; P14091; -.
DR DNASU; 1510; -.
DR Ensembl; ENST00000358184; ENSP00000350911; ENSG00000196188.
DR Ensembl; ENST00000360218; ENSP00000353350; ENSG00000196188.
DR Ensembl; ENST00000581049; ENSP00000463969; ENSG00000264606.
DR Ensembl; ENST00000583663; ENSP00000463953; ENSG00000264606.
DR GeneID; 1510; -.
DR KEGG; hsa:1510; -.
DR CTD; 1510; -.
DR GeneCards; GC01P206319; -.
DR HGNC; HGNC:2530; CTSE.
DR HPA; HPA008021; -.
DR MIM; 116890; gene.
DR neXtProt; NX_P14091; -.
DR PharmGKB; PA27030; -.
DR eggNOG; NOG248684; -.
DR HOGENOM; HOG000197681; -.
DR HOVERGEN; HBG000482; -.
DR InParanoid; P14091; -.
DR KO; K01382; -.
DR Reactome; REACT_6900; Immune System.
DR SABIO-RK; P14091; -.
DR EvolutionaryTrace; P14091; -.
DR GeneWiki; Cathepsin_E; -.
DR GenomeRNAi; 1510; -.
DR NextBio; 6251; -.
DR PMAP-CutDB; P14091; -.
DR PRO; PR:P14091; -.
DR ArrayExpress; P14091; -.
DR Bgee; P14091; -.
DR CleanEx; HS_CTSE; -.
DR Genevestigator; P14091; -.
DR GO; GO:0005768; C:endosome; IDA: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; IDA:UniProtKB.
DR GO; GO:0007586; P:digestion; TAS:ProtInc.
DR GO; GO:0016540; P:protein autoprocessing; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR012848; Aspartic_peptidase_N.
DR InterPro; IPR021109; Peptidase_aspartic_dom.
DR PANTHER; PTHR13683; PTHR13683; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Aspartyl protease;
KW Autocatalytic cleavage; Complete proteome; Direct protein sequencing;
KW Disulfide bond; Endosome; Glycoprotein; Hydrolase; Polymorphism;
KW Protease; Reference proteome; Signal; Zymogen.
FT SIGNAL 1 19
FT PROPEP 20 53 Activation peptide.
FT /FTId=PRO_0000025974.
FT CHAIN 54 401 Cathepsin E form I.
FT /FTId=PRO_0000025975.
FT CHAIN 57 401 Cathepsin E form II.
FT /FTId=PRO_0000354668.
FT ACT_SITE 96 96 By similarity.
FT ACT_SITE 286 286 By similarity.
FT CARBOHYD 90 90 N-linked (GlcNAc...).
FT DISULFID 60 60 Interchain.
FT DISULFID 109 114 By similarity.
FT DISULFID 277 281 By similarity.
FT DISULFID 319 356 By similarity.
FT VAR_SEQ 155 159 Missing (in isoform 1 and isoform 2).
FT /FTId=VSP_009729.
FT VAR_SEQ 268 368 IQVGGTVMFCSEGCQAIVDTGTSLITGPSDKIKQLQNAIGA
FT APVDGEYAVECANLNVMPDVTFTINGVPYTLSPTAYTLLDF
FT VDGMQFCSSGFQGLDIHPP -> MLWSVPTLTSCRMSPSPL
FT TESPIPSAQLPTPYWTSWMECSSAAVAFKDLTSTLQLGPSG
FT SWGMSSFDSFTQSLTVGITVWDWPQQSPKEGPCVCACLSDR
FT P (in isoform 2).
FT /FTId=VSP_009730.
FT VAR_SEQ 369 401 Missing (in isoform 2).
FT /FTId=VSP_009731.
FT VARIANT 82 82 I -> V (in dbSNP:rs57621203).
FT /FTId=VAR_061731.
FT VARIANT 329 329 T -> I (in dbSNP:rs6503).
FT /FTId=VAR_014572.
FT MUTAGEN 60 60 C->A: Abolishes homodimerization.
FT STRAND 22 25
FT HELIX 71 73
FT STRAND 74 76
FT STRAND 79 84
FT TURN 85 88
FT STRAND 89 96
FT STRAND 102 106
FT HELIX 112 114
FT HELIX 122 124
FT STRAND 134 141
FT STRAND 143 154
FT STRAND 163 173
FT HELIX 179 183
FT STRAND 187 191
FT HELIX 195 197
FT HELIX 199 201
FT HELIX 205 211
FT STRAND 216 223
FT STRAND 235 238
FT HELIX 243 245
FT STRAND 251 254
FT TURN 258 261
FT STRAND 262 270
FT STRAND 273 276
FT STRAND 281 285
FT STRAND 290 294
FT HELIX 296 306
FT STRAND 312 317
FT HELIX 319 324
FT STRAND 328 332
FT STRAND 335 339
FT TURN 341 343
FT STRAND 344 346
FT STRAND 356 362
FT TURN 367 369
FT STRAND 373 375
FT HELIX 377 382
FT STRAND 383 388
FT TURN 389 392
FT STRAND 393 399
SQ SEQUENCE 401 AA; 43312 MW; 46A2BA35266032CB CRC64;
MKTLLLLLLV LLELGEAQGS LHRVPLRRHP SLKKKLRARS QLSEFWKSHN LDMIQFTESC
SMDQSAKEPL INYLDMEYFG TISIGSPPQN FTVIFDTGSS NLWVPSVYCT SPACKTHSRF
QPSQSSTYSQ PGQSFSIQYG TGSLSGIIGA DQVSAFATQV EGLTVVGQQF GESVTEPGQT
FVDAEFDGIL GLGYPSLAVG GVTPVFDNMM AQNLVDLPMF SVYMSSNPEG GAGSELIFGG
YDHSHFSGSL NWVPVTKQAY WQIALDNIQV GGTVMFCSEG CQAIVDTGTS LITGPSDKIK
QLQNAIGAAP VDGEYAVECA NLNVMPDVTF TINGVPYTLS PTAYTLLDFV DGMQFCSSGF
QGLDIHPPAG PLWILGDVFI RQFYSVFDRG NNRVGLAPAV P
//
MIM
116890
*RECORD*
*FIELD* NO
116890
*FIELD* TI
*116890 CATHEPSIN E; CTSE
;;CATE
*FIELD* TX
DESCRIPTION
Cathepsin E, an endolysosomal aspartic proteinase predominantly
read moreexpressed in cells of the immune system, has an important role in immune
responses (Yanagawa et al., 2007).
CLONING
Taggart et al. (1989) used sets of complementary oligonucleotide probes
specific for the highly conserved active site region of aspartic
proteinases to isolate cDNA clones encoding novel enzymes of this class.
They identified 6 classes of cDNA clones in a gastric adenocarcinoma
cDNA library using a set of 18-mer probes. One of the cDNAs, designated
AGS402, was shown by DNA analysis to correspond to the predicted coding
sequence of cathepsin E. Couvreur et al. (1989, 1990) also isolated a
full-length CTSE cDNA clone from a gastric adenocarcinoma cDNA library.
Azuma et al. (1989, 1989) reported the amino acid sequence of CTSE
predicted on the basis of the cDNA sequence and compared the sequence
with that of other aspartic proteinases. Azuma et al. (1992)
demonstrated that multiple transcripts result from alternative
polyadenylation of the primary transcripts of the single CTSE gene.
GENE STRUCTURE
Azuma et al. (1992) determined that the CTSE gene contains 9 exons and
spans 17.5 kb. The size and placement of the exons are highly conserved
relative to other aspartic proteinases.
MAPPING
By somatic cell hybrid analysis, Taggart et al. (1989) mapped the CTSE
gene to chromosome 1. Azuma et al. (1989, 1989) also assigned the CTSE
gene to chromosome 1.
Couvreur et al. (1989, 1990) mapped the CTSE gene to chromosome
1q23-qter by analysis of human/rodent hybrid cell lines containing
different X;1 translocations. CTSE was further localized to chromosome
1q31 by in situ hybridization.
ANIMAL MODEL
Yanagawa et al. (2007) found that cathepsin E deficiency in mice
resulted in a lysosome storage disorder in macrophages that was
characterized by accumulation of major lysosomal membrane
sialoglycoproteins, including Lamp1 (153330), Lamp2 (309060), and Limp2
(SCARB2; 602257), and elevated lysosomal pH. Trafficking of soluble
lysosomal proteins to lysosomes was also partially impaired in Cate -/-
macrophages. Treatment of wildtype macrophages with a cathepsin E
inhibitor also led to accumulation of these lysosomal proteins and
elevated pH. Since vacuolar-type H(+) ATPase (see 603097) activity was
not altered in Cate -/- macrophages, Yanagawa et al. (2007) hypothesized
that the elevated lysosomal pH in Cate -/- macrophages was likely due to
the accumulation of the highly acidic lysosomal sialoglycoproteins.
*FIELD* RF
1. Azuma, T.; Liu, W. G.; Vander Laan, D. J.; Bowcock, A. M.; Taggart,
R. T.: Human gastric cathepsin E gene: multiple transcripts result
from alternative polyadenylation of the primary transcripts of a single
gene locus at 1q31-q32. J. Biol. Chem. 267: 1609-1614, 1992.
2. Azuma, T.; Pals, G.; Mohandas, T. K.; Couvreur, J. M.; Taggart,
R. T.: Cathepsin E: molecular cloning and characterization using
aspartyl proteinase active site probes. (Abstract) Am. J. Hum. Genet. 45
(suppl.): A171 only, 1989.
3. Azuma, T.; Pals, G.; Mohandas, T. K.; Couvreur, J. M.; Taggart,
R. T.: Human gastric cathepsin E: predicted sequence, localization
to chromosome 1, and sequence homology with other aspartic proteinases. J.
Biol. Chem. 264: 16748-16753, 1989.
4. Couvreur, J. M.; Azuma, T.; Miller, D. A.; Rocchi, M.; Mohandas,
T. K.; Boudi, F. A.; Taggart, R. T.: Assignment of cathepsin E (CTSE)
to human chromosome region 1q31 by in situ hybridization and analysis
of somatic cell hybrids. Cytogenet. Cell Genet. 53: 137-139, 1990.
5. Couvreur, J. M.; Johnson, M. P.; Azuma, T.; Boudi, F. A.; Rocchi,
M.; Mohandas, T. K.; Miller, D. A.; Taggart, R. T.: Cathepsin E:
localization of a single gene locus to 1q31 by restriction analysis
of X;1 translocation somatic cell hybrids, and in situ hybridization.
(Abstract) Am. J. Hum. Genet. 45 (suppl.): A135 only, 1989.
6. Taggart, R. T.; Azuma, T.; Couvreur, J. M.; Mohandas, T. K.: Isolation
and mapping genes identified with probes specific for the conserved
active site of aspartic proteinases. (Abstract) Cytogenet. Cell Genet. 51:
1088 only, 1989.
7. Yanagawa, M.; Tsukuba, T.; Nishioku, T.; Okamoto, Y.; Okamoto,
K.; Takii, R.; Terada, Y.; Nakayama, K. I.; Kadowaki, T.; Yamamoto,
K.: Cathepsin E deficiency induces a novel form of lysosomal storage
disorder showing the accumulation of lysosomal membrane sialoglycoproteins
and the elevation of lysosomal pH in macrophages. J. Biol. Chem. 282:
1851-1862, 2007.
*FIELD* CN
Patricia A. Hartz - updated: 9/25/2007
*FIELD* CD
Victor A. McKusick: 6/2/1989
*FIELD* ED
mgross: 10/03/2007
mgross: 10/3/2007
terry: 9/25/2007
carol: 1/13/1993
supermim: 3/16/1992
supermim: 9/28/1990
supermim: 3/20/1990
carol: 12/1/1989
carol: 11/10/1989
*RECORD*
*FIELD* NO
116890
*FIELD* TI
*116890 CATHEPSIN E; CTSE
;;CATE
*FIELD* TX
DESCRIPTION
Cathepsin E, an endolysosomal aspartic proteinase predominantly
read moreexpressed in cells of the immune system, has an important role in immune
responses (Yanagawa et al., 2007).
CLONING
Taggart et al. (1989) used sets of complementary oligonucleotide probes
specific for the highly conserved active site region of aspartic
proteinases to isolate cDNA clones encoding novel enzymes of this class.
They identified 6 classes of cDNA clones in a gastric adenocarcinoma
cDNA library using a set of 18-mer probes. One of the cDNAs, designated
AGS402, was shown by DNA analysis to correspond to the predicted coding
sequence of cathepsin E. Couvreur et al. (1989, 1990) also isolated a
full-length CTSE cDNA clone from a gastric adenocarcinoma cDNA library.
Azuma et al. (1989, 1989) reported the amino acid sequence of CTSE
predicted on the basis of the cDNA sequence and compared the sequence
with that of other aspartic proteinases. Azuma et al. (1992)
demonstrated that multiple transcripts result from alternative
polyadenylation of the primary transcripts of the single CTSE gene.
GENE STRUCTURE
Azuma et al. (1992) determined that the CTSE gene contains 9 exons and
spans 17.5 kb. The size and placement of the exons are highly conserved
relative to other aspartic proteinases.
MAPPING
By somatic cell hybrid analysis, Taggart et al. (1989) mapped the CTSE
gene to chromosome 1. Azuma et al. (1989, 1989) also assigned the CTSE
gene to chromosome 1.
Couvreur et al. (1989, 1990) mapped the CTSE gene to chromosome
1q23-qter by analysis of human/rodent hybrid cell lines containing
different X;1 translocations. CTSE was further localized to chromosome
1q31 by in situ hybridization.
ANIMAL MODEL
Yanagawa et al. (2007) found that cathepsin E deficiency in mice
resulted in a lysosome storage disorder in macrophages that was
characterized by accumulation of major lysosomal membrane
sialoglycoproteins, including Lamp1 (153330), Lamp2 (309060), and Limp2
(SCARB2; 602257), and elevated lysosomal pH. Trafficking of soluble
lysosomal proteins to lysosomes was also partially impaired in Cate -/-
macrophages. Treatment of wildtype macrophages with a cathepsin E
inhibitor also led to accumulation of these lysosomal proteins and
elevated pH. Since vacuolar-type H(+) ATPase (see 603097) activity was
not altered in Cate -/- macrophages, Yanagawa et al. (2007) hypothesized
that the elevated lysosomal pH in Cate -/- macrophages was likely due to
the accumulation of the highly acidic lysosomal sialoglycoproteins.
*FIELD* RF
1. Azuma, T.; Liu, W. G.; Vander Laan, D. J.; Bowcock, A. M.; Taggart,
R. T.: Human gastric cathepsin E gene: multiple transcripts result
from alternative polyadenylation of the primary transcripts of a single
gene locus at 1q31-q32. J. Biol. Chem. 267: 1609-1614, 1992.
2. Azuma, T.; Pals, G.; Mohandas, T. K.; Couvreur, J. M.; Taggart,
R. T.: Cathepsin E: molecular cloning and characterization using
aspartyl proteinase active site probes. (Abstract) Am. J. Hum. Genet. 45
(suppl.): A171 only, 1989.
3. Azuma, T.; Pals, G.; Mohandas, T. K.; Couvreur, J. M.; Taggart,
R. T.: Human gastric cathepsin E: predicted sequence, localization
to chromosome 1, and sequence homology with other aspartic proteinases. J.
Biol. Chem. 264: 16748-16753, 1989.
4. Couvreur, J. M.; Azuma, T.; Miller, D. A.; Rocchi, M.; Mohandas,
T. K.; Boudi, F. A.; Taggart, R. T.: Assignment of cathepsin E (CTSE)
to human chromosome region 1q31 by in situ hybridization and analysis
of somatic cell hybrids. Cytogenet. Cell Genet. 53: 137-139, 1990.
5. Couvreur, J. M.; Johnson, M. P.; Azuma, T.; Boudi, F. A.; Rocchi,
M.; Mohandas, T. K.; Miller, D. A.; Taggart, R. T.: Cathepsin E:
localization of a single gene locus to 1q31 by restriction analysis
of X;1 translocation somatic cell hybrids, and in situ hybridization.
(Abstract) Am. J. Hum. Genet. 45 (suppl.): A135 only, 1989.
6. Taggart, R. T.; Azuma, T.; Couvreur, J. M.; Mohandas, T. K.: Isolation
and mapping genes identified with probes specific for the conserved
active site of aspartic proteinases. (Abstract) Cytogenet. Cell Genet. 51:
1088 only, 1989.
7. Yanagawa, M.; Tsukuba, T.; Nishioku, T.; Okamoto, Y.; Okamoto,
K.; Takii, R.; Terada, Y.; Nakayama, K. I.; Kadowaki, T.; Yamamoto,
K.: Cathepsin E deficiency induces a novel form of lysosomal storage
disorder showing the accumulation of lysosomal membrane sialoglycoproteins
and the elevation of lysosomal pH in macrophages. J. Biol. Chem. 282:
1851-1862, 2007.
*FIELD* CN
Patricia A. Hartz - updated: 9/25/2007
*FIELD* CD
Victor A. McKusick: 6/2/1989
*FIELD* ED
mgross: 10/03/2007
mgross: 10/3/2007
terry: 9/25/2007
carol: 1/13/1993
supermim: 3/16/1992
supermim: 9/28/1990
supermim: 3/20/1990
carol: 12/1/1989
carol: 11/10/1989