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P14091 (CATE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 158. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cathepsin E

EC=3.4.23.34

Cleaved into the following 2 chains:

  1. Cathepsin E form I
  2. Cathepsin E form II
Gene names
Name:CTSE
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length401 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.12

Catalytic activity

Similar to cathepsin D, but slightly broader specificity. Ref.11 Ref.12

Subunit structure

Homodimer; disulfide-linked. Ref.11

Subcellular location

Endosome. Note: The proenzyme is localized to the endoplasmic reticulum and Golgi apparatus, while the mature enzyme is localized to the endosome. Ref.3

Tissue specificity

Expressed abundantly in the stomach, the Clara cells of the lung and activated B-lymphocytes, and at lower levels in lymph nodes, skin and spleen. Not expressed in resting B-lymphocytes. Ref.2 Ref.12 Ref.13

Post-translational modification

Glycosylated. The nature of the carbohydrate chain varies between cell types. In fibroblasts, the proenzyme contains a high mannose-type oligosaccharide, while the mature enzyme contains a complex-type oligosaccharide. In erythrocyte membranes, both the proenzyme and mature enzyme contain a complex-type oligosaccharide. Ref.3 Ref.9 Ref.10

Two forms are produced by autocatalytic cleavage, form I begins at Ile-54, form II begins at Thr-57.

Sequence similarities

Belongs to the peptidase A1 family.

Biophysicochemical properties

Kinetic parameters:

KM=0.06 mM for hemoglobin Ref.9

KM=0.13 mM for Pro-Pro-Thr-Ile-Phe-Phe(4-NO2)-Arg-Leu

KM=0.04 mM for Lys-Pro-Ile-Glu-Phe-Phe(4-NO2)-Arg-Leu

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 3 (identifier: P14091-3)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 1 (identifier: P14091-1)

The sequence of this isoform differs from the canonical sequence as follows:
     155-159: Missing.
Isoform 2 (identifier: P14091-2)

The sequence of this isoform differs from the canonical sequence as follows:
     155-159: Missing.
     268-368: IQVGGTVMFC...GFQGLDIHPP → MLWSVPTLTS...CVCACLSDRP
     369-401: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.9
Propeptide20 – 5334Activation peptide
PRO_0000025974
Chain54 – 401348Cathepsin E form I
PRO_0000025975
Chain57 – 401345Cathepsin E form II
PRO_0000354668

Sites

Active site961 By similarity
Active site2861 By similarity

Amino acid modifications

Glycosylation901N-linked (GlcNAc...)
Disulfide bond60Interchain Ref.11
Disulfide bond109 ↔ 114 By similarity
Disulfide bond277 ↔ 281 By similarity
Disulfide bond319 ↔ 356 By similarity

Natural variations

Alternative sequence155 – 1595Missing in isoform 1 and isoform 2.
VSP_009729
Alternative sequence268 – 368101IQVGG…DIHPP → MLWSVPTLTSCRMSPSPLTE SPIPSAQLPTPYWTSWMECS SAAVAFKDLTSTLQLGPSGS WGMSSFDSFTQSLTVGITVW DWPQQSPKEGPCVCACLSDR P in isoform 2.
VSP_009730
Alternative sequence369 – 40133Missing in isoform 2.
VSP_009731
Natural variant821I → V.
Corresponds to variant rs57621203 [ dbSNP | Ensembl ].
VAR_061731
Natural variant3291T → I.
Corresponds to variant rs6503 [ dbSNP | Ensembl ].
VAR_014572

Experimental info

Mutagenesis601C → A: Abolishes homodimerization. Ref.11

Secondary structure

......................................................................... 401
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 3 [UniParc].

Last modified March 29, 2004. Version 2.
Checksum: 46A2BA35266032CB

FASTA40143,312
        10         20         30         40         50         60 
MKTLLLLLLV LLELGEAQGS LHRVPLRRHP SLKKKLRARS QLSEFWKSHN LDMIQFTESC 

        70         80         90        100        110        120 
SMDQSAKEPL INYLDMEYFG TISIGSPPQN FTVIFDTGSS NLWVPSVYCT SPACKTHSRF 

       130        140        150        160        170        180 
QPSQSSTYSQ PGQSFSIQYG TGSLSGIIGA DQVSAFATQV EGLTVVGQQF GESVTEPGQT 

       190        200        210        220        230        240 
FVDAEFDGIL GLGYPSLAVG GVTPVFDNMM AQNLVDLPMF SVYMSSNPEG GAGSELIFGG 

       250        260        270        280        290        300 
YDHSHFSGSL NWVPVTKQAY WQIALDNIQV GGTVMFCSEG CQAIVDTGTS LITGPSDKIK 

       310        320        330        340        350        360 
QLQNAIGAAP VDGEYAVECA NLNVMPDVTF TINGVPYTLS PTAYTLLDFV DGMQFCSSGF 

       370        380        390        400 
QGLDIHPPAG PLWILGDVFI RQFYSVFDRG NNRVGLAPAV P 

« Hide

Isoform 1 [UniParc].

Checksum: 40B643C5FB01521E
Show »

FASTA39642,794
Isoform 2 [UniParc].

Checksum: 4443819D6393C1FC
Show »

FASTA36339,553

References

« Hide 'large scale' references
[1]"Human gastric cathepsin E. Predicted sequence, localization to chromosome 1, and sequence homology with other aspartic proteinases."
Azuma T., Pals G., Mohandas T.K., Couvreur J.M., Taggart R.T.
J. Biol. Chem. 264:16748-16753(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Tissue: Gastric mucosa.
[2]"Human gastric cathepsin E gene. Multiple transcripts result from alternative polyadenylation of the primary transcripts of a single gene locus at 1q31-q32."
Azuma T., Liu W.G., Vander Laan D.J., Bowcock A.M., Taggart R.T.
J. Biol. Chem. 267:1609-1614(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), TISSUE SPECIFICITY.
[3]"Subcellular localization and targeting of cathepsin E."
Finley E.M., Kornfeld S.
J. Biol. Chem. 269:31259-31266(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), SUBCELLULAR LOCATION, GLYCOSYLATION.
Tissue: Intestine.
[4]"An alternatively spliced variant of cathepsin E in human gastric adenocarcinoma cells."
Tatnell P.J., Cook M., Kay J.
Biochim. Biophys. Acta 1625:203-206(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Tissue: Gastric adenocarcinoma.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Stomach.
[6]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[9]"Isolation and biochemical characterization of procathepsin E from human erythrocyte membranes."
Takeda-Ezaki M., Yamamoto K.
Arch. Biochem. Biophys. 304:352-358(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-38 AND 54-76, BIOPHYSICOCHEMICAL PROPERTIES, AUTOCATALYTIC CLEAVAGE, GLYCOSYLATION.
Tissue: Erythrocyte.
[10]"Structural evidence for two isozymic forms and the carbohydrate attachment site of human gastric cathepsin E."
Athauda S.B.P., Matsuzaki O., Kgeyama T., Takahashi K.
Biochem. Biophys. Res. Commun. 168:878-885(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 54-68; 77-95; 141-154; 280-290 AND 394-401, GLYCOSYLATION.
Tissue: Gastric mucosa.
[11]"Monomeric human cathepsin E."
Fowler S.D., Kay J., Dunn B.M., Tatnell P.J.
FEBS Lett. 366:72-74(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, SUBUNIT, DISULFIDE BONDS, MUTAGENESIS OF CYS-60.
[12]"Regulation of cathepsin E expression during human B cell differentiation in vitro."
Sealy L., Mota F., Rayment N., Tatnell P.J., Kay J., Chain B.
Eur. J. Immunol. 26:1838-1843(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
[13]"Regulation of human and mouse procathepsin E gene expression."
Cook M., Caswell R.C., Richards R.J., Kay J., Tatnell P.J.
Eur. J. Biochem. 268:2658-2668(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J05036 mRNA. Translation: AAA52130.1.
M84424 expand/collapse EMBL AC list , M84413, M84417, M84418, M84419, M84420, M84421, M84422 Genomic DNA. Translation: AAA52300.1.
AJ250716 mRNA. Translation: CAB82849.1.
AJ250717 mRNA. Translation: CAB82850.1.
AK292057 mRNA. Translation: BAF84746.1.
BX571818 Genomic DNA. Translation: CAH73264.1.
BX571818 Genomic DNA. Translation: CAH73265.1.
CH471067 Genomic DNA. Translation: EAW91592.1.
CH471067 Genomic DNA. Translation: EAW91593.1.
BC042537 mRNA. Translation: AAH42537.1.
PIRA34401. A42038.
RefSeqNP_001901.1. NM_001910.3.
NP_683865.1. NM_148964.2.
UniGeneHs.644082.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LCGmodel-A1-401[»]
1TZSX-ray2.35A54-401[»]
P19-53[»]
ProteinModelPortalP14091.
SMRP14091. Positions 21-400.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107890. 1 interaction.
IntActP14091. 2 interactions.
MINTMINT-1388890.
STRING9606.ENSP00000350911.

Chemistry

BindingDBP14091.
ChEMBLCHEMBL3092.
GuidetoPHARMACOLOGY2346.

Protein family/group databases

MEROPSA01.010.

PTM databases

PhosphoSiteP14091.

Polymorphism databases

DMDM46397366.

Proteomic databases

PaxDbP14091.
PRIDEP14091.

Protocols and materials databases

DNASU1510.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000358184; ENSP00000350911; ENSG00000196188. [P14091-1]
ENST00000360218; ENSP00000353350; ENSG00000196188. [P14091-2]
ENST00000581049; ENSP00000463969; ENSG00000264606. [P14091-2]
ENST00000583663; ENSP00000463953; ENSG00000264606. [P14091-1]
GeneID1510.
KEGGhsa:1510.
UCSCuc001hdu.3. human. [P14091-1]
uc001hdv.3. human. [P14091-2]

Organism-specific databases

CTD1510.
GeneCardsGC01P206319.
HGNCHGNC:2530. CTSE.
HPACAB032687.
HPA012940.
MIM116890. gene.
neXtProtNX_P14091.
PharmGKBPA27030.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG248684.
HOGENOMHOG000197681.
HOVERGENHBG000482.
InParanoidP14091.
KOK01382.
PhylomeDBP14091.
TreeFamTF314990.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SABIO-RKP14091.

Gene expression databases

ArrayExpressP14091.
BgeeP14091.
CleanExHS_CTSE.
GenevestigatorP14091.

Family and domain databases

Gene3D2.40.70.10. 2 hits.
InterProIPR001461. Aspartic_peptidase.
IPR001969. Aspartic_peptidase_AS.
IPR012848. Aspartic_peptidase_N.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERPTHR13683. PTHR13683. 1 hit.
PfamPF07966. A1_Propeptide. 1 hit.
PF00026. Asp. 1 hit.
[Graphical view]
PRINTSPR00792. PEPSIN.
SUPFAMSSF50630. SSF50630. 1 hit.
PROSITEPS00141. ASP_PROTEASE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP14091.
GeneWikiCathepsin_E.
GenomeRNAi1510.
NextBio6251.
PMAP-CutDBP14091.
PROP14091.
SOURCESearch...

Entry information

Entry nameCATE_HUMAN
AccessionPrimary (citable) accession number: P14091
Secondary accession number(s): Q5TZ01 expand/collapse secondary AC list , Q5TZ02, Q9NY58, Q9UCE3, Q9UCE4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: March 29, 2004
Last modified: April 16, 2014
This is version 158 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM