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Protein

Cathepsin L

Gene

Cp1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Important for the overall degradation of proteins in lysosomes. Essential for adult male and female fertility. May play a role in digestion.3 Publications

Catalytic activityi

Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity toward protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei178 – 1781By similarity
Active sitei317 – 3171By similarity
Active sitei338 – 3381By similarity

GO - Molecular functioni

  • cysteine-type endopeptidase activity Source: FlyBase
  • peptidase activity Source: FlyBase

GO - Biological processi

  • autophagic cell death Source: FlyBase
  • digestion Source: UniProtKB-KW
  • protein catabolic process Source: FlyBase
  • proteolysis Source: FlyBase
  • salivary gland cell autophagic cell death Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Digestion

Enzyme and pathway databases

ReactomeiR-DME-1442490. Collagen degradation.
R-DME-1474228. Degradation of the extracellular matrix.
R-DME-1592389. Activation of Matrix Metalloproteinases.
R-DME-1679131. Trafficking and processing of endosomal TLR.
R-DME-2132295. MHC class II antigen presentation.

Protein family/group databases

MEROPSiC01.092.

Names & Taxonomyi

Protein namesi
Recommended name:
Cathepsin L (EC:3.4.22.15)
Alternative name(s):
Cysteine proteinase 1
Cleaved into the following 2 chains:
Gene namesi
Name:Cp1
Synonyms:fs(2)50Ca
ORF Names:CG6692
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0013770. Cp1.

Subcellular locationi

  • Lysosome 1 Publication

GO - Cellular componenti

  • fusome Source: FlyBase
  • lysosome Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Disruption phenotypei

Flies exhibit wing and pigmentation defects. Females are sterile, males are partially sterile.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4848Sequence analysisAdd
BLAST
Propeptidei49 – 153105Activation peptidePRO_0000026265Add
BLAST
Chaini154 – 326173Cathepsin L heavy chainPRO_0000026266Add
BLAST
Propeptidei327 – 3293PRO_0000026267
Chaini330 – 37142Cathepsin L light chainPRO_0000026268Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi127 – 1271N-linked (GlcNAc...)Sequence analysis
Disulfide bondi175 ↔ 218By similarity
Disulfide bondi209 ↔ 251By similarity
Disulfide bondi310 ↔ 360Interchain (between heavy and light chains)By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiQ95029.
PRIDEiQ95029.

Expressioni

Tissue specificityi

In the embryo, predominantly expressed in the midgut. Also expressed in larval alimentary organs such as salivary gland and midgut including gastric caeca.1 Publication

Developmental stagei

Expressed in embryo, larva, pupa and adult.1 Publication

Gene expression databases

BgeeiQ95029.
ExpressionAtlasiQ95029. differential.
GenevisibleiQ95029. DM.

Interactioni

Subunit structurei

Dimer of a heavy and a light chain linked by disulfide bonds.

Protein-protein interaction databases

BioGridi62300. 36 interactions.
IntActiQ95029. 2 interactions.
MINTiMINT-814156.
STRINGi7227.FBpp0086719.

Structurei

3D structure databases

ProteinModelPortaliQ95029.
SMRiQ95029. Positions 58-371.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1543. Eukaryota.
COG4870. LUCA.
GeneTreeiENSGT00760000118871.
InParanoidiQ95029.
KOiK01365.
OMAiMEEWHTF.
OrthoDBiEOG786H3P.
PhylomeDBiQ95029.

Family and domain databases

InterProiIPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PfamiPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSiPR00705. PAPAIN.
SMARTiSM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform C (identifier: Q95029-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MNHLGVFETR FRPRTRHKSQ RAQLIPEQIT MRTAVLLPLL ALLAVAQAVS
60 70 80 90 100
FADVVMEEWH TFKLEHRKNY QDETEERFRL KIFNENKHKI AKHNQRFAEG
110 120 130 140 150
KVSFKLAVNK YADLLHHEFR QLMNGFNYTL HKQLRAADES FKGVTFISPA
160 170 180 190 200
HVTLPKSVDW RTKGAVTAVK DQGHCGSCWA FSSTGALEGQ HFRKSGVLVS
210 220 230 240 250
LSEQNLVDCS TKYGNNGCNG GLMDNAFRYI KDNGGIDTEK SYPYEAIDDS
260 270 280 290 300
CHFNKGTVGA TDRGFTDIPQ GDEKKMAEAV ATVGPVSVAI DASHESFQFY
310 320 330 340 350
SEGVYNEPQC DAQNLDHGVL VVGFGTDESG EDYWLVKNSW GTTWGDKGFI
360 370
KMLRNKENQC GIASASSYPL V
Note: No experimental confirmation available.
Length:371
Mass (Da):41,601
Last modified:November 28, 2006 - v2
Checksum:i01955EB4735316D7
GO
Isoform A (identifier: Q95029-2) [UniParc]FASTAAdd to basket

Also known as: B

The sequence of this isoform differs from the canonical sequence as follows:
     2-31: Missing.

Show »
Length:341
Mass (Da):37,971
Checksum:iD18382396ACE1D59
GO

Sequence cautioni

The sequence BAA06738.1 differs from that shown.Intron retention.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti228 – 2281R → P in BAA06738 (PubMed:7851441).Curated
Sequence conflicti255 – 2573KGT → RAQ in BAA06738 (PubMed:7851441).Curated
Sequence conflicti277 – 2815AEAVA → PEPVP in BAA06738 (PubMed:7851441).Curated
Sequence conflicti365 – 3651A → P in BAA06738 (PubMed:7851441).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2 – 3130Missing in isoform A. 2 PublicationsVSP_021771Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U75652 mRNA. Translation: AAB18345.1.
AF012089 Genomic DNA. Translation: AAB65749.1.
AE013599 Genomic DNA. Translation: AAF58311.1.
AE013599 Genomic DNA. Translation: AAM68565.1.
BT016071 mRNA. Translation: AAV36956.1.
D31970 Genomic DNA. Translation: BAA06738.1. Sequence problems.
RefSeqiNP_523735.2. NM_079011.3. [Q95029-1]
NP_725347.1. NM_166026.3. [Q95029-2]
UniGeneiDm.7400.

Genome annotation databases

EnsemblMetazoaiFBtr0087593; FBpp0086719; FBgn0013770. [Q95029-1]
GeneIDi36546.
KEGGidme:Dmel_CG6692.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U75652 mRNA. Translation: AAB18345.1.
AF012089 Genomic DNA. Translation: AAB65749.1.
AE013599 Genomic DNA. Translation: AAF58311.1.
AE013599 Genomic DNA. Translation: AAM68565.1.
BT016071 mRNA. Translation: AAV36956.1.
D31970 Genomic DNA. Translation: BAA06738.1. Sequence problems.
RefSeqiNP_523735.2. NM_079011.3. [Q95029-1]
NP_725347.1. NM_166026.3. [Q95029-2]
UniGeneiDm.7400.

3D structure databases

ProteinModelPortaliQ95029.
SMRiQ95029. Positions 58-371.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi62300. 36 interactions.
IntActiQ95029. 2 interactions.
MINTiMINT-814156.
STRINGi7227.FBpp0086719.

Protein family/group databases

MEROPSiC01.092.

Proteomic databases

PaxDbiQ95029.
PRIDEiQ95029.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0087593; FBpp0086719; FBgn0013770. [Q95029-1]
GeneIDi36546.
KEGGidme:Dmel_CG6692.

Organism-specific databases

CTDi36546.
FlyBaseiFBgn0013770. Cp1.

Phylogenomic databases

eggNOGiKOG1543. Eukaryota.
COG4870. LUCA.
GeneTreeiENSGT00760000118871.
InParanoidiQ95029.
KOiK01365.
OMAiMEEWHTF.
OrthoDBiEOG786H3P.
PhylomeDBiQ95029.

Enzyme and pathway databases

ReactomeiR-DME-1442490. Collagen degradation.
R-DME-1474228. Degradation of the extracellular matrix.
R-DME-1592389. Activation of Matrix Metalloproteinases.
R-DME-1679131. Trafficking and processing of endosomal TLR.
R-DME-2132295. MHC class II antigen presentation.

Miscellaneous databases

GenomeRNAii36546.
PROiQ95029.

Gene expression databases

BgeeiQ95029.
ExpressionAtlasiQ95029. differential.
GenevisibleiQ95029. DM.

Family and domain databases

InterProiIPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PfamiPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSiPR00705. PAPAIN.
SMARTiSM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cysteine proteinase 1 (CP1), a cathepsin L-like enzyme expressed in the Drosophila melanogaster haemocyte cell line mbn-2."
    Tryselius Y., Hultmark D.
    Insect Mol. Biol. 6:173-181(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR LOCATION.
    Tissue: Hemocyte.
  2. "Structure and associated mutational effects of the cysteine proteinase (CP1) gene of Drosophila melanogaster."
    Gray Y.H.M., Sved J.A., Preston C.R., Engels W.R.
    Insect Mol. Biol. 7:291-293(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE.
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  5. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
    Strain: Berkeley.
    Tissue: Larva and Pupae.
  6. "A putative digestive cysteine proteinase from Drosophila melanogaster is predominantly expressed in the embryonic and larval midgut."
    Matsumoto I., Watanabe H., Abe K., Arai S., Emori Y.
    Eur. J. Biochem. 227:582-587(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 64-371, FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: Canton-S.

Entry informationi

Entry nameiCATL_DROME
AccessioniPrimary (citable) accession number: Q95029
Secondary accession number(s): O97431, Q5U121
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: November 28, 2006
Last modified: June 8, 2016
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.