Reviewed, UniProtKB/Swiss-Prot Q95029 (CATL_DROME)

Names and origin

Protein names

Recommended name:
    Cathepsin L
    EC=3.4.22.15
Alternative name(s):
    Cysteine proteinase 1
Cleaved into the following 2 chains:
    1- Recommended name:
            Cathepsin L heavy chain
    2- Recommended name:
            Cathepsin L light chain

Gene names

Name:	Cp1
Synonyms:	fs(2)50Ca
ORF Names:	CG6692

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	371 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Important for the overall degradation of proteins in lysosomes. Essential for adult male and female fertility. May play a role in digestion. Ref.1 Ref.2 Ref.6
Catalytic activity	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.
Subunit structure	Dimer of a heavy and a light chain linked by disulfide bonds.
Subcellular location	Lysosome Ref.1.
Tissue specificity	In the embryo, predominantly expressed in the midgut. Also expressed in larval alimentary organs such as salivary gland and midgut including gastric caeca. Ref.6
Developmental stage	Expressed in embryo, larva, pupa and adult. Ref.6
Disruption phenotype	Flies exhibit wing and pigmentation defects. Females are sterile, males are partially sterile. Ref.2
Sequence similarities	Belongs to the peptidase C1 family.
Sequence caution	The sequence BAA06738.1 differs from that shown. Reason: Miscellaneous discrepancy. Intron retention.

Ontologies

Keywords
Biological process	Digestion
Cellular component	Lysosome
Coding sequence diversity	Alternative splicing
Domain	Signal
Molecular function	Developmental protein Hydrolase Protease Thiol protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	digestion Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: InterPro salivary gland cell autophagic cell death Inferred from expression pattern. Source: FlyBase
Cellular component	lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cysteine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Atpalpha	P13607-1	1	EBI-162713,EBI-213208

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform C (identifier: Q95029-1)

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.

Note: No experimental confirmation available.

Isoform A (identifier: Q95029-2)

Also known as: B;

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 48	48	Potential
	Propeptide	49 – 153	105	Activation peptide		PRO_0000026265
	Chain	154 – 326	173	Cathepsin L heavy chain		PRO_0000026266
	Propeptide	327 – 329	3			PRO_0000026267
	Chain	330 – 371	42	Cathepsin L light chain		PRO_0000026268
Sites
	Active site	178	1	By similarity
	Active site	317	1	By similarity
	Active site	338	1	By similarity
Amino acid modifications
	Glycosylation	127	1	N-linked (GlcNAc...) Potential
	Disulfide bond	175 ↔ 218		By similarity
	Disulfide bond	209 ↔ 251		By similarity
	Disulfide bond	310 ↔ 360		Interchain (between heavy and light chains) By similarity
Natural variations
	Alternative sequence	2 – 31	30	Missing in isoform A.		VSP_021771
Experimental info
	Sequence conflict	228	1	R → P in BAA06738. Ref.6
	Sequence conflict	255 – 257	3	KGT → RAQ in BAA06738. Ref.6
	Sequence conflict	277 – 281	5	AEAVA → PEPVP in BAA06738. Ref.6
	Sequence conflict	365	1	A → P in BAA06738. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform C [UniParc]. Last modified November 28, 2006. Version 2. Checksum: 01955EB4735316D7	FASTA	371	41,601
	10 20 30 40 50 60 MNHLGVFETR FRPRTRHKSQ RAQLIPEQIT MRTAVLLPLL ALLAVAQAVS FADVVMEEWH 70 80 90 100 110 120 TFKLEHRKNY QDETEERFRL KIFNENKHKI AKHNQRFAEG KVSFKLAVNK YADLLHHEFR 130 140 150 160 170 180 QLMNGFNYTL HKQLRAADES FKGVTFISPA HVTLPKSVDW RTKGAVTAVK DQGHCGSCWA 190 200 210 220 230 240 FSSTGALEGQ HFRKSGVLVS LSEQNLVDCS TKYGNNGCNG GLMDNAFRYI KDNGGIDTEK 250 260 270 280 290 300 SYPYEAIDDS CHFNKGTVGA TDRGFTDIPQ GDEKKMAEAV ATVGPVSVAI DASHESFQFY 310 320 330 340 350 360 SEGVYNEPQC DAQNLDHGVL VVGFGTDESG EDYWLVKNSW GTTWGDKGFI KMLRNKENQC 370 GIASASSYPL V
	Isoform A (B). Checksum: D18382396ACE1D59	FASTA	341	37,971
	10 20 30 40 50 60 MRTAVLLPLL ALLAVAQAVS FADVVMEEWH TFKLEHRKNY QDETEERFRL KIFNENKHKI 70 80 90 100 110 120 AKHNQRFAEG KVSFKLAVNK YADLLHHEFR QLMNGFNYTL HKQLRAADES FKGVTFISPA 130 140 150 160 170 180 HVTLPKSVDW RTKGAVTAVK DQGHCGSCWA FSSTGALEGQ HFRKSGVLVS LSEQNLVDCS 190 200 210 220 230 240 TKYGNNGCNG GLMDNAFRYI KDNGGIDTEK SYPYEAIDDS CHFNKGTVGA TDRGFTDIPQ 250 260 270 280 290 300 GDEKKMAEAV ATVGPVSVAI DASHESFQFY SEGVYNEPQC DAQNLDHGVL VVGFGTDESG 310 320 330 340 EDYWLVKNSW GTTWGDKGFI KMLRNKENQC GIASASSYPL V

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 9099581] [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: 9662479] [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: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[4]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
[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: 7851441] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 64-371, FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Strain: Canton-S.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
RefSeq	NP_523735.2. NP_725347.1. NP_725348.1.
UniGene	Dm.7400
3D structure databases
SMR	Q95029. Positions 54-371.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q95029. 6 interactions.
STRING	Q95029.
Protein family/group databases
MEROPS	C01.092.
Genome annotation databases
Ensembl	FBtr0087591; FBpp0086717; FBgn0013770; Drosophila melanogaster. [Genome view] FBtr0087592; FBpp0086718; FBgn0013770; Drosophila melanogaster. [Genome view] FBtr0087593; FBpp0086719; FBgn0013770; Drosophila melanogaster. [Genome view]
GeneID	36546.
KEGG	dme:Dmel_CG6692.
Organism-specific databases
CTD	36546.
FlyBase	FBgn0013770. Cp1.
Phylogenomic databases
eggNOG	inNOG08450.
InParanoid	Q95029.
OMA	GICGSAR.
OrthoDB	EOG9NS3JV.
PhylomeDB	Q95029.
Enzyme and pathway databases
BioCyc	DMEL-XXX-02:DMEL-XXX-02-004526-MONOMER. DMEL-XXX-02:DMEL-XXX-02-004527-MONOMER.
BRENDA	3.4.22.15. 48.
Gene expression databases
GermOnline	CG6692. Drosophila melanogaster.
Family and domain databases
InterPro	IPR000169. Pept_cys_AS. IPR013128. Peptidase_C1A. IPR000668. Peptidase_C1A_C. IPR013201. Prot_inhib_I29. [Graphical view]
PANTHER	PTHR12411. Peptidase_C1A. 1 hit.
Pfam	PF08246. Inhibitor_I29. 1 hit. PF00112. Peptidase_C1. 1 hit. [Graphical view]
PRINTS	PR00705. PAPAIN.
SMART	SM00848. Inhibitor_I29. 1 hit. SM00645. Pept_C1. 1 hit. [Graphical view]
PROSITE	PS00640. THIOL_PROTEASE_ASN. 1 hit. PS00139. THIOL_PROTEASE_CYS. 1 hit. PS00639. THIOL_PROTEASE_HIS. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	799136.

Entry information

Entry name

CATL_DROME

Accession

Primary (citable) accession number: Q95029
Secondary accession number(s): O97431, Q5U121

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	November 28, 2006
Last modified:	January 19, 2010
This is version 87 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project