Cathepsin L1 precursor - Mus musculus (Mouse)

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P06797 (CATL1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 134. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Cathepsin L1
EC=3.4.22.15

Alternative name(s):
Major excreted protein
Short name=MEP
p39 cysteine proteinase

Gene names

Name:	Ctsl1
Synonyms:	Ctsl

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	334 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.
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.
Sequence similarities	Belongs to the peptidase C1 family.

Ontologies

Keywords
Cellular component	Lysosome
Domain	Signal
Molecular function	Hydrolase Protease Thiol protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	Sertoli cell differentiation Inferred from sequence or structural similarity. Source: BHF-UCL autophagic cell death Inferred from sequence or structural similarity. Source: BHF-UCL cellular response to starvation Inferred from sequence or structural similarity. Source: BHF-UCL decidualization Inferred from sequence or structural similarity. Source: BHF-UCL multicellular organismal aging Inferred from sequence or structural similarity. Source: BHF-UCL nerve development Inferred from sequence or structural similarity. Source: BHF-UCL proteolysis Inferred from direct assay PubMed 18957203. Source: BHF-UCL response to glucocorticoid stimulus Inferred from sequence or structural similarity. Source: BHF-UCL response to glucose stimulus Inferred from sequence or structural similarity. Source: BHF-UCL response to gonadotropin stimulus Inferred from sequence or structural similarity. Source: BHF-UCL spermatogenesis Inferred from sequence or structural similarity. Source: BHF-UCL stem cell differentiation Non-traceable author statement PubMed 18957203. Source: BHF-UCL
Cellular_component	external side of plasma membrane Inferred from sequence or structural similarity. Source: BHF-UCL lysosome Inferred from sequence or structural similarity. Source: BHF-UCL microvillus Inferred from sequence or structural similarity. Source: BHF-UCL neuron projection Inferred from sequence or structural similarity. Source: BHF-UCL nucleolus Non-traceable author statement PubMed 20338168. Source: BHF-UCL perikaryon Inferred from sequence or structural similarity. Source: BHF-UCL
Molecular_function	aminopeptidase activity Inferred from sequence or structural similarity. Source: BHF-UCL cysteine-type endopeptidase activity Inferred from sequence or structural similarity. Source: BHF-UCL histone binding Non-traceable author statement PubMed 18957203. Source: BHF-UCL peptide binding Inferred from sequence or structural similarity. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 17

Ref.7

Propeptide

18 – 113

Activation peptide

PRO_0000026248

Chain

114 – 288

175

Cathepsin L1 heavy chain

PRO_0000026249

Propeptide

289 – 290

PRO_0000026250

Chain

291 – 334

Cathepsin L1 light chain

PRO_0000026251

Sites

Active site

138

By similarity

Active site

276

By similarity

Active site

300

By similarity

Amino acid modifications

Glycosylation

221

N-linked (GlcNAc...) (high mannose) Ref.4 Ref.9

Disulfide bond

135 ↔ 178

By similarity

Disulfide bond

169 ↔ 211

By similarity

Disulfide bond

269 ↔ 322

Interchain (between heavy and light chains) By similarity

Experimental info

Sequence conflict

M → I in AAA39984. Ref.2

Sequence conflict

M → I in AAD32136. Ref.2

Sequence conflict

M → I in AAD32137. Ref.2

Sequence conflict

M → I in AAD32138. Ref.2

Sequence conflict

177

G → R Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

P06797 [UniParc].

Last modified November 1, 1990. Version 2.
Checksum: FE6747043307AD98
Show »

FASTA

334

37,547

        10         20         30         40         50         60 
MNLLLLLAVL CLGTALATPK FDQTFSAEWH QWKSTHRRLY GTNEEEWRRA IWEKNMRMIQ 

        70         80         90        100        110        120 
LHNGEYSNGQ HGFSMEMNAF GDMTNEEFRQ VVNGYRHQKH KKGRLFQEPL MLKIPKSVDW 

       130        140        150        160        170        180 
REKGCVTPVK NQGQCGSCWA FSASGCLEGQ MFLKTGKLIS LSEQNLVDCS HAQGNQGCNG 

       190        200        210        220        230        240 
GLMDFAFQYI KENGGLDSEE SYPYEAKDGS CKYRAEFAVA NDTGFVDIPQ QEKALMKAVA 

       250        260        270        280        290        300 
TVGPISVAMD ASHPSLQFYS SGIYYEPNCS SKNLDHGVLL VGYGYEGTDS NKNKYWLVKN 

       310        320        330 
SWGSEWGMEG YIKIAKDRDN HCGLATAASY PVVN

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and expression of the cDNA for MEP (major excreted protein), a transformation-regulated secreted cathepsin." Troen B.R., Gal S., Gottesman M.M. Biochem. J. 246:731-735(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]	"Complete nucleotide and deduced amino acid sequences of human and murine preprocathepsin L. An abundant transcript induced by transformation of fibroblasts." Joseph L.J., Chang L.C., Stamenkovich D., Sukhatme V.P. J. Clin. Invest. 81:1621-1629(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Cloning and characterization of a mouse cysteine proteinase." Portnoy D.A., Erickson A.H., Kochan J., Ravetch J.V., Unkeless J.C. J. Biol. Chem. 261:14697-14703(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Comparison of cathepsin L synthesized by normal and transformed cells at the gene, message, protein, and oligosaccharide levels." Stearns N.A., Dong J., Pan J.X., Brenner D.A., Sahagian G.G. Arch. Biochem. Biophys. 283:447-457(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE, GLYCOSYLATION AT ASN-221. Tissue: Liver.
[5]	"Mutant cells selected during persistent reovirus infection do not express mature cathepsin L and do not support reovirus disassembly." Baer G.S., Ebert D.H., Chung C.J., Erickson A.H., Dermody T.S. J. Virol. 73:9532-9543(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C3H/An.
[6]	"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]. Strain: C57BL/6. Tissue: Brain.
[7]	"Identification on melanoma cells of p39, a cysteine proteinase that cleaves C3, the third component of complement: amino-acid-sequence identities with procathepsin L." Jean D., Hermann J., Rodrigues-Lima F., Barel M., Balbo M., Frade R. Biochem. J. 312:961-969(1995) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 18-34; 273-292 AND 295-313.
[8]	"Close relationship of the major excreted protein of transformed murine fibroblasts to thiol-dependent cathepsins." Denhardt D.T., Hamilton R.T., Parfett C.L.J., Edwards D.R., Pierre R.S., Waterhouse P., Nilson-Hamilton M. Cancer Res. 46:4590-4593(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 89-300. Strain: BNL.
[9]	"High throughput quantitative glycomics and glycoform-focused proteomics of murine dermis and epidermis." Uematsu R., Furukawa J., Nakagawa H., Shinohara Y., Deguchi K., Monde K., Nishimura S. Mol. Cell. Proteomics 4:1977-1989(2005) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-221, MASS SPECTROMETRY. Tissue: Epidermis.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X06086 mRNA. Translation: CAA29470.1.
J02583 mRNA. Translation: AAA37445.1.
M20495 Genomic DNA. Translation: AAA39984.1.
AF121837 mRNA. Translation: AAD32136.1.
AF121838 mRNA. Translation: AAD32137.1.
AF121839 mRNA. Translation: AAD32138.1.
BC068163 mRNA. Translation: AAH68163.1.
X04392 mRNA. Translation: CAA27980.1.

IPI

IPI00128154.

PIR

KHMSL. S01177.

RefSeq

NP_034114.1. NM_009984.3.

UniGene

Mm.930.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MVV	model	-	A	22-334	[»]

ProteinModelPortal

P06797.

SMR

P06797. Positions 21-333.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-1863740.

Protein family/group databases

MEROPS

C01.032.

PTM databases

PhosphoSite

P06797.

Proteomic databases

PaxDb

P06797.

PRIDE

P06797.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000021933; ENSMUSP00000021933; ENSMUSG00000021477.

GeneID

13039.

KEGG

mmu:13039.

UCSC

uc007qyw.1. mouse.

Organism-specific databases

CTD

13039.

MGI

MGI:88564. Ctsl.

Phylogenomic databases

eggNOG

COG4870.

HOGENOM

HOG000230774.

HOVERGEN

HBG011513.

InParanoid

P06797.

K01365.

OMA

EEFRATH.

OrthoDB

EOG48PMKF.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-14812.

BRENDA

3.4.22.15. 3474.

Gene expression databases

ArrayExpress

P06797.

Bgee

P06797.

CleanEx

MM_CTSL.

Genevestigator

P06797.

GermOnline

ENSMUSG00000021477. Mus musculus.

Family and domain databases

InterPro

IPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]

PANTHER

PTHR12411. PTHR12411. 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

BindingDB

P06797.

ChEMBL

CHEMBL5291.

ChiTaRS

CTSL1. mouse.

NextBio

282928.

SOURCE

Search...

Entry information

Entry name

CATL1_MOUSE

Accession

Primary (citable) accession number: P06797
Secondary accession number(s): Q91UZ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	November 1, 1990
Last modified:	May 29, 2013
This is version 134 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following 2 chains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents