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UniProtKB/Swiss-Prot entry P06797


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CATL1_MOUSE
Primary accession number P06797
Secondary accession number Q91UZ0
Integrated into Swiss-Prot on January 1, 1988
Sequence was last modified on November 1, 1990 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 94)
Name and origin of the protein
Protein name Cathepsin L1 [Precursor]
Synonyms EC 3.4.22.15
Major excreted protein
MEP
p39 cysteine proteinase
Contains Cathepsin L1 heavy chain
Cathepsin L1 light chain
Gene name
Name: Ctsl1
Synonyms: Ctsl
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=3689328 [NCBI, ExPASy, EBI, Israel, Japan]
Troen B.R., Gal S., Gottesman M.M.;
"Sequence and expression of the cDNA for MEP (major excreted protein), a transformation-regulated secreted cathepsin.";
Biochem. J. 246:731-735(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2835398 [NCBI, ExPASy, EBI, Israel, Japan]
Joseph L.J., Chang L.C., Stamenkovich D., Sukhatme V.P.;
"Complete nucleotide and deduced amino acid sequences of human and murine preprocathepsin L. An abundant transcript induced by transformation of fibroblasts.";
J. Clin. Invest. 81:1621-1629(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3533924 [NCBI, ExPASy, EBI, Israel, Japan]
Portnoy D.A., Erickson A.H., Kochan J., Ravetch J.V., Unkeless J.C.;
"Cloning and characterization of a mouse cysteine proteinase.";
J. Biol. Chem. 261:14697-14703(1986).
[4]
NUCLEOTIDE SEQUENCE, AND GLYCOSYLATION AT ASN-221.
TISSUE=Liver;
DOI=10.1016/0003-9861(90)90666-M; PubMed=2275556 [NCBI, ExPASy, EBI, Israel, Japan]
Stearns N.A., Dong J., Pan J.X., Brenner D.A., Sahagian G.G.;
"Comparison of cathepsin L synthesized by normal and transformed cells at the gene, message, protein, and oligosaccharide levels.";
Arch. Biochem. Biophys. 283:447-457(1990).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C3H/An;
PubMed=10516062 [NCBI, ExPASy, EBI, Israel, Japan]
Baer G.S., Ebert D.H., Chung C.J., Erickson A.H., Dermody T.S.;
"Mutant cells selected during persistent reovirus infection do not express mature cathepsin L and do not support reovirus disassembly.";
J. Virol. 73:9532-9543(1999).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6;
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 18-34; 273-292 AND 295-313.
PubMed=8554545 [NCBI, ExPASy, EBI, Israel, Japan]
Jean D., Hermann J., Rodrigues-Lima F., Barel M., Balbo M., Frade R.;
"Identification on melanoma cells of p39, a cysteine proteinase that cleaves C3, the third component of complement: amino-acid-sequence identities with procathepsin L.";
Biochem. J. 312:961-969(1995).
[8]
NUCLEOTIDE SEQUENCE OF 89-300.
STRAIN=BNL;
PubMed=3755373 [NCBI, ExPASy, EBI, Israel, Japan]
Denhardt D.T., Hamilton R.T., Parfett C.L.J., Edwards D.R., Pierre R.S., Waterhouse P., Nilson-Hamilton M.;
"Close relationship of the major excreted protein of transformed murine fibroblasts to thiol-dependent cathepsins.";
Cancer Res. 46:4590-4593(1986).
[9]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-221, AND MASS SPECTROMETRY.
TISSUE=Epidermis;
DOI=10.1074/mcp.M500203-MCP200; PubMed=16170054 [NCBI, ExPASy, EBI, Israel, Japan]
Uematsu R., Furukawa J., Nakagawa H., Shinohara Y., Deguchi K., Monde K., Nishimura S.;
"High throughput quantitative glycomics and glycoform-focused proteomics of murine dermis and epidermis.";
Mol. Cell. Proteomics 4:1977-1989(2005).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X06086; CAA29470.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J02583; AAA37445.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M20495; AAA39984.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF121837; AAD32136.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF121838; AAD32137.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF121839; AAD32138.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC068163; AAH68163.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X04392; CAA27980.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S01177; KHMSL.
RefSeq NP_034114.1; -.
UniGene Mm.930
3D structure databases
PDB
1MVV; Model; -; A=22-334.[ExPASy / RCSB / EBI]
PDBsum 1MVV; -.
SMR P06797; 21-333.
ModBase P06797.
Protein family/group databases
MEROPS C01.032; -.
I29.010; -.
Organism-specific databases
MGI MGI:88564; Ctsl.
Gene expression databases
ArrayExpress P06797; -.
CleanEx MM_CTSL; -.
GermOnline ENSMUSG00000021477; Mus musculus.
Ontologies
GO
GO:0008234; Molecular function: cysteine-type peptidase activity (traceable author statement from MGI).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from MGI).
QuickGo view.
Family and domain databases
InterPro IPR000169; Pept_cys_AS.
IPR013128; Peptidase_C1A.
IPR000668; Peptidase_C1A_C.
IPR013201; Prot_inhib_I29.
Graphical view of domain structure.
PANTHER PTHR12411; Peptidase_C1A; 1.
Pfam PF08246; Inhibitor_I29; 1.
PF00112; Peptidase_C1; 1.
Pfam graphical view of domain structure.
PRINTS PR00705; PAPAIN.
ProDom PD000158; Peptidase_C1; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00645; Pept_C1; 1.
SMART graphical view of domain structure.
PROSITE PS00640; THIOL_PROTEASE_ASN; 1.
PS00139; THIOL_PROTEASE_CYS; 1.
PS00639; THIOL_PROTEASE_HIS; 1.
BLOCKS P06797.
ProtoNet P06797.
Genome annotation databases
Ensembl ENSMUSG00000021477; Mus musculus. [Contig view]
GeneID 13039; -.
KEGG mmu:13039; -.
Phylogenomic databases
HOGENOM P06797; -.
HOVERGEN P06797; -.
Other
NextBio 282928; -.
SOURCE Ctsl1; Mus musculus.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Direct protein sequencing; Glycoprotein; Hydrolase; Lysosome; Protease; Signal; Thiol protease; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    17  17      
PROPEP   18   113  96     Activation peptide. PRO_0000026248
CHAIN   114   288  175     Cathepsin L1 heavy chain. PRO_0000026249
PROPEP   289   290  2      PRO_0000026250
CHAIN   291   334  44     Cathepsin L1 light chain. PRO_0000026251
ACT_SITE   138   138        By similarity. 
ACT_SITE   276   276        By similarity. 
ACT_SITE   300   300        By similarity. 
CARBOHYD   221   221        N-linked (GlcNAc...) (high mannose). 
DISULFID   135   178        By similarity. 
DISULFID   169   211        By similarity. 
DISULFID   269   322        Interchain (between heavy and light chains) (By similarity). 
CONFLICT   58    58        M -> I (in Ref. 2; AAA39984/AAD32136/AAD32137/AAD32138). 
CONFLICT   177   177        G -> R (in Ref. 3). 
Sequence information
Length: 334 AA [This is the length of the unprocessed precursor] Molecular weight: 37547 Da [This is the MW of the unprocessed precursor] CRC64: FE6747043307AD98 [This is a checksum on the sequence]
        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 

P06797 in FASTA format

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