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P06797

- CATL1_MOUSE

UniProt

P06797 - CATL1_MOUSE

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Protein

Cathepsin L1

Gene

Ctsl

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Important for the overall degradation of proteins in lysosomes.

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 sitei138 – 1381By similarity
Active sitei276 – 2761By similarity
Active sitei300 – 3001By similarity

GO - Molecular functioni

  1. aminopeptidase activity Source: BHF-UCL
  2. cysteine-type carboxypeptidase activity Source: MGI
  3. cysteine-type endopeptidase activity Source: BHF-UCL
  4. histone binding Source: BHF-UCL
  5. peptide binding Source: BHF-UCL

GO - Biological processi

  1. autophagic cell death Source: BHF-UCL
  2. catagen Source: MGI
  3. cell communication Source: BHF-UCL
  4. cellular response to starvation Source: BHF-UCL
  5. decidualization Source: BHF-UCL
  6. hair follicle morphogenesis Source: MGI
  7. male gonad development Source: BHF-UCL
  8. multicellular organismal aging Source: BHF-UCL
  9. negative regulation of keratinocyte proliferation Source: MGI
  10. nerve development Source: BHF-UCL
  11. protein autoprocessing Source: MGI
  12. protein processing Source: MGI
  13. proteolysis Source: BHF-UCL
  14. regulation of actin cytoskeleton reorganization Source: MGI
  15. response to glucocorticoid Source: BHF-UCL
  16. response to glucose Source: BHF-UCL
  17. response to gonadotropin Source: BHF-UCL
  18. response to organic cyclic compound Source: BHF-UCL
  19. Sertoli cell differentiation Source: BHF-UCL
  20. spermatogenesis Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14812.
BRENDAi3.4.22.15. 3474.
ReactomeiREACT_196550. MHC class II antigen presentation.
REACT_198976. Trafficking and processing of endosomal TLR.
REACT_199000. Activation of Matrix Metalloproteinases.
REACT_199046. Assembly of collagen fibrils and other multimeric structures.
REACT_199052. Degradation of the extracellular matrix.
REACT_199055. Collagen degradation.

Protein family/group databases

MEROPSiC01.032.

Names & Taxonomyi

Protein namesi
Recommended name:
Cathepsin L1 (EC:3.4.22.15)
Alternative name(s):
Cathepsin L
Major excreted protein
Short name:
MEP
p39 cysteine proteinase
Cleaved into the following 2 chains:
Gene namesi
Name:Ctsl
Synonyms:Ctsl1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 13

Organism-specific databases

MGIiMGI:88564. Ctsl.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: BHF-UCL
  2. cytoplasmic vesicle Source: MGI
  3. external side of plasma membrane Source: BHF-UCL
  4. extracellular space Source: MGI
  5. extracellular vesicular exosome Source: Ensembl
  6. lysosome Source: BHF-UCL
  7. microvillus Source: BHF-UCL
  8. neuron projection Source: BHF-UCL
  9. nucleolus Source: BHF-UCL
  10. nucleus Source: BHF-UCL
  11. perikaryon Source: BHF-UCL
  12. vacuole Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 17171 PublicationAdd
BLAST
Propeptidei18 – 11396Activation peptidePRO_0000026248Add
BLAST
Chaini114 – 288175Cathepsin L1 heavy chainPRO_0000026249Add
BLAST
Propeptidei289 – 2902PRO_0000026250
Chaini291 – 33444Cathepsin L1 light chainPRO_0000026251Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi135 ↔ 178By similarity
Disulfide bondi169 ↔ 211By similarity
Glycosylationi221 – 2211N-linked (GlcNAc...) (high mannose)2 Publications
Disulfide bondi269 ↔ 322Interchain (between heavy and light chains)By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQBiP06797.
PaxDbiP06797.
PRIDEiP06797.

PTM databases

PhosphoSiteiP06797.

Expressioni

Gene expression databases

BgeeiP06797.
CleanExiMM_CTSL.
ExpressionAtlasiP06797. baseline and differential.
GenevestigatoriP06797.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiP06797. 3 interactions.
MINTiMINT-1863740.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MVVmodel-A22-334[»]
ProteinModelPortaliP06797.
SMRiP06797. Positions 21-333.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG4870.
HOGENOMiHOG000230774.
HOVERGENiHBG011513.
InParanoidiP06797.
KOiK01365.
OMAiSMEMNAF.
OrthoDBiEOG786H3P.
PhylomeDBiP06797.
TreeFamiTF313739.

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]

Sequencei

Sequence statusi: Complete.

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

P06797-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNLLLLLAVL CLGTALATPK FDQTFSAEWH QWKSTHRRLY GTNEEEWRRA
60 70 80 90 100
IWEKNMRMIQ LHNGEYSNGQ HGFSMEMNAF GDMTNEEFRQ VVNGYRHQKH
110 120 130 140 150
KKGRLFQEPL MLKIPKSVDW REKGCVTPVK NQGQCGSCWA FSASGCLEGQ
160 170 180 190 200
MFLKTGKLIS LSEQNLVDCS HAQGNQGCNG GLMDFAFQYI KENGGLDSEE
210 220 230 240 250
SYPYEAKDGS CKYRAEFAVA NDTGFVDIPQ QEKALMKAVA TVGPISVAMD
260 270 280 290 300
ASHPSLQFYS SGIYYEPNCS SKNLDHGVLL VGYGYEGTDS NKNKYWLVKN
310 320 330
SWGSEWGMEG YIKIAKDRDN HCGLATAASY PVVN
Length:334
Mass (Da):37,547
Last modified:November 1, 1990 - v2
Checksum:iFE6747043307AD98
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti58 – 581M → I in AAA39984. (PubMed:2835398)Curated
Sequence conflicti58 – 581M → I in AAD32136. (PubMed:2835398)Curated
Sequence conflicti58 – 581M → I in AAD32137. (PubMed:2835398)Curated
Sequence conflicti58 – 581M → I in AAD32138. (PubMed:2835398)Curated
Sequence conflicti177 – 1771G → R(PubMed:3533924)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS26600.1.
PIRiS01177. KHMSL.
RefSeqiNP_034114.1. NM_009984.3.
XP_006517143.1. XM_006517080.1.
XP_006517144.1. XM_006517081.1.
UniGeneiMm.930.

Genome annotation databases

EnsembliENSMUST00000021933; ENSMUSP00000021933; ENSMUSG00000021477.
GeneIDi13039.
KEGGimmu:13039.
UCSCiuc007qyw.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS26600.1.
PIRi S01177. KHMSL.
RefSeqi NP_034114.1. NM_009984.3.
XP_006517143.1. XM_006517080.1.
XP_006517144.1. XM_006517081.1.
UniGenei Mm.930.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1MVV model - A 22-334 [» ]
ProteinModelPortali P06797.
SMRi P06797. Positions 21-333.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P06797. 3 interactions.
MINTi MINT-1863740.

Chemistry

BindingDBi P06797.
ChEMBLi CHEMBL5291.

Protein family/group databases

MEROPSi C01.032.

PTM databases

PhosphoSitei P06797.

Proteomic databases

MaxQBi P06797.
PaxDbi P06797.
PRIDEi P06797.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000021933 ; ENSMUSP00000021933 ; ENSMUSG00000021477 .
GeneIDi 13039.
KEGGi mmu:13039.
UCSCi uc007qyw.1. mouse.

Organism-specific databases

CTDi 1514.
MGIi MGI:88564. Ctsl.

Phylogenomic databases

eggNOGi COG4870.
HOGENOMi HOG000230774.
HOVERGENi HBG011513.
InParanoidi P06797.
KOi K01365.
OMAi SMEMNAF.
OrthoDBi EOG786H3P.
PhylomeDBi P06797.
TreeFami TF313739.

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-14812.
BRENDAi 3.4.22.15. 3474.
Reactomei REACT_196550. MHC class II antigen presentation.
REACT_198976. Trafficking and processing of endosomal TLR.
REACT_199000. Activation of Matrix Metalloproteinases.
REACT_199046. Assembly of collagen fibrils and other multimeric structures.
REACT_199052. Degradation of the extracellular matrix.
REACT_199055. Collagen degradation.

Miscellaneous databases

NextBioi 282928.
PROi P06797.
SOURCEi Search...

Gene expression databases

Bgeei P06797.
CleanExi MM_CTSL.
ExpressionAtlasi P06797. baseline and differential.
Genevestigatori P06797.

Family and domain databases

InterProi 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 ]
PANTHERi PTHR12411. PTHR12411. 1 hit.
Pfami PF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view ]
PRINTSi PR00705. PAPAIN.
SMARTi SM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view ]
PROSITEi PS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    Tissue: Epidermis.

Entry informationi

Entry nameiCATL1_MOUSE
AccessioniPrimary (citable) accession number: P06797
Secondary accession number(s): Q91UZ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: November 1, 1990
Last modified: November 26, 2014
This is version 150 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3