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Cathepsin L1 (EC 3.4.22.15) (Cathepsin L) (Major excreted protein) (MEP) (p39 cysteine proteinase) [Cleaved into: Cathepsin L1 heavy chain; Cathepsin L1 light chain]

 CATL1_MOUSE             Reviewed;         334 AA.
P06797; Q91UZ0;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-NOV-1990, sequence version 2.
22-NOV-2017, entry version 180.
RecName: Full=Cathepsin L1;
EC=3.4.22.15;
AltName: Full=Cathepsin L;
AltName: Full=Major excreted protein;
Short=MEP;
AltName: Full=p39 cysteine proteinase;
Contains:
RecName: Full=Cathepsin L1 heavy chain;
Contains:
RecName: Full=Cathepsin L1 light chain;
Flags: Precursor;
Name=Ctsl; Synonyms=Ctsl1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=3689328; DOI=10.1042/bj2460731;
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; DOI=10.1172/JCI113497;
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;
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;
PubMed=2275556; DOI=10.1016/0003-9861(90)90666-M;
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;
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/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
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; DOI=10.1042/bj3120961;
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;
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.
TISSUE=Epidermis;
PubMed=16170054; DOI=10.1074/mcp.M500203-MCP200;
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).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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: Dimer of a heavy and a light chain linked by disulfide
bonds.
-!- SUBCELLULAR LOCATION: Lysosome.
-!- SIMILARITY: Belongs to the peptidase C1 family.
{ECO:0000255|PROSITE-ProRule:PRU10088, ECO:0000255|PROSITE-
ProRule:PRU10089, ECO:0000255|PROSITE-ProRule:PRU10090}.
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EMBL; X06086; CAA29470.1; -; mRNA.
EMBL; J02583; AAA37445.1; -; mRNA.
EMBL; M20495; AAA39984.1; -; Genomic_DNA.
EMBL; AF121837; AAD32136.1; -; mRNA.
EMBL; AF121838; AAD32137.1; -; mRNA.
EMBL; AF121839; AAD32138.1; -; mRNA.
EMBL; BC068163; AAH68163.1; -; mRNA.
EMBL; X04392; CAA27980.1; -; mRNA.
CCDS; CCDS26600.1; -.
PIR; S01177; KHMSL.
RefSeq; NP_034114.1; NM_009984.4.
RefSeq; XP_006517143.1; XM_006517080.1.
UniGene; Mm.471755; -.
UniGene; Mm.930; -.
PDB; 1MVV; Model; -; A=22-334.
PDBsum; 1MVV; -.
ProteinModelPortal; P06797; -.
SMR; P06797; -.
BioGrid; 198975; 2.
IntAct; P06797; 5.
MINT; MINT-1863740; -.
STRING; 10090.ENSMUSP00000021933; -.
BindingDB; P06797; -.
ChEMBL; CHEMBL5291; -.
MEROPS; C01.032; -.
iPTMnet; P06797; -.
PhosphoSitePlus; P06797; -.
SwissPalm; P06797; -.
UniCarbKB; P06797; -.
EPD; P06797; -.
PaxDb; P06797; -.
PeptideAtlas; P06797; -.
PRIDE; P06797; -.
Ensembl; ENSMUST00000021933; ENSMUSP00000021933; ENSMUSG00000021477.
Ensembl; ENSMUST00000222517; ENSMUSP00000152169; ENSMUSG00000021477.
GeneID; 13039; -.
KEGG; mmu:13039; -.
UCSC; uc007qyw.1; mouse.
CTD; 1514; -.
MGI; MGI:88564; Ctsl.
eggNOG; KOG1543; Eukaryota.
eggNOG; COG4870; LUCA.
GeneTree; ENSGT00900000140823; -.
HOGENOM; HOG000230774; -.
HOVERGEN; HBG011513; -.
InParanoid; P06797; -.
KO; K01365; -.
OMA; PKFDQNL; -.
OrthoDB; EOG091G0AKT; -.
PhylomeDB; P06797; -.
TreeFam; TF313739; -.
BioCyc; MetaCyc:MONOMER-14812; -.
BRENDA; 3.4.22.15; 3474.
Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases.
Reactome; R-MMU-2132295; MHC class II antigen presentation.
Reactome; R-MMU-8939242; RUNX1 regulates transcription of genes involved in differentiation of keratinocytes.
PRO; PR:P06797; -.
Proteomes; UP000000589; Chromosome 13.
Bgee; ENSMUSG00000021477; -.
CleanEx; MM_CTSL; -.
ExpressionAtlas; P06797; baseline and differential.
Genevisible; P06797; MM.
GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
GO; GO:0009897; C:external side of plasma membrane; ISS:BHF-UCL.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005615; C:extracellular space; IDA:MGI.
GO; GO:0005764; C:lysosome; IDA:MGI.
GO; GO:0005902; C:microvillus; ISS:BHF-UCL.
GO; GO:0043005; C:neuron projection; ISS:BHF-UCL.
GO; GO:0005730; C:nucleolus; IDA:BHF-UCL.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0043204; C:perikaryon; ISS:BHF-UCL.
GO; GO:0005773; C:vacuole; ISS:BHF-UCL.
GO; GO:0004177; F:aminopeptidase activity; ISS:BHF-UCL.
GO; GO:0016807; F:cysteine-type carboxypeptidase activity; IDA:MGI.
GO; GO:0004197; F:cysteine-type endopeptidase activity; ISS:BHF-UCL.
GO; GO:0042393; F:histone binding; IDA:BHF-UCL.
GO; GO:0042277; F:peptide binding; ISS:BHF-UCL.
GO; GO:0048102; P:autophagic cell death; ISS:BHF-UCL.
GO; GO:0007154; P:cell communication; ISS:BHF-UCL.
GO; GO:0009267; P:cellular response to starvation; ISS:BHF-UCL.
GO; GO:0046697; P:decidualization; IGI:MGI.
GO; GO:0031069; P:hair follicle morphogenesis; IMP:MGI.
GO; GO:0008584; P:male gonad development; ISS:BHF-UCL.
GO; GO:0010259; P:multicellular organism aging; ISS:BHF-UCL.
GO; GO:0010839; P:negative regulation of keratinocyte proliferation; IMP:MGI.
GO; GO:0021675; P:nerve development; ISS:BHF-UCL.
GO; GO:0016540; P:protein autoprocessing; IDA:MGI.
GO; GO:0016485; P:protein processing; IDA:MGI.
GO; GO:0006508; P:proteolysis; IDA:BHF-UCL.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IBA:GO_Central.
GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; IGI:MGI.
GO; GO:0051384; P:response to glucocorticoid; ISS:BHF-UCL.
GO; GO:0009749; P:response to glucose; ISS:BHF-UCL.
GO; GO:0034698; P:response to gonadotropin; ISS:BHF-UCL.
GO; GO:0014070; P:response to organic cyclic compound; ISS:BHF-UCL.
GO; GO:0060008; P:Sertoli cell differentiation; ISS:BHF-UCL.
GO; GO:0007283; P:spermatogenesis; ISS:BHF-UCL.
InterPro; IPR025661; Pept_asp_AS.
InterPro; IPR000169; Pept_cys_AS.
InterPro; IPR025660; Pept_his_AS.
InterPro; IPR013128; Peptidase_C1A.
InterPro; IPR000668; Peptidase_C1A_C.
InterPro; IPR013201; Prot_inhib_I29.
PANTHER; PTHR12411; PTHR12411; 1.
Pfam; PF08246; Inhibitor_I29; 1.
Pfam; PF00112; Peptidase_C1; 1.
PRINTS; PR00705; PAPAIN.
SMART; SM00848; Inhibitor_I29; 1.
SMART; SM00645; Pept_C1; 1.
PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Protease;
Reference proteome; Signal; Thiol protease; Zymogen.
SIGNAL 1 17 {ECO:0000269|PubMed:8554545}.
PROPEP 18 113 Activation peptide.
/FTId=PRO_0000026248.
CHAIN 114 288 Cathepsin L1 heavy chain.
/FTId=PRO_0000026249.
PROPEP 289 290
/FTId=PRO_0000026250.
CHAIN 291 334 Cathepsin L1 light chain.
/FTId=PRO_0000026251.
ACT_SITE 138 138 {ECO:0000250}.
ACT_SITE 276 276 {ECO:0000250}.
ACT_SITE 300 300 {ECO:0000250}.
CARBOHYD 221 221 N-linked (GlcNAc...) (high mannose)
asparagine. {ECO:0000269|PubMed:16170054,
ECO:0000269|PubMed:2275556}.
DISULFID 135 178 {ECO:0000250}.
DISULFID 169 211 {ECO:0000250}.
DISULFID 269 322 Interchain (between heavy and light
chains). {ECO:0000250}.
CONFLICT 58 58 M -> I (in Ref. 2; AAA39984/AAD32136/
AAD32137/AAD32138). {ECO:0000305}.
CONFLICT 177 177 G -> R (in Ref. 3). {ECO:0000305}.
SEQUENCE 334 AA; 37547 MW; FE6747043307AD98 CRC64;
MNLLLLLAVL CLGTALATPK FDQTFSAEWH QWKSTHRRLY GTNEEEWRRA IWEKNMRMIQ
LHNGEYSNGQ HGFSMEMNAF GDMTNEEFRQ VVNGYRHQKH KKGRLFQEPL MLKIPKSVDW
REKGCVTPVK NQGQCGSCWA FSASGCLEGQ MFLKTGKLIS LSEQNLVDCS HAQGNQGCNG
GLMDFAFQYI KENGGLDSEE SYPYEAKDGS CKYRAEFAVA NDTGFVDIPQ QEKALMKAVA
TVGPISVAMD ASHPSLQFYS SGIYYEPNCS SKNLDHGVLL VGYGYEGTDS NKNKYWLVKN
SWGSEWGMEG YIKIAKDRDN HCGLATAASY PVVN


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