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Protein

Cathepsin L1

Gene

Ctsl

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Important for the overall degradation of proteins in lysosomes. Procathepsin L is required for maximal stimulation of steroidogenesis by TIMP1.1 Publication

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

  • aminopeptidase activity Source: RGD
  • cysteine-type carboxypeptidase activity Source: Ensembl
  • cysteine-type endopeptidase activity Source: RGD
  • kininogen binding Source: RGD
  • peptide binding Source: RGD
  • protein complex binding Source: RGD

GO - Biological processi

  • autophagic cell death Source: RGD
  • cell communication Source: RGD
  • cellular response to starvation Source: RGD
  • decidualization Source: RGD
  • hair follicle morphogenesis Source: Ensembl
  • male gonad development Source: RGD
  • multicellular organism aging Source: RGD
  • negative regulation of keratinocyte proliferation Source: Ensembl
  • nerve development Source: RGD
  • protein autoprocessing Source: Ensembl
  • proteolysis Source: RGD
  • proteolysis involved in cellular protein catabolic process Source: GO_Central
  • regulation of actin cytoskeleton reorganization Source: Ensembl
  • response to glucocorticoid Source: RGD
  • response to glucose Source: RGD
  • response to gonadotropin Source: RGD
  • response to organic cyclic compound Source: RGD
  • Sertoli cell differentiation Source: RGD
  • spermatogenesis Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Enzyme and pathway databases

BRENDAi3.4.22.15. 5301.
ReactomeiR-RNO-1474228. Degradation of the extracellular matrix.
R-RNO-1592389. Activation of Matrix Metalloproteinases.
R-RNO-2022090. Assembly of collagen fibrils and other multimeric structures.
R-RNO-2132295. MHC class II antigen presentation.
SABIO-RKP07154.

Protein family/group databases

MEROPSiC01.032.

Names & Taxonomyi

Protein namesi
Recommended name:
Cathepsin L1 (EC:3.4.22.15)
Alternative name(s):
Cathepsin L
Cyclic protein 2
Short name:
CP-2
Major excreted protein
Short name:
MEP
Cleaved into the following 3 chains:
Gene namesi
Name:Ctsl
Synonyms:Ctsl1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 17

Organism-specific databases

RGDi2448. Ctsl.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: RGD
  • cytoplasmic vesicle Source: Ensembl
  • external side of plasma membrane Source: RGD
  • extracellular exosome Source: Ensembl
  • extracellular space Source: GO_Central
  • lysosome Source: RGD
  • microvillus Source: RGD
  • neuron projection Source: RGD
  • nucleolus Source: Ensembl
  • perikaryon Source: RGD
  • vacuole Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Lysosome, Secreted

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2305.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 17173 PublicationsAdd
BLAST
Chaini18 – 334317Procathepsin LPRO_0000304796Add
BLAST
Propeptidei18 – 11396Activation peptide1 PublicationPRO_0000026256Add
BLAST
Chaini114 – 288175Cathepsin L1 heavy chainPRO_0000026257Add
BLAST
Propeptidei289 – 29021 PublicationPRO_0000026258
Chaini291 – 33444Cathepsin L1 light chainPRO_0000026259Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP07154.
PRIDEiP07154.

PTM databases

PhosphoSiteiP07154.

Expressioni

Tissue specificityi

Both mature cathepsin L1 and procathepsin L are found in the upper epidermis. The lower epidermis predominantly contains procathepsin L. In seminiferous tubules expression is greater at stages VI-VII than at stages IX-XII.2 Publications

Inductioni

Expression in Sertoli cells is repressed by germ cells.1 Publication

Gene expression databases

BgeeiENSRNOG00000018566.
ExpressionAtlasiP07154. baseline and differential.
GenevisibleiP07154. RN.

Interactioni

Subunit structurei

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

GO - Molecular functioni

  • kininogen binding Source: RGD
  • protein complex binding Source: RGD

Protein-protein interaction databases

BioGridi247726. 1 interaction.
IntActiP07154. 1 interaction.
STRINGi10116.ENSRNOP00000025462.

Chemistry

BindingDBiP07154.

Structurei

3D structure databases

ProteinModelPortaliP07154.
SMRiP07154. Positions 21-333.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1543. Eukaryota.
COG4870. LUCA.
GeneTreeiENSGT00760000118871.
HOGENOMiHOG000230774.
HOVERGENiHBG011513.
InParanoidiP07154.
KOiK01365.
OMAiNGEYSNG.
OrthoDBiEOG091G0AKT.
PhylomeDBiP07154.
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.

P07154-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTPLLLLAVL CLGTALATPK FDQTFNAQWH QWKSTHRRLY GTNEEEWRRA
60 70 80 90 100
VWEKNMRMIQ LHNGEYSNGK HGFTMEMNAF GDMTNEEFRQ IVNGYRHQKH
110 120 130 140 150
KKGRLFQEPL MLQIPKTVDW REKGCVTPVK NQGQCGSCWA FSASGCLEGQ
160 170 180 190 200
MFLKTGKLIS LSEQNLVDCS HDQGNQGCNG GLMDFAFQYI KENGGLDSEE
210 220 230 240 250
SYPYEAKDGS CKYRAEYAVA NDTGFVDIPQ QEKALMKAVA TVGPISVAMD
260 270 280 290 300
ASHPSLQFYS SGIYYEPNCS SKDLDHGVLV VGYGYEGTDS NKDKYWLVKN
310 320 330
SWGKEWGMDG YIKIAKDRNN HCGLATAASY PIVN
Length:334
Mass (Da):37,660
Last modified:February 1, 1991 - v2
Checksum:iAFFA997582E34AF6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti238 – 2381A → P in CAA68691 (PubMed:3666143).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00697 mRNA. Translation: CAA68691.1.
AF025476 Genomic DNA. Translation: AAB81616.1.
BC063175 mRNA. Translation: AAH63175.1.
S85184 mRNA. Translation: AAB21516.1.
PIRiS07098. KHRTL.
RefSeqiNP_037288.1. NM_013156.2.
UniGeneiRn.1294.

Genome annotation databases

EnsembliENSRNOT00000025462; ENSRNOP00000025462; ENSRNOG00000018566.
GeneIDi25697.
KEGGirno:25697.
UCSCiRGD:2448. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00697 mRNA. Translation: CAA68691.1.
AF025476 Genomic DNA. Translation: AAB81616.1.
BC063175 mRNA. Translation: AAH63175.1.
S85184 mRNA. Translation: AAB21516.1.
PIRiS07098. KHRTL.
RefSeqiNP_037288.1. NM_013156.2.
UniGeneiRn.1294.

3D structure databases

ProteinModelPortaliP07154.
SMRiP07154. Positions 21-333.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247726. 1 interaction.
IntActiP07154. 1 interaction.
STRINGi10116.ENSRNOP00000025462.

Chemistry

BindingDBiP07154.
ChEMBLiCHEMBL2305.

Protein family/group databases

MEROPSiC01.032.

PTM databases

PhosphoSiteiP07154.

Proteomic databases

PaxDbiP07154.
PRIDEiP07154.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000025462; ENSRNOP00000025462; ENSRNOG00000018566.
GeneIDi25697.
KEGGirno:25697.
UCSCiRGD:2448. rat.

Organism-specific databases

CTDi1514.
RGDi2448. Ctsl.

Phylogenomic databases

eggNOGiKOG1543. Eukaryota.
COG4870. LUCA.
GeneTreeiENSGT00760000118871.
HOGENOMiHOG000230774.
HOVERGENiHBG011513.
InParanoidiP07154.
KOiK01365.
OMAiNGEYSNG.
OrthoDBiEOG091G0AKT.
PhylomeDBiP07154.
TreeFamiTF313739.

Enzyme and pathway databases

BRENDAi3.4.22.15. 5301.
ReactomeiR-RNO-1474228. Degradation of the extracellular matrix.
R-RNO-1592389. Activation of Matrix Metalloproteinases.
R-RNO-2022090. Assembly of collagen fibrils and other multimeric structures.
R-RNO-2132295. MHC class II antigen presentation.
SABIO-RKP07154.

Miscellaneous databases

PROiP07154.

Gene expression databases

BgeeiENSRNOG00000018566.
ExpressionAtlasiP07154. baseline and differential.
GenevisibleiP07154. RN.

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]
ProtoNetiSearch...

Entry informationi

Entry nameiCATL1_RAT
AccessioniPrimary (citable) accession number: P07154
Secondary accession number(s): Q9QV07
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: February 1, 1991
Last modified: September 7, 2016
This is version 152 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.