Reviewed, UniProtKB/Swiss-Prot P07154 (CATL1_RAT)

Names and origin

Protein names

Recommended name:
    Cathepsin L1
    EC=3.4.22.15
Alternative name(s):
    Major excreted protein
      Short name=MEP
    Cyclic protein 2
      Short name=CP-2
Cleaved into the following 3 chains:
    1- Recommended name:
            Procathepsin L
    2- Recommended name:
            Cathepsin L1 heavy chain
    3- Recommended name:
            Cathepsin L1 light chain

Gene names

Name:	Ctsl1
Synonyms:	Ctsl

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

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. Procathepsin L is required for maximal stimulation of steroidogenesis by TIMP1. Ref.6
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. Ref.6 Procathepsin L: Secreted. Ref.6
Tissue specificity	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. Ref.4 Ref.7
Induction	Expression in Sertoli cells is repressed by germ cells. Ref.4
Sequence similarities	Belongs to the peptidase C1 family.

Ontologies

Keywords
Cellular component	Lysosome Secreted
Domain	Signal
Molecular function	Hydrolase Protease Thiol protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Inferred from expression pattern. Source: RGD
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-KW lysosome Inferred from direct assay. Source: RGD soluble fraction Inferred from direct assay. Source: RGD
Molecular function	aminopeptidase activity Inferred from direct assay. Source: RGD cysteine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro kininogen binding Inferred from physical interaction. Source: RGD peptide binding Inferred from direct assay. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 17	17	Ref.6 Ref.7
	Chain	18 – 334	317	Procathepsin L		PRO_0000304796
	Propeptide	18 – 113	96	Activation peptide Ref.8		PRO_0000026256
	Chain	114 – 288	175	Cathepsin L1 heavy chain		PRO_0000026257
	Propeptide	289 – 290	2			PRO_0000026258
	Chain	291 – 334	44	Cathepsin L1 light chain		PRO_0000026259
Sites
	Active site	138	1	By similarity
	Active site	276	1	By similarity
	Active site	300	1	By similarity
Amino acid modifications
	Glycosylation	221	1	N-linked (GlcNAc...)
	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	238	1	A → P in CAA68691. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P07154-1 [UniParc]. Last modified February 1, 1991. Version 2. Checksum: AFFA997582E34AF6	FASTA	334	37,660
	10 20 30 40 50 60 MTPLLLLAVL CLGTALATPK FDQTFNAQWH QWKSTHRRLY GTNEEEWRRA VWEKNMRMIQ 70 80 90 100 110 120 LHNGEYSNGK HGFTMEMNAF GDMTNEEFRQ IVNGYRHQKH KKGRLFQEPL MLQIPKTVDW 130 140 150 160 170 180 REKGCVTPVK NQGQCGSCWA FSASGCLEGQ MFLKTGKLIS LSEQNLVDCS HDQGNQGCNG 190 200 210 220 230 240 GLMDFAFQYI KENGGLDSEE SYPYEAKDGS CKYRAEYAVA NDTGFVDIPQ QEKALMKAVA 250 260 270 280 290 300 TVGPISVAMD ASHPSLQFYS SGIYYEPNCS SKDLDHGVLV VGYGYEGTDS NKDKYWLVKN 310 320 330 SWGKEWGMDG YIKIAKDRNN HCGLATAASY PIVN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and sequencing of cDNA for rat cathepsin L." Ishidoh K., Towatari T., Imajoh S., Kawasaki H., Kominami E., Katunuma N., Suzuki K. FEBS Lett. 223:69-73(1987) [PubMed: 3666143] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Wistar. Tissue: Kidney.
[2]	"Gene structure and 5'-upstream sequence of rat cathepsin L." Ishidoh K., Kominami E., Suzuki K., Katunuma N. FEBS Lett. 259:71-74(1989) [PubMed: 2599113] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Pituitary.
[4]	"Male germ cells regulate transcription of the cathepsin L gene by rat Sertoli cells." Zabludoff S.D., Charron M., DeCerbo J.N., Simukova N., Wright W.W. Endocrinology 142:2318-2327(2001) [PubMed: 11356678] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42, TISSUE SPECIFICITY, INDUCTION. Strain: Sprague-Dawley.
[5]	"Cyclic protein-2, a secretory product of rat Sertoli cells, is the proenzyme form of cathepsin L." Erickson-Lawrence M., Zabludoff S.D., Wright W.W. Mol. Endocrinol. 5:1789-1798(1991) [PubMed: 1791830] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 88-334. Tissue: Sertoli cell.
[6]	"Identification of a stimulator of steroid hormone synthesis isolated from testis." Boujrad N., Ogwuegbu S.O., Garnier M., Lee C.-H., Martin B.M., Papadopoulos V. Science 268:1609-1612(1995) [PubMed: 7777858] [Abstract] Cited for: PROTEIN SEQUENCE OF 18-37, FUNCTION, SUBCELLULAR LOCATION. Strain: Sprague-Dawley. Tissue: Sertoli cell.
[7]	"Precursor of rat epidermal cathepsin L: purification and immunohistochemical localization." Kawada A., Hara K., Kominami E., Tezuka T., Takahashi M., Takahara H. J. Dermatol. Sci. 23:36-45(2000) [PubMed: 10699763] [Abstract] Cited for: PROTEIN SEQUENCE OF 18-28, TISSUE SPECIFICITY. Strain: Sprague-Dawley. Tissue: Epidermis.
[8]	"Amino acid sequence of rat liver cathepsin L." Towatari T., Katunuma N. FEBS Lett. 236:57-61(1988) [PubMed: 3402618] [Abstract] Cited for: PROTEIN SEQUENCE OF 114-288 AND 291-334. Tissue: Liver.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Y00697 mRNA. Translation: CAA68691.1. AF025476 Genomic DNA. Translation: AAB81616.1. BC063175 mRNA. Translation: AAH63175.1. S85184 mRNA. Translation: AAB21516.1.
IPI	IPI00326070.
PIR	KHRTL. S07098.
RefSeq	NP_037288.1.
UniGene	Rn.1294
3D structure databases
HSSP	HSSP built from PDB template 1ICF based on UniProtKB P07711.
SMR	P07154. Positions 21-333.
ModBase	Search...
Protein family/group databases
MEROPS	C01.032.
Proteomic databases
PRIDE	P07154.
Genome annotation databases
Ensembl	ENSRNOG00000018566. Rattus norvegicus. [Contig view]
GeneID	25697.
KEGG	rno:25697.
Organism-specific databases
RGD	2448. Ctsl.
Phylogenomic databases
HOVERGEN	P07154.
OMA	P07154. YGFEGAN.
Enzyme and pathway databases
BRENDA	3.4.22.15. 248.
Gene expression databases
ArrayExpress	P07154.
GermOnline	ENSRNOG00000018566. Rattus norvegicus.
Family and domain databases
InterPro	IPR000169. Pept_cys_AS. IPR013128. Peptidase_C1A. IPR000668. Peptidase_C1A_C. IPR013201. Prot_inhib_I29. [Graphical view]
PANTHER	PTHR12411. Peptidase_C1A. 1 hit.
Pfam	PF08246. Inhibitor_I29. 1 hit. PF00112. Peptidase_C1. 1 hit. [Graphical view]
PRINTS	PR00705. PAPAIN.
ProDom	PD000158. Peptidase_C1. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	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 Resources
NextBio	607715.

Entry information

Entry name

CATL1_RAT

Accession

Primary (citable) accession number: P07154
Secondary accession number(s): Q9QV07

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	February 1, 1991
Last modified:	June 16, 2009
This is version 93 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)