[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Wistar; TISSUE=Kidney; DOI=10.1016/0014-5793(87)80511-2; PubMed=3666143 [NCBI, ExPASy, EBI, Israel, Japan] Ishidoh K., Towatari T., Imajoh S., Kawasaki H., Kominami E., Katunuma N., Suzuki K.; "Molecular cloning and sequencing of cDNA for rat cathepsin L."; FEBS Lett. 223:69-73(1987).
[2]	NUCLEOTIDE SEQUENCE. DOI=10.1016/0014-5793(89)81497-8; PubMed=2599113 [NCBI, ExPASy, EBI, Israel, Japan] Ishidoh K., Kominami E., Suzuki K., Katunuma N.; "Gene structure and 5'-upstream sequence of rat cathepsin L."; FEBS Lett. 259:71-74(1989).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Pituitary; 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).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42, TISSUE SPECIFICITY, AND INDUCTION. STRAIN=Sprague-Dawley; DOI=10.1210/en.142.6.2318; PubMed=11356678 [NCBI, ExPASy, EBI, Israel, Japan] Zabludoff S.D., Charron M., DeCerbo J.N., Simukova N., Wright W.W.; "Male germ cells regulate transcription of the cathepsin L gene by rat Sertoli cells."; Endocrinology 142:2318-2327(2001).
[5]	NUCLEOTIDE SEQUENCE [MRNA] OF 88-334. TISSUE=Sertoli cell; PubMed=1791830 [NCBI, ExPASy, EBI, Israel, Japan] Erickson-Lawrence M., Zabludoff S.D., Wright W.W.; "Cyclic protein-2, a secretory product of rat Sertoli cells, is the proenzyme form of cathepsin L."; Mol. Endocrinol. 5:1789-1798(1991).
[6]	PROTEIN SEQUENCE OF 18-37, FUNCTION, AND SUBCELLULAR LOCATION. STRAIN=Sprague-Dawley; TISSUE=Sertoli cell; PubMed=7777858 [NCBI, ExPASy, EBI, Israel, Japan] Boujrad N., Ogwuegbu S.O., Garnier M., Lee C.-H., Martin B.M., Papadopoulos V.; "Identification of a stimulator of steroid hormone synthesis isolated from testis."; Science 268:1609-1612(1995).
[7]	PROTEIN SEQUENCE OF 18-28, AND TISSUE SPECIFICITY. STRAIN=Sprague-Dawley; TISSUE=Epidermis; DOI=10.1016/S0923-1811(99)00063-8; PubMed=10699763 [NCBI, ExPASy, EBI, Israel, Japan] Kawada A., Hara K., Kominami E., Tezuka T., Takahashi M., Takahara H.; "Precursor of rat epidermal cathepsin L: purification and immunohistochemical localization."; J. Dermatol. Sci. 23:36-45(2000).
[8]	PROTEIN SEQUENCE OF 114-288 AND 291-334. TISSUE=Liver; DOI=10.1016/0014-5793(88)80285-0; PubMed=3402618 [NCBI, ExPASy, EBI, Israel, Japan] Towatari T., Katunuma N.; "Amino acid sequence of rat liver cathepsin L."; FEBS Lett. 236:57-61(1988).

Comments

FUNCTION: Important for the overall degradation of proteins in lysosomes. Procathepsin L is required for maximal stimulation of steroidogenesis by TIMP1.
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.
SUBCELLULAR LOCATION: Procathepsin L: Secreted.
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.
INDUCTION: Expression in Sertoli cells is repressed by germ cells.
SIMILARITY: Belongs to the peptidase C1 family [view classification].

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

Y00697; CAA68691.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF025476; AAB81616.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC063175; AAH63175.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S85184; AAB21516.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S07098; KHRTL.

NP_037288.1; -.

3D structure databases

HSSP

P07711; 1ICF. [HSSP ENTRY / PDB]

SMR

P07154; 21-333.

ModBase

P07154.

Protein family/group databases

MEROPS

C01.032; -.
I29.010; -.

Organism-specific databases

RGD

2448; Ctsl.

Gene expression databases

ArrayExpress

P07154; -.

GermOnline

ENSRNOG00000018566; Rattus norvegicus.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0005764;	Cellular component: lysosome (inferred from electronic annotation from UniProtKB-KW).
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.

Genome annotation databases

Ensembl

ENSRNOG00000018566; Rattus norvegicus. [Contig view]

GeneID

25697; -.

KEGG

rno:25697; -.

Phylogenomic databases

HOVERGEN

P07154; -.

Other

NextBio

607715; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; Glycoprotein; Hydrolase; Lysosome; Protease; Secreted; Signal; Thiol protease; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 17`	`17`
`CHAIN`	`18 334`	`317`	`Procathepsin L.`	`PRO_0000304796`
`PROPEP`	`18 113`	`96`	`Activation peptide.`	`PRO_0000026256`
`CHAIN`	`114 288`	`175`	`Cathepsin L1 heavy chain.`	`PRO_0000026257`
`PROPEP`	`289 290`	`2`		`PRO_0000026258`
`CHAIN`	`291 334`	`44`	`Cathepsin L1 light chain.`	`PRO_0000026259`
`ACT_SITE`	`138 138`		`By similarity.`
`ACT_SITE`	`276 276`		`By similarity.`
`ACT_SITE`	`300 300`		`By similarity.`
`CARBOHYD`	`221 221`		`N-linked (GlcNAc...).`
`DISULFID`	`135 178`		`By similarity.`
`DISULFID`	`169 211`		`By similarity.`
`DISULFID`	`269 322`		`Interchain (between heavy and light chains) (By similarity).`
`CONFLICT`	`238 238`		`A -> P (in Ref. 1; CAA68691).`

Sequence information

Length: 334 AA [This is the length of the unprocessed precursor]

Molecular weight: 37660 Da [This is the MW of the unprocessed precursor]

CRC64: AFFA997582E34AF6 [This is a checksum on the sequence]

        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

P07154 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools