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Cathepsin L1 (EC 3.4.22.15) (Cathepsin L) (Cyclic protein 2) (CP-2) (Major excreted protein) (MEP) [Cleaved into: Procathepsin L; Cathepsin L1 heavy chain; Cathepsin L1 light chain]

 CATL1_RAT               Reviewed;         334 AA.
P07154; Q9QV07;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 2.
25-APR-2018, entry version 167.
RecName: Full=Cathepsin L1;
EC=3.4.22.15;
AltName: Full=Cathepsin L;
AltName: Full=Cyclic protein 2;
Short=CP-2;
AltName: Full=Major excreted protein;
Short=MEP;
Contains:
RecName: Full=Procathepsin L;
Contains:
RecName: Full=Cathepsin L1 heavy chain;
Contains:
RecName: Full=Cathepsin L1 light chain;
Flags: Precursor;
Name=Ctsl; Synonyms=Ctsl1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Wistar; TISSUE=Kidney;
PubMed=3666143; DOI=10.1016/0014-5793(87)80511-2;
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.
PubMed=2599113; DOI=10.1016/0014-5793(89)81497-8;
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;
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).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42, TISSUE SPECIFICITY, AND
INDUCTION.
STRAIN=Sprague-Dawley;
PubMed=11356678; DOI=10.1210/endo.142.6.8106;
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; DOI=10.1210/mend-5-12-1789;
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; DOI=10.1126/science.7777858;
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;
PubMed=10699763; DOI=10.1016/S0923-1811(99)00063-8;
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;
PubMed=3402618; DOI=10.1016/0014-5793(88)80285-0;
Towatari T., Katunuma N.;
"Amino acid sequence of rat liver cathepsin L.";
FEBS Lett. 236:57-61(1988).
[9]
CLEAVAGE OF SIGNAL PEPTIDE AFTER ALA-17, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=26479776; DOI=10.1021/acs.jproteome.5b00820;
Tsuchiya T., Osaki T., Minamino N., Sasaki K.;
"Peptidomics for studying limited proteolysis.";
J. Proteome Res. 14:4921-4931(2015).
-!- FUNCTION: Important for the overall degradation of proteins in
lysosomes. Procathepsin L is required for maximal stimulation of
steroidogenesis by TIMP1. {ECO:0000269|PubMed:7777858}.
-!- 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 {ECO:0000269|PubMed:7777858}.
-!- 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.
{ECO:0000269|PubMed:10699763, ECO:0000269|PubMed:11356678}.
-!- INDUCTION: Expression in Sertoli cells is repressed by germ cells.
{ECO:0000269|PubMed:11356678}.
-!- 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; Y00697; CAA68691.1; -; mRNA.
EMBL; AF025476; AAB81616.1; -; Genomic_DNA.
EMBL; BC063175; AAH63175.1; -; mRNA.
EMBL; S85184; AAB21516.1; -; mRNA.
PIR; S07098; KHRTL.
RefSeq; NP_037288.1; NM_013156.2.
UniGene; Rn.1294; -.
ProteinModelPortal; P07154; -.
SMR; P07154; -.
BioGrid; 247726; 1.
IntAct; P07154; 1.
STRING; 10116.ENSRNOP00000025462; -.
BindingDB; P07154; -.
ChEMBL; CHEMBL2305; -.
MEROPS; C01.032; -.
PhosphoSitePlus; P07154; -.
PaxDb; P07154; -.
PRIDE; P07154; -.
Ensembl; ENSRNOT00000025462; ENSRNOP00000025462; ENSRNOG00000018566.
GeneID; 25697; -.
KEGG; rno:25697; -.
UCSC; RGD:2448; rat.
CTD; 1514; -.
RGD; 2448; Ctsl.
eggNOG; KOG1543; Eukaryota.
eggNOG; COG4870; LUCA.
GeneTree; ENSGT00900000140823; -.
HOGENOM; HOG000230774; -.
HOVERGEN; HBG011513; -.
InParanoid; P07154; -.
KO; K01365; -.
OMA; PKFDQNL; -.
OrthoDB; EOG091G0AKT; -.
PhylomeDB; P07154; -.
TreeFam; TF313739; -.
BRENDA; 3.4.22.15; 5301.
Reactome; R-RNO-1474228; Degradation of the extracellular matrix.
Reactome; R-RNO-1592389; Activation of Matrix Metalloproteinases.
Reactome; R-RNO-1679131; Trafficking and processing of endosomal TLR.
Reactome; R-RNO-2022090; Assembly of collagen fibrils and other multimeric structures.
Reactome; R-RNO-2132295; MHC class II antigen presentation.
Reactome; R-RNO-8939242; RUNX1 regulates transcription of genes involved in differentiation of keratinocytes.
SABIO-RK; P07154; -.
PRO; PR:P07154; -.
Proteomes; UP000002494; Chromosome 17.
Bgee; ENSRNOG00000018566; -.
ExpressionAtlas; P07154; baseline and differential.
Genevisible; P07154; RN.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
GO; GO:0009897; C:external side of plasma membrane; IDA:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005615; C:extracellular space; ISO:RGD.
GO; GO:0005764; C:lysosome; IDA:RGD.
GO; GO:0005902; C:microvillus; IDA:RGD.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0005730; C:nucleolus; ISO:RGD.
GO; GO:0005634; C:nucleus; ISO:RGD.
GO; GO:0043204; C:perikaryon; IDA:RGD.
GO; GO:0005773; C:vacuole; IDA:RGD.
GO; GO:0004177; F:aminopeptidase activity; IDA:RGD.
GO; GO:0005518; F:collagen binding; ISO:RGD.
GO; GO:0016807; F:cysteine-type carboxypeptidase activity; ISO:RGD.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:CAFA.
GO; GO:0008234; F:cysteine-type peptidase activity; ISO:RGD.
GO; GO:0001968; F:fibronectin binding; ISO:RGD.
GO; GO:0042393; F:histone binding; ISO:RGD.
GO; GO:0030984; F:kininogen binding; IPI:RGD.
GO; GO:0042277; F:peptide binding; IDA:RGD.
GO; GO:0043394; F:proteoglycan binding; ISO:RGD.
GO; GO:0097655; F:serpin family protein binding; ISO:RGD.
GO; GO:0002250; P:adaptive immune response; ISO:RGD.
GO; GO:0048102; P:autophagic cell death; IEP:RGD.
GO; GO:0007154; P:cell communication; IDA:RGD.
GO; GO:0009267; P:cellular response to starvation; IEP:RGD.
GO; GO:0097067; P:cellular response to thyroid hormone stimulus; ISO:RGD.
GO; GO:0030574; P:collagen catabolic process; ISO:RGD.
GO; GO:0046697; P:decidualization; IEP:RGD.
GO; GO:0031069; P:hair follicle morphogenesis; ISO:RGD.
GO; GO:0008584; P:male gonad development; IEP:RGD.
GO; GO:0010259; P:multicellular organism aging; IEP:RGD.
GO; GO:0010839; P:negative regulation of keratinocyte proliferation; ISO:RGD.
GO; GO:0021675; P:nerve development; IEP:RGD.
GO; GO:0016540; P:protein autoprocessing; ISO:RGD.
GO; GO:0016485; P:protein processing; ISO:RGD.
GO; GO:0006508; P:proteolysis; IDA:CAFA.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; ISO:RGD.
GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; ISO:RGD.
GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
GO; GO:0009749; P:response to glucose; IEP:RGD.
GO; GO:0034698; P:response to gonadotropin; IEP:RGD.
GO; GO:1990834; P:response to odorant; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0060008; P:Sertoli cell differentiation; IEP:RGD.
GO; GO:0007283; P:spermatogenesis; IEP:RGD.
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;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Hydrolase; Lysosome; Protease; Reference proteome;
Secreted; Signal; Thiol protease; Zymogen.
SIGNAL 1 17 {ECO:0000269|PubMed:10699763,
ECO:0000269|PubMed:26479776,
ECO:0000269|PubMed:7777858}.
CHAIN 18 334 Procathepsin L.
/FTId=PRO_0000304796.
PROPEP 18 113 Activation peptide.
{ECO:0000269|PubMed:3402618}.
/FTId=PRO_0000026256.
CHAIN 114 288 Cathepsin L1 heavy chain.
/FTId=PRO_0000026257.
PROPEP 289 290 {ECO:0000269|PubMed:3402618}.
/FTId=PRO_0000026258.
CHAIN 291 334 Cathepsin L1 light chain.
/FTId=PRO_0000026259.
ACT_SITE 138 138 {ECO:0000250}.
ACT_SITE 276 276 {ECO:0000250}.
ACT_SITE 300 300 {ECO:0000250}.
CARBOHYD 221 221 N-linked (GlcNAc...) asparagine.
DISULFID 135 178 {ECO:0000250}.
DISULFID 169 211 {ECO:0000250}.
DISULFID 269 322 Interchain (between heavy and light
chains). {ECO:0000250}.
CONFLICT 238 238 A -> P (in Ref. 1; CAA68691).
{ECO:0000305}.
SEQUENCE 334 AA; 37660 MW; AFFA997582E34AF6 CRC64;
MTPLLLLAVL CLGTALATPK FDQTFNAQWH QWKSTHRRLY GTNEEEWRRA VWEKNMRMIQ
LHNGEYSNGK HGFTMEMNAF GDMTNEEFRQ IVNGYRHQKH KKGRLFQEPL MLQIPKTVDW
REKGCVTPVK NQGQCGSCWA FSASGCLEGQ MFLKTGKLIS LSEQNLVDCS HDQGNQGCNG
GLMDFAFQYI KENGGLDSEE SYPYEAKDGS CKYRAEYAVA NDTGFVDIPQ QEKALMKAVA
TVGPISVAMD ASHPSLQFYS SGIYYEPNCS SKDLDHGVLV VGYGYEGTDS NKDKYWLVKN
SWGKEWGMDG YIKIAKDRNN HCGLATAASY PIVN


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