Cathepsin L1

CTSL
Available structures
PDB	Human UniProt search: PDBe RCSB
List of PDB id codes
	1CJL, 1CS8, 1ICF, 1MHW, 2NQD, 2VHS, 2XU1, 2XU3, 2XU4, 2XU5, 2YJ2, 2YJ8, 2YJ9, 2YJB, 2YJC, 3BC3, 3H89, 3H8B, 3H8C, 3HHA, 3HWN, 3IV2, 3K24, 3KSE, 3OF8, 3OF9, 4AXL, 4AXM, 5F02, 5I4H
Identifiers
Aliases	CTSL, CATL, CTSL1, MEP, cathepsin L
External IDs	OMIM: 116880; HomoloGene: 129366; GeneCards: CTSL; OMA:CTSL - orthologs
Gene location (Human)
Chr.	Chromosome 9 (human)
End	87,731,469 bp
RNA expression pattern
	Top expressed in
	stromal cell of endometrium; ; decidua; ; islet of Langerhans; ; pericardium; ; gallbladder; ; upper lobe of left lung; ; left uterine tube; ; renal medulla; ; muscle layer of sigmoid colon; ; gastric mucosa;
	n/a
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	fibronectin binding; cysteine-type peptidase activity; collagen binding; histone binding; serpin family protein binding; peptidase activity; protein binding; cysteine-type endopeptidase activity; hydrolase activity; proteoglycan binding; serine-type endopeptidase activity;
Cellular component	extracellular region; endolysosome lumen; lysosomal lumen; lysosome; extracellular exosome; nucleus; extracellular space; collagen-containing extracellular matrix; multivesicular body; plasma membrane;
Biological process	macrophage apoptotic process; antigen processing and presentation; adaptive immune response; antigen processing and presentation of exogenous peptide antigen via MHC class II; extracellular matrix disassembly; proteolysis; toll-like receptor signaling pathway; cellular response to thyroid hormone stimulus; collagen catabolic process; proteolysis involved in cellular protein catabolic process; regulation of keratinocyte differentiation;
	Sources:Amigo / QuickGO
Orthologs
	1514
	n/a
	ENSG00000135047
	n/a
	P07711; Q9HBQ7
	n/a
NM_001257971; NM_001257972; NM_001257973; NM_001912; NM_145918;
	NM_001382757; NM_001382758; NM_001382766; NM_001382767; NM_001382768
	n/a
NP_001244900; NP_001244901; NP_001244902; NP_001903; NP_666023;
	NP_001369686; NP_001369687; NP_001369695; NP_001369696; NP_001369697; NP_001244902.1
	n/a
	Wikidata
View/Edit Human

Cathepsin L1 is a protein that in humans is encoded by the CTSL1 gene.^[3]^[4]^[5] The protein is a cysteine cathepsin, a lysosomal cysteine protease that plays a major role in intracellular protein catabolism.^[6]^[7]^[8]^[9]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000135047 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Chauhan SS, Popescu NC, Ray D, Fleischmann R, Gottesman MM, Troen BR (Feb 1993). "Cloning, genomic organization, and chromosomal localization of human cathepsin L". J Biol Chem. 268 (2): 1039–45. doi:10.1016/S0021-9258(18)54038-2. PMID 8419312.
^ Joseph LJ, Chang LC, Stamenkovich D, Sukhatme VP (Jun 1988). "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 (5): 1621–9. doi:10.1172/JCI113497. PMC 442598. PMID 2835398.
^ "Entrez Gene: CTSL1 cathepsin L1".
^ Barrett AJ, Kirschke H (1981). "Cathepsin B, cathepsin H, and cathepsin L". Proteolytic Enzymes, Part C. Methods in Enzymology. Vol. 80 Pt C. pp. 535–561. doi:10.1016/s0076-6879(81)80043-2. ISBN 9780121819804. PMID 7043200.
^ Barrett AJ, Buttle DJ, Mason RW (1988). "Lysosomal cysteine proteinases". ISI Atlas of Science. Biochemistry. 1: 256–260.
^ Joseph LJ, Chang LC, Stamenkovich D, Sukhatme VP (May 1988). "Complete nucleotide and deduced amino acid sequences of human and murine preprocathepsin L. An abundant transcript induced by transformation of fibroblasts". The Journal of Clinical Investigation. 81 (5): 1621–1629. doi:10.1172/JCI113497. PMC 442598. PMID 2835398.
^ Kirschke H, Wikstrom P, Shaw E (February 1988). "Active center differences between cathepsins L and B: the S1 binding region". FEBS Letters. 228 (1): 128–130. Bibcode:1988FEBSL.228..128K. doi:10.1016/0014-5793(88)80600-8. PMID 3342870.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000135047 – Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid8419312-3] Chauhan SS, Popescu NC, Ray D, Fleischmann R, Gottesman MM, Troen BR (Feb 1993). "Cloning, genomic organization, and chromosomal localization of human cathepsin L". J Biol Chem. 268 (2): 1039–45. doi:10.1016/S0021-9258(18)54038-2. PMID 8419312.

[pmid2835398-4] Joseph LJ, Chang LC, Stamenkovich D, Sukhatme VP (Jun 1988). "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 (5): 1621–9. doi:10.1172/JCI113497. PMC 442598. PMID 2835398.

[entrez-5] "Entrez Gene: CTSL1 cathepsin L1".

[6] Barrett AJ, Kirschke H (1981). "Cathepsin B, cathepsin H, and cathepsin L". Proteolytic Enzymes, Part C. Methods in Enzymology. Vol. 80 Pt C. pp. 535–561. doi:10.1016/s0076-6879(81)80043-2. ISBN 9780121819804. PMID 7043200.

[7] Barrett AJ, Buttle DJ, Mason RW (1988). "Lysosomal cysteine proteinases". ISI Atlas of Science. Biochemistry. 1: 256–260.

[8] Joseph LJ, Chang LC, Stamenkovich D, Sukhatme VP (May 1988). "Complete nucleotide and deduced amino acid sequences of human and murine preprocathepsin L. An abundant transcript induced by transformation of fibroblasts". The Journal of Clinical Investigation. 81 (5): 1621–1629. doi:10.1172/JCI113497. PMC 442598. PMID 2835398.

[9] Kirschke H, Wikstrom P, Shaw E (February 1988). "Active center differences between cathepsins L and B: the S1 binding region". FEBS Letters. 228 (1): 128–130. Bibcode:1988FEBSL.228..128K. doi:10.1016/0014-5793(88)80600-8. PMID 3342870.

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