CTSF

Protein identityUniProt · HPA

UniProt accession

Q9UBX1

Gene

CTSF

Ensembl

ENSG00000174080

Chromosome

11

Canonical length

484 aa

Protein class

Disease related genes, Enzymes, Human disease related genes, Metabolic proteins, Plasma proteins, Potential drug targets, Predicted intracellular proteins

Subcellular location

Endoplasmic reticulum,Vesicles,Plasma membrane

Secretome location

Intracellular and membrane

OverviewNCBI Gene

Cathepsins are papain family cysteine proteinases that represent a major component of the lysosomal proteolytic system. Cathepsins generally contain a signal sequence, followed by a propeptide and then a catalytically active mature region. The very long (251 amino acid residues) proregion of the cathepsin F precursor contains a C-terminal domain similar to the pro-segment of cathepsin L-like enzymes, a 50-residue flexible linker peptide, and an N-terminal domain predicted to adopt a cystatin-like fold. The cathepsin F proregion is unique within the papain family cysteine proteases in that it contains this additional N-terminal segment predicted to share structural similarities with cysteine protease inhibitors of the cystatin superfamily. This cystatin-like domain contains some of the elements known to be important for inhibitory activity. CTSF encodes a predicted protein of 484 amino acids which contains a 19 residue signal peptide. Cathepsin F contains five potential N-glycosylation sites, and it may be targeted to the endosomal/lysosomal compartment via the mannose 6-phosphate receptor pathway. The cathepsin F gene is ubiquitously expressed, and it maps to chromosome 11q13, close to the gene encoding cathepsin W. [provided by RefSeq, Jul 2008]

Canonical amino-acid sequenceUniProt

484 residues, UniProt reviewed canonical sequence.

>Q9UBX1|CTSF
     1  MAPWLQLLSL LGLLPGAVAA PAQPRAASFQ AWGPPSPELL APTRFALEMF NRGRAAGTRA
    61  VLGLVRGRVR RAGQGSLYSL EATLEEPPCN DPMVCRLPVS KKTLLCSFQV LDELGRHVLL
   121  RKDCGPVDTK VPGAGEPKSA FTQGSAMISS LSQNHPDNRN ETFSSVISLL NEDPLSQDLP
   181  VKMASIFKNF VITYNRTYES KEEARWRLSV FVNNMVRAQK IQALDRGTAQ YGVTKFSDLT
   241  EEEFRTIYLN TLLRKEPGNK MKQAKSVGDL APPEWDWRSK GAVTKVKDQG MCGSCWAFSV
   301  TGNVEGQWFL NQGTLLSLSE QELLDCDKMD KACMGGLPSN AYSAIKNLGG LETEDDYSYQ
   361  GHMQSCNFSA EKAKVYINDS VELSQNEQKL AAWLAKRGPI SVAINAFGMQ FYRHGISRPL
   421  RPLCSPWLID HAVLLVGYGN RSDVPFWAIK NSWGTDWGEK GYYYLHRGSG ACGVNTMASS
   481  AVVD

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against CTSF can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability

Intracellular

Secreted

No

Transmembrane segments

0

Mean surface accessibility (rSASA)

0.31

Highest tissue expression

124 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about CTSF.

Disease | AllUniProt

Conditions CTSF is implicated in, by any mechanism.

• Ceroid lipofuscinosis, neuronal, 13 (Kufs type) (CLN13) MIM:615362

Disease | GeneticClinVar

37 pathogenic / likely-pathogenic of 321 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

• Neuronal ceroid lipofuscinosis 13
• Neuronal ceroid lipofuscinosis
• Inborn genetic diseases
• Neurodevelopmental disorder
• See cases

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)

1.2

gnomAD pLI

0

gnomAD missense Z

0.74

DepMap mean gene effect

-0.12

DepMap dependency class

selective

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 5% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• antigen processing and presentation of exogenous peptide antigen via MHC class II
• proteolysis
• proteolysis involved in protein catabolic process

Molecular functions

• cysteine-type endopeptidase activity
• cysteine-type peptidase activity

Cellular components

• endoplasmic reticulum
• extracellular exosome
• extracellular matrix
• extracellular space
• extracellular vesicle
• lysosomal lumen
• lysosome
• plasma membrane

Protein domainsUniProt · Pfam · InterPro

• Cysteine peptidase, cysteine active site
• Peptidase C1A, papain C-terminal
• Peptidase C1A
• Cathepsin propeptide inhibitor domain (I29)
• Cysteine peptidase, histidine active site
• Papain-like cysteine peptidase superfamily
• Papain-like cysteine endopeptidase
• Papain family cysteine protease
• Cathepsin propeptide inhibitor domain (I29)

KeywordsUniProt

• Disulfide bond
• Glycoprotein
• Hydrolase
• Lysosome
• Neurodegeneration
• Neuronal ceroid lipofuscinosis
• Protease
• Signal
• Thiol protease
• Zymogen