Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9UBX1 (CATF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cathepsin F

Short name=CATSF
EC=3.4.22.41
Gene names
Name:CTSF
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length484 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis.

Catalytic activity

The recombinant enzyme cleaves synthetic substrates with Phe and Leu (better than Val) in P2, with high specificity constant (k(cat)/K(m)) comparable to that of cathepsin L.

Subcellular location

Lysosome.

Tissue specificity

High expression levels in heart, skeletal muscle, brain, testis and ovary; moderate levels in prostate, placenta, liver and colon; and no detectable expression in peripheral leukocytes and thymus.

Involvement in disease

Ceroid lipofuscinosis, neuronal, 13 (CLN13) [MIM:615362]: A form of neuronal ceroid lipofuscinosis characterized by adult onset of progressive cognitive decline and motor dysfunction leading to dementia and often early death. Some patients develop seizures. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12

Sequence similarities

Belongs to the peptidase C1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Propeptide20 – 270251Activation peptide
PRO_0000026202
Chain271 – 484214Cathepsin F
PRO_0000026203

Sites

Active site2951 Ref.11
Active site4311 Ref.11
Active site4511 By similarity

Amino acid modifications

Glycosylation1601N-linked (GlcNAc...) Potential
Glycosylation1951N-linked (GlcNAc...) Potential
Glycosylation3671N-linked (GlcNAc...) Ref.10
Glycosylation3781N-linked (GlcNAc...) Ref.10
Glycosylation4401N-linked (GlcNAc...) Ref.10
Disulfide bond292 ↔ 333 Ref.11
Disulfide bond326 ↔ 366 Ref.11
Disulfide bond424 ↔ 472 By similarity

Natural variations

Natural variant1531Q → R.
Corresponds to variant rs11550508 [ dbSNP | Ensembl ].
VAR_051513
Natural variant2311Y → C in CLN13. Ref.12
VAR_070159
Natural variant3211Q → R in CLN13. Ref.12
VAR_070160
Natural variant4581G → A in CLN13. Ref.12
VAR_070161
Natural variant4801S → L in CLN13. Ref.12
VAR_070162

Experimental info

Sequence conflict3051E → K in AAF13146. Ref.5
Sequence conflict442 – 48443SDVPF…SAVVD → EFRCLSCIQPGHRQGWDHSI SGPLEGK Ref.9

Secondary structure

........................................ 484
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9UBX1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 1D5D551B489D822B

FASTA48453,366
        10         20         30         40         50         60 
MAPWLQLLSL LGLLPGAVAA PAQPRAASFQ AWGPPSPELL APTRFALEMF NRGRAAGTRA 

        70         80         90        100        110        120 
VLGLVRGRVR RAGQGSLYSL EATLEEPPCN DPMVCRLPVS KKTLLCSFQV LDELGRHVLL 

       130        140        150        160        170        180 
RKDCGPVDTK VPGAGEPKSA FTQGSAMISS LSQNHPDNRN ETFSSVISLL NEDPLSQDLP 

       190        200        210        220        230        240 
VKMASIFKNF VITYNRTYES KEEARWRLSV FVNNMVRAQK IQALDRGTAQ YGVTKFSDLT 

       250        260        270        280        290        300 
EEEFRTIYLN TLLRKEPGNK MKQAKSVGDL APPEWDWRSK GAVTKVKDQG MCGSCWAFSV 

       310        320        330        340        350        360 
TGNVEGQWFL NQGTLLSLSE QELLDCDKMD KACMGGLPSN AYSAIKNLGG LETEDDYSYQ 

       370        380        390        400        410        420 
GHMQSCNFSA EKAKVYINDS VELSQNEQKL AAWLAKRGPI SVAINAFGMQ FYRHGISRPL 

       430        440        450        460        470        480 
RPLCSPWLID HAVLLVGYGN RSDVPFWAIK NSWGTDWGEK GYYYLHRGSG ACGVNTMASS 


AVVD 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and structural and functional characterization of human cathepsin F, a new cysteine proteinase of the papain family with a long propeptide domain."
Santamaria I., Velasco G., Pendas A.M., Paz A., Lopez-Otin C.
J. Biol. Chem. 274:13800-13809(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Prostate.
[2]"Full-length cDNA of human cathepsin F predicts the presence of a cystatin domain at the N-terminus of the cysteine protease zymogen."
Naegler D.K., Sulea T., Menard R.
Biochem. Biophys. Res. Commun. 257:313-318(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Ovary.
[3]"The human cathepsin F gene -- a fusion product between an ancestral cathepsin and cystatin gene."
Wex T., Wex H., Broemme D.
Biol. Chem. 380:1439-1442(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Human cathepsins F and W: a new subgroup of cathepsins."
Wex T., Levy B., Wex H., Bromme D.
Biochem. Biophys. Res. Commun. 259:401-407(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Cathepsin F, a novel cysteine protease with an extremely long propeptide."
Deussing J., Tisljar K., Papazoglou A., Peters C.
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.
[6]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung and Testis.
[8]"Human cathepsin F. Molecular cloning, functional expression, tissue localization, and enzymatic characterization."
Wang B., Shi G.-P., Yao P.M., Li Z., Chapman H.A., Broemme D.
J. Biol. Chem. 273:32000-32008(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 147-484, CHARACTERIZATION.
Tissue: Brain and Smooth muscle.
[9]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 161-484.
Tissue: Testis.
[10]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-367; ASN-378 AND ASN-440.
Tissue: Liver.
[11]"The crystal structure of human cathepsin F and its implications for the development of novel immunomodulators."
Somoza J.R., Palmer J.T., Ho J.D.
J. Mol. Biol. 322:559-568(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 271-484, ACTIVE SITE, DISULFIDE BONDS.
[12]"Cathepsin F mutations cause Type B Kufs disease, an adult-onset neuronal ceroid lipofuscinosis."
Smith K.R., Dahl H.H., Canafoglia L., Andermann E., Damiano J., Morbin M., Bruni A.C., Giaccone G., Cossette P., Saftig P., Groetzinger J., Schwake M., Andermann F., Staropoli J.F., Sims K.B., Mole S.E., Franceschetti S., Alexander N.A. expand/collapse author list , Cooper J.D., Chapman H.A., Carpenter S., Berkovic S.F., Bahlo M.
Hum. Mol. Genet. 22:1417-1423(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CLN13 CYS-231; ARG-321; ALA-458 AND LEU-480.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ007331 mRNA. Translation: CAB42883.1.
AF088886 mRNA. Translation: AAD26616.2.
AF132894 Genomic DNA. Translation: AAD41790.1.
AF136279 mRNA. Translation: AAF13146.1.
AF071748 mRNA. Translation: AAC78838.1.
AF071749 mRNA. Translation: AAC78839.1.
AK313657 mRNA. Translation: BAG36411.1.
BC011682 mRNA. Translation: AAH11682.1.
BC036451 mRNA. Translation: AAH36451.1.
AL137742 mRNA. Translation: CAB70900.1.
RefSeqNP_003784.2. NM_003793.3.
UniGeneHs.11590.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1D5Umodel-A271-484[»]
1M6DX-ray1.70A/B271-484[»]
ProteinModelPortalQ9UBX1.
SMRQ9UBX1. Positions 194-484.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000310832.

Chemistry

BindingDBQ9UBX1.
ChEMBLCHEMBL2517.

Protein family/group databases

MEROPSC01.018.

PTM databases

PhosphoSiteQ9UBX1.

Polymorphism databases

DMDM12643325.

Proteomic databases

PaxDbQ9UBX1.
PeptideAtlasQ9UBX1.
PRIDEQ9UBX1.

Protocols and materials databases

DNASU8722.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000310325; ENSP00000310832; ENSG00000174080.
GeneID8722.
KEGGhsa:8722.
UCSCuc001oip.3. human.

Organism-specific databases

CTD8722.
GeneCardsGC11M066332.
HGNCHGNC:2531. CTSF.
HPACAB002141.
HPA031431.
HPA055610.
MIM603539. gene.
615362. phenotype.
neXtProtNX_Q9UBX1.
Orphanet352709. CLN13 disease.
PharmGKBPA27031.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4870.
HOGENOMHOG000230774.
HOVERGENHBG011513.
InParanoidQ9UBX1.
KOK01373.
OMADYSYQGH.
OrthoDBEOG7DJSKG.
PhylomeDBQ9UBX1.
TreeFamTF314550.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressQ9UBX1.
BgeeQ9UBX1.
CleanExHS_CTSF.
GenevestigatorQ9UBX1.

Family and domain databases

InterProIPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERPTHR12411. PTHR12411. 1 hit.
PfamPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSPR00705. PAPAIN.
SMARTSM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEPS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCTSF. human.
EvolutionaryTraceQ9UBX1.
GeneWikiCathepsin_F.
GenomeRNAi8722.
NextBio32715.
PROQ9UBX1.
SOURCESearch...

Entry information

Entry nameCATF_HUMAN
AccessionPrimary (citable) accession number: Q9UBX1
Secondary accession number(s): B2R964 expand/collapse secondary AC list , O95240, Q9NSU4, Q9UKQ5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM