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Reviewed, UniProtKB/Swiss-Prot Q9UBX1 (CATF_HUMAN)

Last modified June 16, 2009. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Cathepsin F
      Short name=CATSF
    EC=3.4.22.41
Gene names
Name: CTSF
OrganismHomo sapiens (Human)
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.

Sequence similarities

Belongs to the peptidase C1 family.

Ontologies

Keywords
   Cellular componentLysosome
   Coding sequence diversityPolymorphism
   DomainSignal
   Molecular functionHydrolase
Protease
Thiol protease
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Zymogen
   Technical term3D-structure
Gene Ontology (GO)
   Biological processproteolysis Ref.8

Traceable author statement. Source: ProtInc

   Cellular componentlysosome Ref.8

Traceable author statement. Source: ProtInc

   Molecular functioncysteine-type endopeptidase activity Ref.8

Traceable author statement. Source: ProtInc

Complete GO annotation...

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.12
Active site4311 Ref.12
Active site4511 By similarity

Amino acid modifications

Modified residue3531Phosphothreonine Ref.10
Modified residue3651Phosphoserine Ref.10
Glycosylation1601N-linked (GlcNAc...) Potential
Glycosylation1951N-linked (GlcNAc...) Potential
Glycosylation3671N-linked (GlcNAc...)
Glycosylation3781N-linked (GlcNAc...)
Glycosylation4401N-linked (GlcNAc...)
Disulfide bond292 ↔ 333 Ref.12
Disulfide bond326 ↔ 366 Ref.12
Disulfide bond424 ↔ 472 By similarity

Natural variations

Natural variant1531Q → R: dbSNP rs11550508.
VAR_051513

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
Q9UBX1-1 [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: 10318784] [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: 10198209] [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: 10661872] [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: 10362521] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Cathepsin F, a novel cysteine protease with an extremly 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: 14702039] [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: 15489334] [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: 9822672] [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., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 161-484.
Tissue: Testis.
[10]"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-353 AND SER-365, MASS SPECTROMETRY.
[11]"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: 19159218] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-367; ASN-378 AND ASN-440, MASS SPECTROMETRY.
Tissue: Liver.
[12]"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: 12225749] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 271-484, ACTIVE SITE, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
IPIIPI00002816.
RefSeqNP_003784.2.
UniGeneHs.11590

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1D5Umodel-A271-484[»]
1M6DX-ray1.70A/B271-484[»]
ModBaseSearch...

Protein family/group databases

MEROPSC01.018.

PTM databases

PhosphoSiteQ9UBX1.

Proteomic databases

PeptideAtlasQ9UBX1.
PRIDEQ9UBX1.

Genome annotation databases

EnsemblENSG00000174080. Homo sapiens. [Contig view]
GeneID8722.
KEGGhsa:8722.

Organism-specific databases

GeneCardsGC11M066088.
H-InvDBHIX0009840.
HGNCHGNC:2531. CTSF.
HPACAB002141.
MIM603539. gene.
PharmGKBPA27031.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ9UBX1.
HOVERGENQ9UBX1.
OMAQ9UBX1. KTLLCSF.

Enzyme and pathway databases

BRENDA3.4.22.41. 247.

Gene expression databases

BgeeQ9UBX1.
CleanExHS_CTSF.
GermOnlineENSG00000174080. Homo sapiens.

Family and domain databases

InterProIPR000169. Pept_cys_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERPTHR12411. Peptidase_C1A. 1 hit.
PfamPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSPR00705. PAPAIN.
ProDomPD000158. Peptidase_C1. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEPS00640. THIOL_PROTEASE_ASN. False negative.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio32715.
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: June 16, 2009
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 11

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents