Cathepsin F precursor - Homo sapiens (Human)

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Names and origin

Protein names

Recommended name:
    Cathepsin F
      Short name=CATSF
    EC=3.4.22.41

Gene names

Name:

CTSF

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	484 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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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.

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Ontologies

Keywords
Cellular component	Lysosome
Coding sequence diversity	Polymorphism
Domain	Signal
Molecular function	Hydrolase Protease Thiol protease
PTM	Disulfide bond Glycoprotein Phosphoprotein Zymogen
Technical term	3D-structure
Gene Ontology (GO)
Biological process	proteolysis Ref.8 Traceable author statement. Source: ProtInc
Cellular component	lysosome Ref.8 Traceable author statement. Source: ProtInc
Molecular function	cysteine-type endopeptidase activity Ref.8 Traceable author statement. Source: ProtInc
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

19

Potential

Propeptide

20 – 270

251

Activation peptide

PRO_0000026202

Chain

271 – 484

214

Cathepsin F

PRO_0000026203

Sites

Active site

1

Active site

1

Active site

1

By similarity

Amino acid modifications

Modified residue

353

1

Phosphothreonine Ref.10

Modified residue

365

1

Phosphoserine Ref.10

Glycosylation

160

1

N-linked (GlcNAc...) Potential

Glycosylation

195

1

N-linked (GlcNAc...) Potential

Glycosylation

367

1

N-linked (GlcNAc...)

Glycosylation

378

1

N-linked (GlcNAc...)

Glycosylation

440

1

N-linked (GlcNAc...)

Disulfide bond

Disulfide bond

Disulfide bond

By similarity

Natural variations

Natural variant

153

1

Q → R: dbSNP rs11550508.

VAR_051513

Experimental info

Sequence conflict

305

1

E → K in AAF13146. Ref.5

Sequence conflict

442 – 484

43

SDVPF…SAVVD → EFRCLSCIQPGHRQGWDHSI SGPLEGK Ref.9

Secondary structure

1

.

484

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

Q9UBX1-1 [UniParc].

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

484

53,366

        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

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References

	« Hide 'large scale' referencesShow '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. 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.

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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.

IPI

IPI00002816.

RefSeq

NP_003784.2.

UniGene

Hs.11590

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1D5U	model	-	A	271-484	[»]
1M6D	X-ray	1.70	A/B	271-484	[»]

ModBase

Search...

Protein family/group databases

MEROPS

C01.018.

PTM databases

PhosphoSite

Q9UBX1.

Proteomic databases

PeptideAtlas

Q9UBX1.

PRIDE

Q9UBX1.

Genome annotation databases

Ensembl

ENSG00000174080. Homo sapiens. [Contig view]

GeneID

8722.

KEGG

hsa:8722.

Organism-specific databases

GeneCards

GC11M066088.

H-InvDB

HIX0009840.

HGNC

HGNC:2531. CTSF.

HPA

CAB002141.

MIM

603539. gene.

PharmGKB

PA27031.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q9UBX1.

HOVERGEN

Q9UBX1.

OMA

Q9UBX1. KTLLCSF.

Enzyme and pathway databases

BRENDA

3.4.22.41. 247.

Gene expression databases

Bgee

Q9UBX1.

CleanEx

HS_CTSF.

GermOnline

ENSG00000174080. Homo sapiens.

Family and domain databases

InterPro

IPR000169. Pept_cys_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]

PANTHER

PTHR12411. Peptidase_C1A. 1 hit.

Pfam

PF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]

PRINTS

PR00705. PAPAIN.

ProDom

PD000158. Peptidase_C1. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00645. Pept_C1. 1 hit.
[Graphical view]

PROSITE

PS00640. THIOL_PROTEASE_ASN. False negative.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

32715.

SOURCE

Search...

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Entry information

Entry name

CATF_HUMAN

Accession

Primary (citable) accession number: Q9UBX1
Secondary accession number(s): B2R964

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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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