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Protein

Cathepsin F

Gene

Ctsf

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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

Catalytic activityi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei273 – 2731By similarity
Active sitei409 – 4091By similarity
Active sitei429 – 4291By similarity

GO - Molecular functioni

  1. cysteine-type peptidase activity Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Enzyme and pathway databases

ReactomeiREACT_196550. MHC class II antigen presentation.

Protein family/group databases

MEROPSiC01.018.

Names & Taxonomyi

Protein namesi
Recommended name:
Cathepsin F (EC:3.4.22.41)
Gene namesi
Name:Ctsf
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 19

Organism-specific databases

MGIiMGI:1861434. Ctsf.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: MGI
  2. lysosome Source: UniProtKB-SubCell
  3. vesicle Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Propeptidei20 – 248229Activation peptidePRO_0000026204Add
BLAST
Chaini249 – 462214Cathepsin FPRO_0000026205Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi35 – 351N-linked (GlcNAc...)Sequence Analysis
Glycosylationi138 – 1381N-linked (GlcNAc...)Sequence Analysis
Glycosylationi173 – 1731N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi270 ↔ 311By similarity
Disulfide bondi304 ↔ 344By similarity
Glycosylationi345 – 3451N-linked (GlcNAc...)Sequence Analysis
Glycosylationi356 – 3561N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi402 ↔ 450By similarity
Glycosylationi418 – 4181N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQBiQ9R013.
PaxDbiQ9R013.
PRIDEiQ9R013.

PTM databases

PhosphoSiteiQ9R013.

Expressioni

Gene expression databases

BgeeiQ9R013.
CleanExiMM_CTSF.
ExpressionAtlasiQ9R013. baseline and differential.
GenevestigatoriQ9R013.

Structurei

3D structure databases

ProteinModelPortaliQ9R013.
SMRiQ9R013. Positions 164-462.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG4870.
GeneTreeiENSGT00760000118871.
HOGENOMiHOG000230774.
HOVERGENiHBG011513.
InParanoidiQ9R013.
KOiK01373.
OMAiNNMVRAQ.
OrthoDBiEOG7DJSKG.
PhylomeDBiQ9R013.
TreeFamiTF314550.

Family and domain databases

InterProiIPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PfamiPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSiPR00705. PAPAIN.
SMARTiSM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEiPS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9R013-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAPLLQLLWL LTLLSTVALS PVPAKPWADD EQAWNLSSQE LLAPARFALD
60 70 80 90 100
MYNYGRAAGT RAVLGAVRGR VRRAGQGSLF SLEATLEEPP CNDPLVCPLP
110 120 130 140 150
ETKKTVLCSF EVLEELKEHL LLRRDCSPVN AKVTEFRNAT FSSFLPLLDK
160 170 180 190 200
DPLPQDFSVK MAPLFKDFMT TYNRTYESRE EAQWRLTVFA RNMIRAQKIQ
210 220 230 240 250
ALDRGTAQYG ITKFSDLTEE EFHTIYLNPL LQKESGRKMS PAKSINDLAP
260 270 280 290 300
PEWDWRKKGA VTEVKNQGMC GSCWAFSVTG NVEGQWFLNR GTLLSLSEQE
310 320 330 340 350
LLDCDKVDKA CLGGLPSNAY AAIKNLGGLE TEDDYGYQGH VQTCNFSAQM
360 370 380 390 400
AKVYINDSVE LSRNENKIAA WLAQKGPISV AINAFGMQFY RHGIAHPFRP
410 420 430 440 450
LCSPWFIDHA VLLVGYGNRS NIPYWAIKNS WGSDWGEEGY YYLYRGSGAC
460
GVNTMASSAV VN
Length:462
Mass (Da):51,661
Last modified:May 1, 2000 - v1
Checksum:i782A1C9D609A4781
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31P → L in CAB42884. (PubMed:10318784)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF136280 mRNA. Translation: AAF13147.1.
AF217224 Genomic DNA. Translation: AAF37228.1.
AJ131851 mRNA. Translation: CAB42884.1.
AK075862 mRNA. Translation: BAC36013.1.
BC058758 mRNA. Translation: AAH58758.1.
CCDSiCCDS29440.1.
RefSeqiNP_063914.1. NM_019861.1.
UniGeneiMm.29561.

Genome annotation databases

EnsembliENSMUST00000119694; ENSMUSP00000112481; ENSMUSG00000083282.
GeneIDi56464.
KEGGimmu:56464.
UCSCiuc008gbc.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF136280 mRNA. Translation: AAF13147.1.
AF217224 Genomic DNA. Translation: AAF37228.1.
AJ131851 mRNA. Translation: CAB42884.1.
AK075862 mRNA. Translation: BAC36013.1.
BC058758 mRNA. Translation: AAH58758.1.
CCDSiCCDS29440.1.
RefSeqiNP_063914.1. NM_019861.1.
UniGeneiMm.29561.

3D structure databases

ProteinModelPortaliQ9R013.
SMRiQ9R013. Positions 164-462.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiC01.018.

PTM databases

PhosphoSiteiQ9R013.

Proteomic databases

MaxQBiQ9R013.
PaxDbiQ9R013.
PRIDEiQ9R013.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000119694; ENSMUSP00000112481; ENSMUSG00000083282.
GeneIDi56464.
KEGGimmu:56464.
UCSCiuc008gbc.1. mouse.

Organism-specific databases

CTDi8722.
MGIiMGI:1861434. Ctsf.

Phylogenomic databases

eggNOGiCOG4870.
GeneTreeiENSGT00760000118871.
HOGENOMiHOG000230774.
HOVERGENiHBG011513.
InParanoidiQ9R013.
KOiK01373.
OMAiNNMVRAQ.
OrthoDBiEOG7DJSKG.
PhylomeDBiQ9R013.
TreeFamiTF314550.

Enzyme and pathway databases

ReactomeiREACT_196550. MHC class II antigen presentation.

Miscellaneous databases

NextBioi312722.
PROiQ9R013.
SOURCEiSearch...

Gene expression databases

BgeeiQ9R013.
CleanExiMM_CTSF.
ExpressionAtlasiQ9R013. baseline and differential.
GenevestigatoriQ9R013.

Family and domain databases

InterProiIPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PfamiPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSiPR00705. PAPAIN.
SMARTiSM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEiPS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse cathepsin F: cDNA cloning, genomic organization and chromosomal assignment of the gene."
    Deussing J., Tisljar K., Papazoglou A., Peters C.
    Gene 251:165-173(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/Ola and C57BL/6J.
    Tissue: Mammary gland.
  2. "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: Brain.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Tongue.
  4. "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: Eye.

Entry informationi

Entry nameiCATF_MOUSE
AccessioniPrimary (citable) accession number: Q9R013
Secondary accession number(s): Q9WUT4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: May 1, 2000
Last modified: February 4, 2015
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.