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Q9R013 (CATF_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

EC=3.4.22.41
Gene names
Name:Ctsf
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length462 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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.

Sequence similarities

Belongs to the peptidase C1 family.

Ontologies

Keywords
   Cellular componentLysosome
   DomainSignal
   Molecular functionHydrolase
Protease
Thiol protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentlysosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncysteine-type peptidase activity

Inferred from sequence or structural similarity Ref.1. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Propeptide20 – 248229Activation peptide
PRO_0000026204
Chain249 – 462214Cathepsin F
PRO_0000026205

Sites

Active site2731 By similarity
Active site4091 By similarity
Active site4291 By similarity

Amino acid modifications

Glycosylation351N-linked (GlcNAc...) Potential
Glycosylation1381N-linked (GlcNAc...) Potential
Glycosylation1731N-linked (GlcNAc...) Potential
Glycosylation3451N-linked (GlcNAc...) Potential
Glycosylation3561N-linked (GlcNAc...) Potential
Glycosylation4181N-linked (GlcNAc...) Potential
Disulfide bond270 ↔ 311 By similarity
Disulfide bond304 ↔ 344 By similarity
Disulfide bond402 ↔ 450 By similarity

Experimental info

Sequence conflict31P → L in CAB42884. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9R013 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 782A1C9D609A4781

FASTA46251,661
        10         20         30         40         50         60 
MAPLLQLLWL LTLLSTVALS PVPAKPWADD EQAWNLSSQE LLAPARFALD MYNYGRAAGT 

        70         80         90        100        110        120 
RAVLGAVRGR VRRAGQGSLF SLEATLEEPP CNDPLVCPLP ETKKTVLCSF EVLEELKEHL 

       130        140        150        160        170        180 
LLRRDCSPVN AKVTEFRNAT FSSFLPLLDK DPLPQDFSVK MAPLFKDFMT TYNRTYESRE 

       190        200        210        220        230        240 
EAQWRLTVFA RNMIRAQKIQ ALDRGTAQYG ITKFSDLTEE EFHTIYLNPL LQKESGRKMS 

       250        260        270        280        290        300 
PAKSINDLAP PEWDWRKKGA VTEVKNQGMC GSCWAFSVTG NVEGQWFLNR GTLLSLSEQE 

       310        320        330        340        350        360 
LLDCDKVDKA CLGGLPSNAY AAIKNLGGLE TEDDYGYQGH VQTCNFSAQM AKVYINDSVE 

       370        380        390        400        410        420 
LSRNENKIAA WLAQKGPISV AINAFGMQFY RHGIAHPFRP LCSPWFIDHA VLLVGYGNRS 

       430        440        450        460 
NIPYWAIKNS WGSDWGEEGY YYLYRGSGAC GVNTMASSAV VN 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS29440.1.
RefSeqNP_063914.1. NM_019861.1.
UniGeneMm.29561.

3D structure databases

ProteinModelPortalQ9R013.
SMRQ9R013. Positions 164-462.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSC01.018.

PTM databases

PhosphoSiteQ9R013.

Proteomic databases

MaxQBQ9R013.
PaxDbQ9R013.
PRIDEQ9R013.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000119694; ENSMUSP00000112481; ENSMUSG00000083282.
GeneID56464.
KEGGmmu:56464.
UCSCuc008gbc.1. mouse.

Organism-specific databases

CTD8722.
MGIMGI:1861434. Ctsf.

Phylogenomic databases

eggNOGCOG4870.
GeneTreeENSGT00750000117440.
HOGENOMHOG000230774.
HOVERGENHBG011513.
InParanoidQ9R013.
KOK01373.
OMADYSYQGH.
OrthoDBEOG7DJSKG.
PhylomeDBQ9R013.
TreeFamTF314550.

Gene expression databases

ArrayExpressQ9R013.
BgeeQ9R013.
CleanExMM_CTSF.
GenevestigatorQ9R013.

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

NextBio312722.
PROQ9R013.
SOURCESearch...

Entry information

Entry nameCATF_MOUSE
AccessionPrimary (citable) accession number: Q9R013
Secondary accession number(s): Q9WUT4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot