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Q9R013

- CATF_MOUSE

UniProt

Q9R013 - CATF_MOUSE

Protein

Cathepsin F

Gene

Ctsf

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    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

    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. lysosome Source: UniProtKB-SubCell

    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

    ArrayExpressiQ9R013.
    BgeeiQ9R013.
    CleanExiMM_CTSF.
    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.
    GeneTreeiENSGT00750000117440.
    HOGENOMiHOG000230774.
    HOVERGENiHBG011513.
    InParanoidiQ9R013.
    KOiK01373.
    OMAiDYSYQGH.
    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

    MAPLLQLLWL LTLLSTVALS PVPAKPWADD EQAWNLSSQE LLAPARFALD    50
    MYNYGRAAGT RAVLGAVRGR VRRAGQGSLF SLEATLEEPP CNDPLVCPLP 100
    ETKKTVLCSF EVLEELKEHL LLRRDCSPVN AKVTEFRNAT FSSFLPLLDK 150
    DPLPQDFSVK MAPLFKDFMT TYNRTYESRE EAQWRLTVFA RNMIRAQKIQ 200
    ALDRGTAQYG ITKFSDLTEE EFHTIYLNPL LQKESGRKMS PAKSINDLAP 250
    PEWDWRKKGA VTEVKNQGMC GSCWAFSVTG NVEGQWFLNR GTLLSLSEQE 300
    LLDCDKVDKA CLGGLPSNAY AAIKNLGGLE TEDDYGYQGH VQTCNFSAQM 350
    AKVYINDSVE LSRNENKIAA WLAQKGPISV AINAFGMQFY RHGIAHPFRP 400
    LCSPWFIDHA VLLVGYGNRS NIPYWAIKNS WGSDWGEEGY YYLYRGSGAC 450
    GVNTMASSAV VN 462
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS29440.1.
    RefSeqi NP_063914.1. NM_019861.1.
    UniGenei Mm.29561.

    3D structure databases

    ProteinModelPortali Q9R013.
    SMRi Q9R013. Positions 164-462.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi C01.018.

    PTM databases

    PhosphoSitei Q9R013.

    Proteomic databases

    MaxQBi Q9R013.
    PaxDbi Q9R013.
    PRIDEi Q9R013.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000119694 ; ENSMUSP00000112481 ; ENSMUSG00000083282 .
    GeneIDi 56464.
    KEGGi mmu:56464.
    UCSCi uc008gbc.1. mouse.

    Organism-specific databases

    CTDi 8722.
    MGIi MGI:1861434. Ctsf.

    Phylogenomic databases

    eggNOGi COG4870.
    GeneTreei ENSGT00750000117440.
    HOGENOMi HOG000230774.
    HOVERGENi HBG011513.
    InParanoidi Q9R013.
    KOi K01373.
    OMAi DYSYQGH.
    OrthoDBi EOG7DJSKG.
    PhylomeDBi Q9R013.
    TreeFami TF314550.

    Enzyme and pathway databases

    Reactomei REACT_196550. MHC class II antigen presentation.

    Miscellaneous databases

    NextBioi 312722.
    PROi Q9R013.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9R013.
    Bgeei Q9R013.
    CleanExi MM_CTSF.
    Genevestigatori Q9R013.

    Family and domain databases

    InterProi IPR000169. Pept_cys_AS.
    IPR025660. Pept_his_AS.
    IPR013128. Peptidase_C1A.
    IPR000668. Peptidase_C1A_C.
    IPR013201. Prot_inhib_I29.
    [Graphical view ]
    PANTHERi PTHR12411. PTHR12411. 1 hit.
    Pfami PF08246. Inhibitor_I29. 1 hit.
    PF00112. Peptidase_C1. 1 hit.
    [Graphical view ]
    PRINTSi PR00705. PAPAIN.
    SMARTi SM00848. Inhibitor_I29. 1 hit.
    SM00645. Pept_C1. 1 hit.
    [Graphical view ]
    PROSITEi PS00139. THIOL_PROTEASE_CYS. 1 hit.
    PS00639. THIOL_PROTEASE_HIS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 120 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