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Q9R013

- CATF_MOUSE

UniProt

Q9R013 - CATF_MOUSE

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Protein

Cathepsin F

Gene
Ctsf
Organism
Mus musculus (Mouse)
Status
Reviewed - 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 – 2731 By similarity
Active sitei409 – 4091 By similarity
Active sitei429 – 4291 By 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. lysosome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

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.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31P → L in CAB42884. 1 Publication

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

« 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: September 3, 2014
This is version 119 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

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