CATF_MOUSE
ID CATF_MOUSE Reviewed; 462 AA.
AC Q9R013; Q9WUT4;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Cathepsin F;
DE EC=3.4.22.41;
DE Flags: Precursor;
GN Name=Ctsf;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Ola, and C57BL/6J; TISSUE=Mammary gland;
RX PubMed=10876093; DOI=10.1016/s0378-1119(00)00196-7;
RA Deussing J., Tisljar K., Papazoglou A., Peters C.;
RT "Mouse cathepsin F: cDNA cloning, genomic organization and chromosomal
RT assignment of the gene.";
RL Gene 251:165-173(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=10318784; DOI=10.1074/jbc.274.20.13800;
RA Santamaria I., Velasco G., Pendas A.M., Paz A., Lopez-Otin C.;
RT "Molecular cloning and structural and functional characterization of human
RT cathepsin F, a new cysteine proteinase of the papain family with a long
RT propeptide domain.";
RL J. Biol. Chem. 274:13800-13809(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Thiol protease which is believed to participate in
CC intracellular degradation and turnover of proteins. Has also been
CC implicated in tumor invasion and metastasis.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=The recombinant enzyme cleaves synthetic substrates with Phe
CC and Leu (better than Val) in P2, with high specificity constant
CC (kcat/Km) comparable to that of cathepsin L.; EC=3.4.22.41;
CC -!- SUBCELLULAR LOCATION: Lysosome.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089}.
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DR EMBL; AF136280; AAF13147.1; -; mRNA.
DR EMBL; AF217224; AAF37228.1; -; Genomic_DNA.
DR EMBL; AJ131851; CAB42884.1; -; mRNA.
DR EMBL; AK075862; BAC36013.1; -; mRNA.
DR EMBL; BC058758; AAH58758.1; -; mRNA.
DR CCDS; CCDS29440.1; -.
DR RefSeq; NP_063914.1; NM_019861.1.
DR AlphaFoldDB; Q9R013; -.
DR SMR; Q9R013; -.
DR STRING; 10090.ENSMUSP00000112481; -.
DR MEROPS; C01.018; -.
DR GlyConnect; 2191; 4 N-Linked glycans (2 sites).
DR GlyGen; Q9R013; 6 sites, 4 N-linked glycans (2 sites).
DR iPTMnet; Q9R013; -.
DR PhosphoSitePlus; Q9R013; -.
DR jPOST; Q9R013; -.
DR MaxQB; Q9R013; -.
DR PaxDb; Q9R013; -.
DR PeptideAtlas; Q9R013; -.
DR PRIDE; Q9R013; -.
DR ProteomicsDB; 265540; -.
DR Antibodypedia; 30202; 288 antibodies from 34 providers.
DR DNASU; 56464; -.
DR Ensembl; ENSMUST00000119694; ENSMUSP00000112481; ENSMUSG00000083282.
DR GeneID; 56464; -.
DR KEGG; mmu:56464; -.
DR UCSC; uc008gbc.1; mouse.
DR CTD; 8722; -.
DR MGI; MGI:1861434; Ctsf.
DR VEuPathDB; HostDB:ENSMUSG00000083282; -.
DR eggNOG; KOG1542; Eukaryota.
DR GeneTree; ENSGT00940000162141; -.
DR HOGENOM; CLU_012184_10_0_1; -.
DR InParanoid; Q9R013; -.
DR OMA; RGHMQAC; -.
DR OrthoDB; 1264766at2759; -.
DR PhylomeDB; Q9R013; -.
DR TreeFam; TF314550; -.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR BioGRID-ORCS; 56464; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Ctsf; mouse.
DR PRO; PR:Q9R013; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9R013; protein.
DR Bgee; ENSMUSG00000083282; Expressed in retinal neural layer and 218 other tissues.
DR ExpressionAtlas; Q9R013; baseline and differential.
DR Genevisible; Q9R013; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0008234; F:cysteine-type peptidase activity; ISS:MGI.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR CDD; cd02248; Peptidase_C1A; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR039417; Peptidase_C1A_papain-like.
DR InterPro; IPR013201; Prot_inhib_I29.
DR Pfam; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00848; Inhibitor_I29; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Protease;
KW Reference proteome; Signal; Thiol protease; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..248
FT /note="Activation peptide"
FT /id="PRO_0000026204"
FT CHAIN 249..462
FT /note="Cathepsin F"
FT /id="PRO_0000026205"
FT ACT_SITE 273
FT /evidence="ECO:0000250"
FT ACT_SITE 409
FT /evidence="ECO:0000250"
FT ACT_SITE 429
FT /evidence="ECO:0000250"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 270..311
FT /evidence="ECO:0000250"
FT DISULFID 304..344
FT /evidence="ECO:0000250"
FT DISULFID 402..450
FT /evidence="ECO:0000250"
FT CONFLICT 3
FT /note="P -> L (in Ref. 2; CAB42884)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 462 AA; 51661 MW; 782A1C9D609A4781 CRC64;
MAPLLQLLWL LTLLSTVALS PVPAKPWADD EQAWNLSSQE LLAPARFALD MYNYGRAAGT
RAVLGAVRGR VRRAGQGSLF SLEATLEEPP CNDPLVCPLP ETKKTVLCSF EVLEELKEHL
LLRRDCSPVN AKVTEFRNAT FSSFLPLLDK DPLPQDFSVK MAPLFKDFMT TYNRTYESRE
EAQWRLTVFA RNMIRAQKIQ ALDRGTAQYG ITKFSDLTEE EFHTIYLNPL LQKESGRKMS
PAKSINDLAP PEWDWRKKGA VTEVKNQGMC GSCWAFSVTG NVEGQWFLNR GTLLSLSEQE
LLDCDKVDKA CLGGLPSNAY AAIKNLGGLE TEDDYGYQGH VQTCNFSAQM AKVYINDSVE
LSRNENKIAA WLAQKGPISV AINAFGMQFY RHGIAHPFRP LCSPWFIDHA VLLVGYGNRS
NIPYWAIKNS WGSDWGEEGY YYLYRGSGAC GVNTMASSAV VN
