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Cathepsin F (CATSF) (EC 3.4.22.41)

 CATF_HUMAN              Reviewed;         484 AA.
Q9UBX1; B2R964; O95240; Q9NSU4; Q9UKQ5;
24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
10-OCT-2018, entry version 164.
RecName: Full=Cathepsin F;
Short=CATSF;
EC=3.4.22.41;
Flags: Precursor;
Name=CTSF;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Prostate;
PubMed=10318784; DOI=10.1074/jbc.274.20.13800;
Santamaria I., Velasco G., Pendas A.M., Paz A., Lopez-Otin C.;
"Molecular cloning and structural and functional characterization of
human cathepsin F, a new cysteine proteinase of the papain family with
a long propeptide domain.";
J. Biol. Chem. 274:13800-13809(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Ovary;
PubMed=10198209; DOI=10.1006/bbrc.1999.0461;
Naegler D.K., Sulea T., Menard R.;
"Full-length cDNA of human cathepsin F predicts the presence of a
cystatin domain at the N-terminus of the cysteine protease zymogen.";
Biochem. Biophys. Res. Commun. 257:313-318(1999).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10661872; DOI=10.1515/BC.1999.185;
Wex T., Wex H., Broemme D.;
"The human cathepsin F gene -- a fusion product between an ancestral
cathepsin and cystatin gene.";
Biol. Chem. 380:1439-1442(1999).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10362521; DOI=10.1006/bbrc.1999.0700;
Wex T., Levy B., Wex H., Bromme D.;
"Human cathepsins F and W: a new subgroup of cathepsins.";
Biochem. Biophys. Res. Commun. 259:401-407(1999).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Kidney;
Deussing J., Tisljar K., Papazoglou A., Peters C.;
"Cathepsin F, a novel cysteine protease with an extremely long
propeptide.";
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 147-484, AND CHARACTERIZATION.
TISSUE=Brain, and Smooth muscle;
PubMed=9822672; DOI=10.1074/jbc.273.48.32000;
Wang B., Shi G.-P., Yao P.M., Li Z., Chapman H.A., Broemme D.;
"Human cathepsin F. Molecular cloning, functional expression, tissue
localization, and enzymatic characterization.";
J. Biol. Chem. 273:32000-32008(1998).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 161-484.
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[10]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-367; ASN-378 AND ASN-440.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[11]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 271-484, ACTIVE SITE, AND
DISULFIDE BONDS.
PubMed=12225749; DOI=10.1016/S0022-2836(02)00780-5;
Somoza J.R., Palmer J.T., Ho J.D.;
"The crystal structure of human cathepsin F and its implications for
the development of novel immunomodulators.";
J. Mol. Biol. 322:559-568(2002).
[12]
VARIANTS CLN13 CYS-231; ARG-321; ALA-458 AND LEU-480.
PubMed=23297359; DOI=10.1093/hmg/dds558;
Smith K.R., Dahl H.H., Canafoglia L., Andermann E., Damiano J.,
Morbin M., Bruni A.C., Giaccone G., Cossette P., Saftig P.,
Groetzinger J., Schwake M., Andermann F., Staropoli J.F., Sims K.B.,
Mole S.E., Franceschetti S., Alexander N.A., Cooper J.D.,
Chapman H.A., Carpenter S., Berkovic S.F., Bahlo M.;
"Cathepsin F mutations cause Type B Kufs disease, an adult-onset
neuronal ceroid lipofuscinosis.";
Hum. Mol. Genet. 22:1417-1423(2013).
-!- 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.
-!- TISSUE SPECIFICITY: High expression levels in heart, skeletal
muscle, brain, testis and ovary; moderate levels in prostate,
placenta, liver and colon; and no detectable expression in
peripheral leukocytes and thymus.
-!- DISEASE: Ceroid lipofuscinosis, neuronal, 13 (CLN13) [MIM:615362]:
A form of neuronal ceroid lipofuscinosis characterized by adult
onset of progressive cognitive decline and motor dysfunction
leading to dementia and often early death. Some patients develop
seizures. Neuronal ceroid lipofuscinoses are progressive
neurodegenerative, lysosomal storage diseases characterized by
intracellular accumulation of autofluorescent liposomal material.
{ECO:0000269|PubMed:23297359}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the peptidase C1 family.
{ECO:0000255|PROSITE-ProRule:PRU10088, ECO:0000255|PROSITE-
ProRule:PRU10089}.
-----------------------------------------------------------------------
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EMBL; AJ007331; CAB42883.1; -; mRNA.
EMBL; AF088886; AAD26616.2; -; mRNA.
EMBL; AF132894; AAD41790.1; -; Genomic_DNA.
EMBL; AF136279; AAF13146.1; -; mRNA.
EMBL; AF071748; AAC78838.1; -; mRNA.
EMBL; AF071749; AAC78839.1; -; mRNA.
EMBL; AK313657; BAG36411.1; -; mRNA.
EMBL; BC011682; AAH11682.1; -; mRNA.
EMBL; BC036451; AAH36451.1; -; mRNA.
EMBL; AL137742; CAB70900.1; -; mRNA.
CCDS; CCDS8144.1; -.
RefSeq; NP_003784.2; NM_003793.3.
UniGene; Hs.11590; -.
PDB; 1D5U; Model; -; A=271-484.
PDB; 1M6D; X-ray; 1.70 A; A/B=271-484.
PDBsum; 1D5U; -.
PDBsum; 1M6D; -.
ProteinModelPortal; Q9UBX1; -.
SMR; Q9UBX1; -.
BioGrid; 114261; 18.
STRING; 9606.ENSP00000310832; -.
BindingDB; Q9UBX1; -.
ChEMBL; CHEMBL2517; -.
DrugBank; DB02243; 4-Morpholin-4-Yl-Piperidine-1-Carboxylic Acid [1-(3-Benzenesulfonyl-1-Propyl-Allylcarbamoyl)-2-Phenylethyl]-Amide.
DrugBank; DB01871; [1-(1-Benzyl-3-Hydroxy-2-Oxo-Propylcarbamoyl)-2-Phenyl-Ethyl]-Carbamic Acid Benzyl Ester.
DrugBank; DB03536; Benzoyl-Arginine-Alanine-Methyl Ketone.
DrugBank; DB08775; BENZOYL-TYROSINE-ALANINE-METHYL KETONE.
DrugBank; DB07913; HOMOPHENYLALANINYLMETHANE.
DrugBank; DB03691; WRR-112.
DrugBank; DB03573; WRR-99.
GuidetoPHARMACOLOGY; 2347; -.
MEROPS; C01.018; -.
GlyConnect; 1080; -.
iPTMnet; Q9UBX1; -.
PhosphoSitePlus; Q9UBX1; -.
BioMuta; CTSF; -.
DMDM; 12643325; -.
EPD; Q9UBX1; -.
MaxQB; Q9UBX1; -.
PaxDb; Q9UBX1; -.
PeptideAtlas; Q9UBX1; -.
PRIDE; Q9UBX1; -.
ProteomicsDB; 84089; -.
DNASU; 8722; -.
Ensembl; ENST00000310325; ENSP00000310832; ENSG00000174080.
GeneID; 8722; -.
KEGG; hsa:8722; -.
UCSC; uc001oip.4; human.
CTD; 8722; -.
DisGeNET; 8722; -.
EuPathDB; HostDB:ENSG00000174080.10; -.
GeneCards; CTSF; -.
GeneReviews; CTSF; -.
HGNC; HGNC:2531; CTSF.
HPA; CAB002141; -.
HPA; HPA031431; -.
HPA; HPA055610; -.
MalaCards; CTSF; -.
MIM; 603539; gene.
MIM; 615362; phenotype.
neXtProt; NX_Q9UBX1; -.
OpenTargets; ENSG00000174080; -.
Orphanet; 352709; CLN13 disease.
PharmGKB; PA27031; -.
eggNOG; KOG1542; Eukaryota.
eggNOG; COG4870; LUCA.
GeneTree; ENSGT00900000140823; -.
HOGENOM; HOG000230774; -.
HOVERGEN; HBG011513; -.
InParanoid; Q9UBX1; -.
KO; K01373; -.
OMA; LAPPEWD; -.
OrthoDB; EOG091G05SD; -.
PhylomeDB; Q9UBX1; -.
TreeFam; TF314550; -.
BRENDA; 3.4.22.41; 2681.
Reactome; R-HSA-2132295; MHC class II antigen presentation.
ChiTaRS; CTSF; human.
EvolutionaryTrace; Q9UBX1; -.
GeneWiki; Cathepsin_F; -.
GenomeRNAi; 8722; -.
PRO; PR:Q9UBX1; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000174080; Expressed in 233 organ(s), highest expression level in right hemisphere of cerebellum.
CleanEx; HS_CTSF; -.
ExpressionAtlas; Q9UBX1; baseline and differential.
Genevisible; Q9UBX1; HS.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:1903561; C:extracellular vesicle; HDA:UniProtKB.
GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
GO; GO:0005764; C:lysosome; TAS:ProtInc.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
GO; GO:0006508; P:proteolysis; TAS:ProtInc.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IBA:GO_Central.
CDD; cd02248; Peptidase_C1A; 1.
InterPro; IPR038765; Papain_like_cys_pep_sf.
InterPro; IPR000169; Pept_cys_AS.
InterPro; IPR025660; Pept_his_AS.
InterPro; IPR013128; Peptidase_C1A.
InterPro; IPR000668; Peptidase_C1A_C.
InterPro; IPR039417; Peptidase_C1A_papain-like.
InterPro; IPR013201; Prot_inhib_I29.
PANTHER; PTHR12411; PTHR12411; 1.
Pfam; PF08246; Inhibitor_I29; 1.
Pfam; PF00112; Peptidase_C1; 1.
PRINTS; PR00705; PAPAIN.
SMART; SM00848; Inhibitor_I29; 1.
SMART; SM00645; Pept_C1; 1.
SUPFAM; SSF54001; SSF54001; 1.
PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Disease mutation; Disulfide bond;
Glycoprotein; Hydrolase; Lysosome; Neurodegeneration;
Neuronal ceroid lipofuscinosis; Polymorphism; Protease;
Reference proteome; Signal; Thiol protease; Zymogen.
SIGNAL 1 19 {ECO:0000255}.
PROPEP 20 270 Activation peptide.
/FTId=PRO_0000026202.
CHAIN 271 484 Cathepsin F.
/FTId=PRO_0000026203.
ACT_SITE 295 295 {ECO:0000269|PubMed:12225749}.
ACT_SITE 431 431 {ECO:0000269|PubMed:12225749}.
ACT_SITE 451 451 {ECO:0000250}.
CARBOHYD 160 160 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 195 195 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 367 367 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 378 378 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 440 440 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
DISULFID 292 333 {ECO:0000269|PubMed:12225749}.
DISULFID 326 366 {ECO:0000269|PubMed:12225749}.
DISULFID 424 472 {ECO:0000250}.
VARIANT 153 153 Q -> R (in dbSNP:rs11550508).
/FTId=VAR_051513.
VARIANT 231 231 Y -> C (in CLN13; dbSNP:rs143889283).
{ECO:0000269|PubMed:23297359}.
/FTId=VAR_070159.
VARIANT 321 321 Q -> R (in CLN13; dbSNP:rs397514731).
{ECO:0000269|PubMed:23297359}.
/FTId=VAR_070160.
VARIANT 458 458 G -> A (in CLN13; dbSNP:rs397514732).
{ECO:0000269|PubMed:23297359}.
/FTId=VAR_070161.
VARIANT 480 480 S -> L (in CLN13; dbSNP:rs397514733).
{ECO:0000269|PubMed:23297359}.
/FTId=VAR_070162.
CONFLICT 305 305 E -> K (in Ref. 5; AAF13146).
{ECO:0000305}.
CONFLICT 442 484 SDVPFWAIKNSWGTDWGEKGYYYLHRGSGACGVNTMASSAV
VD -> EFRCLSCIQPGHRQGWDHSISGPLEGK (in
Ref. 9). {ECO:0000305}.
HELIX 277 280 {ECO:0000244|PDB:1M6D}.
STRAND 291 293 {ECO:0000244|PDB:1M6D}.
HELIX 295 312 {ECO:0000244|PDB:1M6D}.
HELIX 320 326 {ECO:0000244|PDB:1M6D}.
STRAND 328 330 {ECO:0000244|PDB:1M6D}.
HELIX 338 348 {ECO:0000244|PDB:1M6D}.
TURN 354 356 {ECO:0000244|PDB:1M6D}.
HELIX 370 372 {ECO:0000244|PDB:1M6D}.
STRAND 378 382 {ECO:0000244|PDB:1M6D}.
HELIX 387 397 {ECO:0000244|PDB:1M6D}.
STRAND 400 404 {ECO:0000244|PDB:1M6D}.
HELIX 407 411 {ECO:0000244|PDB:1M6D}.
STRAND 414 417 {ECO:0000244|PDB:1M6D}.
HELIX 421 423 {ECO:0000244|PDB:1M6D}.
STRAND 431 441 {ECO:0000244|PDB:1M6D}.
STRAND 444 450 {ECO:0000244|PDB:1M6D}.
STRAND 462 469 {ECO:0000244|PDB:1M6D}.
HELIX 471 473 {ECO:0000244|PDB:1M6D}.
TURN 474 477 {ECO:0000244|PDB:1M6D}.
STRAND 479 482 {ECO:0000244|PDB:1M6D}.
SEQUENCE 484 AA; 53366 MW; 1D5D551B489D822B CRC64;
MAPWLQLLSL LGLLPGAVAA PAQPRAASFQ AWGPPSPELL APTRFALEMF NRGRAAGTRA
VLGLVRGRVR RAGQGSLYSL EATLEEPPCN DPMVCRLPVS KKTLLCSFQV LDELGRHVLL
RKDCGPVDTK VPGAGEPKSA FTQGSAMISS LSQNHPDNRN ETFSSVISLL NEDPLSQDLP
VKMASIFKNF VITYNRTYES KEEARWRLSV FVNNMVRAQK IQALDRGTAQ YGVTKFSDLT
EEEFRTIYLN TLLRKEPGNK MKQAKSVGDL APPEWDWRSK GAVTKVKDQG MCGSCWAFSV
TGNVEGQWFL NQGTLLSLSE QELLDCDKMD KACMGGLPSN AYSAIKNLGG LETEDDYSYQ
GHMQSCNFSA EKAKVYINDS VELSQNEQKL AAWLAKRGPI SVAINAFGMQ FYRHGISRPL
RPLCSPWLID HAVLLVGYGN RSDVPFWAIK NSWGTDWGEK GYYYLHRGSG ACGVNTMASS
AVVD


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