Q9UBX1 (CATF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cathepsin F
Short name=CATSF
EC=3.4.22.41

Gene names

Name:

CTSF

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	484 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein 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.
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.
Sequence similarities	Belongs to the peptidase C1 family.

Ontologies

Keywords
Cellular component	Lysosome
Coding sequence diversity	Polymorphism
Domain	Signal
Molecular function	Hydrolase Protease Thiol protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	antigen processing and presentation of exogenous peptide antigen via MHC class II Traceable author statement. Source: Reactome proteolysis Traceable author statement Ref.8. Source: ProtInc
Cellular_component	lysosomal lumen Traceable author statement. Source: Reactome
Molecular_function	cysteine-type endopeptidase activity Traceable author statement Ref.8. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

19

Potential

Propeptide

20 – 270

251

Activation peptide

PRO_0000026202

Chain

271 – 484

214

Cathepsin F

PRO_0000026203

Sites

Active site

295

1

Ref.11

Active site

431

1

Ref.11

Active site

451

1

By similarity

Amino acid modifications

Glycosylation

160

1

N-linked (GlcNAc...) Potential

Glycosylation

195

1

N-linked (GlcNAc...) Potential

Glycosylation

367

1

N-linked (GlcNAc...) Ref.10

Glycosylation

378

1

N-linked (GlcNAc...) Ref.10

Glycosylation

440

1

N-linked (GlcNAc...) Ref.10

Disulfide bond

292 ↔ 333

Ref.11

Disulfide bond

326 ↔ 366

Ref.11

Disulfide bond

424 ↔ 472

By similarity

Natural variations

Natural variant

153

1

Q → R.
Corresponds to variant rs11550508 [ dbSNP | Ensembl ].

VAR_051513

Experimental info

Sequence conflict

305

1

E → K in AAF13146. Ref.5

Sequence conflict

442 – 484

43

SDVPF…SAVVD → EFRCLSCIQPGHRQGWDHSI SGPLEGK Ref.9

Secondary structure

1

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484

Helix Strand Turn

Details...

Helix

277 – 280

4

Beta strand

291 – 293

3

Helix

295 – 312

18

Helix

320 – 326

7

Beta strand

328 – 330

3

Helix

338 – 348

11

Turn

354 – 356

3

Helix

370 – 372

3

Beta strand

378 – 382

5

Helix

387 – 397

11

Beta strand

400 – 404

5

Helix

407 – 411

5

Beta strand

414 – 417

4

Helix

421 – 423

3

Beta strand

431 – 441

11

Beta strand

444 – 450

7

Beta strand

462 – 469

8

Helix

471 – 473

3

Turn

474 – 477

4

Beta strand

479 – 482

4

Sequences

	Sequence		Length	Mass (Da)
	Q9UBX1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 1D5D551B489D822B	FASTA	484	53,366
	10 20 30 40 50 60 MAPWLQLLSL LGLLPGAVAA PAQPRAASFQ AWGPPSPELL APTRFALEMF NRGRAAGTRA 70 80 90 100 110 120 VLGLVRGRVR RAGQGSLYSL EATLEEPPCN DPMVCRLPVS KKTLLCSFQV LDELGRHVLL 130 140 150 160 170 180 RKDCGPVDTK VPGAGEPKSA FTQGSAMISS LSQNHPDNRN ETFSSVISLL NEDPLSQDLP 190 200 210 220 230 240 VKMASIFKNF VITYNRTYES KEEARWRLSV FVNNMVRAQK IQALDRGTAQ YGVTKFSDLT 250 260 270 280 290 300 EEEFRTIYLN TLLRKEPGNK MKQAKSVGDL APPEWDWRSK GAVTKVKDQG MCGSCWAFSV 310 320 330 340 350 360 TGNVEGQWFL NQGTLLSLSE QELLDCDKMD KACMGGLPSN AYSAIKNLGG LETEDDYSYQ 370 380 390 400 410 420 GHMQSCNFSA EKAKVYINDS VELSQNEQKL AAWLAKRGPI SVAINAFGMQ FYRHGISRPL 430 440 450 460 470 480 RPLCSPWLID HAVLLVGYGN RSDVPFWAIK NSWGTDWGEK GYYYLHRGSG ACGVNTMASS AVVD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: Prostate.
[2]	"Full-length cDNA of human cathepsin F predicts the presence of a cystatin domain at the N-terminus of the cysteine protease zymogen." Naegler D.K., Sulea T., Menard R. Biochem. Biophys. Res. Commun. 257:313-318(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Ovary.
[3]	"The human cathepsin F gene -- a fusion product between an ancestral cathepsin and cystatin gene." Wex T., Wex H., Broemme D. Biol. Chem. 380:1439-1442(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Human cathepsins F and W: a new subgroup of cathepsins." Wex T., Levy B., Wex H., Bromme D. Biochem. Biophys. Res. Commun. 259:401-407(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"Cathepsin F, a novel cysteine protease with an extremely long propeptide." Deussing J., Tisljar K., Papazoglou A., Peters C. Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Kidney.
[6]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	"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: Lung and Testis.
[8]	"Human cathepsin F. Molecular cloning, functional expression, tissue localization, and enzymatic characterization." Wang B., Shi G.-P., Yao P.M., Li Z., Chapman H.A., Broemme D. J. Biol. Chem. 273:32000-32008(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 147-484, CHARACTERIZATION. Tissue: Brain and Smooth muscle.
[9]	"The full-ORF clone resource of the German cDNA consortium." 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. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 161-484. Tissue: Testis.
[10]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-367; ASN-378 AND ASN-440, MASS SPECTROMETRY. Tissue: Liver.
[11]	"The crystal structure of human cathepsin F and its implications for the development of novel immunomodulators." Somoza J.R., Palmer J.T., Ho J.D. J. Mol. Biol. 322:559-568(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 271-484, ACTIVE SITE, DISULFIDE BONDS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ007331 mRNA. Translation: CAB42883.1.
AF088886 mRNA. Translation: AAD26616.2.
AF132894 Genomic DNA. Translation: AAD41790.1.
AF136279 mRNA. Translation: AAF13146.1.
AF071748 mRNA. Translation: AAC78838.1.
AF071749 mRNA. Translation: AAC78839.1.
AK313657 mRNA. Translation: BAG36411.1.
BC011682 mRNA. Translation: AAH11682.1.
BC036451 mRNA. Translation: AAH36451.1.
AL137742 mRNA. Translation: CAB70900.1.

IPI

IPI00002816.

RefSeq

NP_003784.2. NM_003793.3.

UniGene

Hs.11590.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1D5U	model	-	A	271-484	[»]
1M6D	X-ray	1.70	A/B	271-484	[»]

ProteinModelPortal

Q9UBX1.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000310832.

Protein family/group databases

MEROPS

C01.018.

PTM databases

PhosphoSite

Q9UBX1.

Polymorphism databases

DMDM

12643325.

Proteomic databases

PaxDb

Q9UBX1.

PeptideAtlas

Q9UBX1.

PRIDE

Q9UBX1.

Protocols and materials databases

DNASU

8722.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000310325; ENSP00000310832; ENSG00000174080.

GeneID

8722.

KEGG

hsa:8722.

UCSC

uc001oip.3. human.

Organism-specific databases

CTD

8722.

GeneCards

GC11M066332.

HGNC

HGNC:2531. CTSF.

HPA

CAB002141.

MIM

603539. gene.

neXtProt

NX_Q9UBX1.

PharmGKB

PA27031.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG4870.

HOGENOM

HOG000230774.

HOVERGEN

HBG011513.

InParanoid

Q9UBX1.

KO

K01373.

OMA

LAPPEWD.

OrthoDB

EOG4CC41T.

PhylomeDB

Q9UBX1.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

Q9UBX1.

Bgee

Q9UBX1.

CleanEx

HS_CTSF.

Genevestigator

Q9UBX1.

GermOnline

ENSG00000174080. Homo sapiens.

Family and domain databases

InterPro

IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]

PANTHER

PTHR12411. PTHR12411. 1 hit.

Pfam

PF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]

PRINTS

PR00705. PAPAIN.

SMART

SM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]

PROSITE

PS00640. THIOL_PROTEASE_ASN. False negative.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q9UBX1.

ChEMBL

CHEMBL2517.

ChiTaRS

CTSF. human.

EvolutionaryTrace

Q9UBX1.

GenomeRNAi

8722.

NextBio

32715.

SOURCE

Search...

Entry information

Entry name

CATF_HUMAN

Accession

Primary (citable) accession number: Q9UBX1
Secondary accession number(s): B2R964 , O95240, Q9NSU4, Q9UKQ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 124 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.