Cathepsin S precursor - Homo sapiens (Human)

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Names and origin

Protein names

Recommended name:
Cathepsin S
EC=3.4.22.27

Gene names

Name:

CTSS

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	331 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N.
Catalytic activity	Similar to cathepsin L, but with much less activity on Z-Phe-Arg-\|-NHMec, and more activity on the Z-Val-Val-Arg-\|-Xaa compound.
Subunit structure	Monomer.
Subcellular location	Lysosome.
Sequence similarities	Belongs to the peptidase C1 family.

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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
Gene Ontology (GO)
Biological process	immune response Ref.4 Traceable author statement. Source: ProtInc proteolysis Ref.1 Traceable author statement. Source: ProtInc
Cellular component	extracellular region Non-traceable author statement. Source: UniProtKB lysosome Non-traceable author statement. Source: UniProtKB
Molecular function	cysteine-type endopeptidase activity Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 16

16

Potential

Propeptide

17 – 114

98

Activation peptide

PRO_0000026313

Chain

115 – 331

217

Cathepsin S

PRO_0000026314

Sites

Active site

139

1

By similarity

Active site

278

1

By similarity

Active site

298

1

By similarity

Amino acid modifications

Glycosylation

104

1

N-linked (GlcNAc...) Potential

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Natural variations

Natural variant

113

1

R → W: dbSNP rs2230061. Ref.6

VAR_025385

Natural variant

161

1

S → T: dbSNP rs1059604. Ref.1 Ref.4

VAR_025386

Experimental info

Sequence conflict

92

1

M → T Ref.1

Sequence conflict

92

1

M → T Ref.4

Secondary structure

1

.

331

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P25774-1 [UniParc].

Last modified February 21, 2006. Version 3.
Checksum: 86093619DB6F0269
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FASTA

331

37,496

        10         20         30         40         50         60 
MKRLVCVLLV CSSAVAQLHK DPTLDHHWHL WKKTYGKQYK EKNEEAVRRL IWEKNLKFVM 

        70         80         90        100        110        120 
LHNLEHSMGM HSYDLGMNHL GDMTSEEVMS LMSSLRVPSQ WQRNITYKSN PNRILPDSVD 

       130        140        150        160        170        180 
WREKGCVTEV KYQGSCGACW AFSAVGALEA QLKLKTGKLV SLSAQNLVDC STEKYGNKGC 

       190        200        210        220        230        240 
NGGFMTTAFQ YIIDNKGIDS DASYPYKAMD QKCQYDSKYR AATCSKYTEL PYGREDVLKE 

       250        260        270        280        290        300 
AVANKGPVSV GVDARHPSFF LYRSGVYYEP SCTQNVNHGV LVVGYGDLNG KEYWLVKNSW 

       310        320        330 
GHNFGEEGYI RMARNKGNHC GIASFPSYPE I

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and expression of human alveolar macrophage cathepsin S, an elastinolytic cysteine protease." Shi G.-P., Munger J.S., Meara J.P., Rich D.H., Chapman H.A. J. Biol. Chem. 267:7258-7262(1992) [PubMed: 1373132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT THR-161. Tissue: Alveolar macrophage.
[2]	"Phylogenetic conservation of cysteine proteinases. Cloning and expression of a cDNA coding for human cathepsin S." Wiederanders B., Broemme D., Kirschke H., von Figura K., Schmidt B., Peters C. J. Biol. Chem. 267:13708-13713(1992) [PubMed: 1377692] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Testis.
[3]	Wiederanders B., Broemme D., Kirschke H., von Figura K., Schmidt B., Peters C. Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 211.
[4]	"Human cathepsin S: chromosomal localization, gene structure, and tissue distribution." Shi G.-P., Webb A.C., Foster K.E., Knoll J.H.M., Lemere C.A., Munger J.S., Chapman H.A. J. Biol. Chem. 269:11530-11536(1994) [PubMed: 8157683] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-161.
[5]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. Bentley D.R. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT TRP-113. Tissue: Pancreas.
[7]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[8]	"Three-dimensional structures of the cysteine proteases cathepsins K and S deduced by knowledge-based modelling and active site characteristics." Fengler A., Brandt W. Protein Eng. 11:1007-1013(1998) [PubMed: 9876921] [Abstract] Cited for: 3D-STRUCTURE MODELING OF 115-331.
[9]	"Structure of a Cys25-->Ser mutant of human cathepsin S." Turkenburg J.P., Lamers M.B., Brzozowski A.M., Wright L.M., Hubbard R.E., Sturt S.L., Williams D.H. Acta Crystallogr. D 58:451-455(2002) [PubMed: 11856830] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 115-331.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

S93414 mRNA. Translation: AAB22005.1.
M86553 mRNA. Translation: AAA35655.1.
M90696 mRNA. Translation: AAC37592.1.
U07374

U07373 Genomic DNA. Translation: AAB60643.2.
AL356292 Genomic DNA. Translation: CAI13657.1.
BC002642 mRNA. Translation: AAH02642.1.

IPI

IPI00299150.

PIR

A42482.

RefSeq

NP_004070.3.

UniGene

Hs.181301

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BXF	model	-	A	115-331	[»]
1GLO	X-ray	2.20	A	115-331	[»]
1MS6	X-ray	1.90	A	115-331	[»]
1NPZ	X-ray	2.00	A/B	115-331	[»]
1NQC	X-ray	1.80	A	115-331	[»]
2C0Y	X-ray	2.10	A	17-331	[»]
2F1G	X-ray	1.90	A/B	112-331	[»]
2FQ9	X-ray	1.65	A/B	114-331	[»]
2FRA	X-ray	1.90	A/B	114-330	[»]
2FRQ	X-ray	1.60	A/B	115-331	[»]
2FT2	X-ray	1.70	A/B	114-331	[»]
2FUD	X-ray	1.95	A/B	115-331	[»]
2FYE	X-ray	2.20	A	115-331	[»]
2G6D	X-ray	2.50	A	115-331	[»]
2G7Y	X-ray	2.00	A/B	114-330	[»]
2H7J	X-ray	1.50	A/B	112-331	[»]
2HH5	X-ray	1.80	A/B	112-331	[»]
2HHN	X-ray	1.55	A/B	112-331	[»]
2HXZ	X-ray	1.90	A/B/C	112-331	[»]
2OP3	X-ray	1.60	A/B	112-331	[»]
2R9M	X-ray	1.97	A/B	115-331	[»]
2R9N	X-ray	2.00	A/B	115-331	[»]
2R9O	X-ray	2.00	A/B	115-331	[»]

SMR

P25774. Positions 18-331.

ModBase

Search...

Protein family/group databases

MEROPS

C01.034.
I29.004.

Proteomic databases

PeptideAtlas

P25774.

PRIDE

P25774.

Genome annotation databases

Ensembl

ENSG00000163131. Homo sapiens. [Contig view]

GeneID

1520.

KEGG

hsa:1520.

UCSC

uc001evn.1. human.

Organism-specific databases

GeneCards

GC01M148969.

H-InvDB

HIX0001035.

HGNC

HGNC:2545. CTSS.

HPA

CAB000460.
HPA002988.

MIM

116845. gene.

PharmGKB

PA27041.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P25774.

HOVERGEN

P25774.

OMA

P25774. DSVDWRE.

Enzyme and pathway databases

BRENDA

3.4.22.27. 247.

Gene expression databases

ArrayExpress

P25774.

Bgee

P25774.

CleanEx

HS_CTSS.

GermOnline

ENSG00000163131. Homo sapiens.

Family and domain databases

InterPro

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

PANTHER

PTHR12411. Peptidase_C1A. 1 hit.

Pfam

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

PRINTS

PR00705. PAPAIN.

ProDom

PD000158. Peptidase_C1. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00645. Pept_C1. 1 hit.
[Graphical view]

PROSITE

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

ProtoNet

Search...

Other Resources

BindingDB

P25774.

NextBio

6291.

PMAP-CutDB

P25774.

SOURCE

Search...

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Entry information

Entry name

CATS_HUMAN

Accession

Primary (citable) accession number: P25774
Secondary accession number(s): Q5T5I0, Q9BUG3

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	February 21, 2006
Last modified:	July 7, 2009
This is version 105 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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