Cathepsin H precursor - Homo sapiens (Human)

Names and origin

Protein names

Recommended name:
    Cathepsin H
    EC=3.4.22.16
Cleaved into the following 3 chains:
    1- Recommended name:
            Cathepsin H mini chain
    2- Recommended name:
            Cathepsin H heavy chain
    3- Recommended name:
            Cathepsin H light chain

Gene names

Name:	CTSH
Synonyms:	CPSB

Organism

Homo sapiens (Human)

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	335 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	Important for the overall degradation of proteins in lysosomes.
Catalytic activity	Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-\|-Xaa bonds) as well as an endopeptidase.
Subunit structure	Composed of a mini chain and a large chain. The large chain may be split into heavy and light chain. All chains are held together by disulfide bonds.
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 Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Ref.4 Inferred from direct assay. Source: UniProtKB
Cellular component	lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cysteine-type endopeptidase activity Ref.4 Inferred from direct assay. Source: UniProtKB protein binding Inferred from physical interaction. Source: UniProtKB
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 – 22

22

Propeptide

23 – 97

75

Activation peptide Ref.5

PRO_0000026206

Peptide

98 – 105

8

Cathepsin H mini chain

PRO_0000026207

Propeptide

106 – 115

10

PRO_0000026208

Chain

116 – 335

220

Cathepsin H

PRO_0000026209

Chain

116 – 292

177

Cathepsin H heavy chain

PRO_0000026210

Chain

293 – 335

43

Cathepsin H light chain

PRO_0000026211

Sites

Active site

141

1

By similarity

Active site

281

1

By similarity

Active site

301

1

By similarity

Amino acid modifications

Glycosylation

101

1

N-linked (GlcNAc...) Ref.5

Glycosylation

230

1

N-linked (GlcNAc...) Ref.5

Disulfide bond

102 ↔ 327

By similarity

Disulfide bond

138 ↔ 181

By similarity

Disulfide bond

172 ↔ 214

By similarity

Disulfide bond

272 ↔ 322

By similarity

Natural variations

Natural variant

11

1

G → R: dbSNP rs2289702.

VAR_057038

Natural variant

23

1

A → T: dbSNP rs35001431.

VAR_057039

Natural variant

126

1

G → R in a colorectal cancer sample; somatic mutation. Ref.9

VAR_036478

Experimental info

Sequence conflict

179

1

H → Y Ref.1

Sequence conflict

179

1

H → Y Ref.3

Sequence conflict

306

1

Q → E Ref.5

Sequence conflict

306

1

Q → E Ref.6

Secondary structure

1

.

335

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P09668-1 [UniParc].

Last modified May 27, 2002. Version 3.
Checksum: 4690615EE155B767
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FASTA

335

37,378

        10         20         30         40         50         60 
MWATLPLLCA GAWLLGVPVC GAAELSVNSL EKFHFKSWMS KHRKTYSTEE YHHRLQTFAS 

        70         80         90        100        110        120 
NWRKINAHNN GNHTFKMALN QFSDMSFAEI KHKYLWSEPQ NCSATKSNYL RGTGPYPPSV 

       130        140        150        160        170        180 
DWRKKGNFVS PVKNQGACGS CWTFSTTGAL ESAIAIATGK MLSLAEQQLV DCAQDFNNHG 

       190        200        210        220        230        240 
CQGGLPSQAF EYILYNKGIM GEDTYPYQGK DGYCKFQPGK AIGFVKDVAN ITIYDEEAMV 

       250        260        270        280        290        300 
EAVALYNPVS FAFEVTQDFM MYRTGIYSST SCHKTPDKVN HAVLAVGYGE KNGIPYWIVK 

       310        320        330 
NSWGPQWGMN GYFLIERGKN MCGLAACASY PIPLV

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of human preprocathepsin H, a lysosomal cysteine proteinase." Fuchs R., Gassen H.G. Nucleic Acids Res. 17:9471-9471(1989) [PubMed: 2587265] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"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. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
[3]	"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]. Tissue: Eye.
[4]	"Molecular cloning and sequencing of a cDNA coding for mature human kidney cathepsin H." Fuchs R., Machleidt W., Gassen H.G. Biol. Chem. Hoppe-Seyler 369:469-475(1988) [PubMed: 2849458] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 88-335. Tissue: Kidney.
[5]	"Amino acid sequences of the human kidney cathepsins H and L." Ritonja A., Popovic T., Kotnik M., Machleidt W., Turk V. FEBS Lett. 228:341-345(1988) [PubMed: 3342889] [Abstract] Cited for: PROTEIN SEQUENCE OF 98-105 AND 114-335, GLYCOSYLATION AT ASN-101 AND ASN-230. Tissue: Kidney.
[6]	"Human cathepsins B, H and L: characterization by amino acid sequences and some kinetics of inhibition by the kininogens." Machleidt W., Ritonja A., Popovic T., Kotnik M., Brzin J., Turk V., Machleidt I., Mueller-Esterl W. (In) Turk V. (eds.); Cysteine proteinases and their inhibitors, pp.3-18, Walter de Gruyter, Berlin and New York (1986) Cited for: PROTEIN SEQUENCE OF 99-105; 116-159 AND 294-335.
[7]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[8]	"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: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-230, MASS SPECTROMETRY. Tissue: Liver.
[9]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-126.
+	Additional computationally mapped references.

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Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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Cross-references

Sequence databases

X07549 mRNA. Translation: CAA30428.1.
X07549 mRNA. Translation: CAA30429.1. Sequence problems.
AK314698 mRNA. Translation: BAG37247.1.
BC002479 mRNA. Translation: AAH02479.1.
X16832 mRNA. Translation: CAA34734.1.

IPI

IPI00297487.

PIR

KHHUH. S12486.

UniGene

Hs.148641

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BZN	model	-	B	116-335	[»]

SMR

P09668. Positions 116-335.

ModBase

Search...

Protein family/group databases

MEROPS

C01.040.

Proteomic databases

PRIDE

P09668.

Genome annotation databases

Ensembl

ENSG00000103811. Homo sapiens. [Contig view]

Organism-specific databases

GeneCards

GC15M077001.

H-InvDB

HIX0012481.

HGNC

HGNC:2535. CTSH.

HPA

CAB000458.
HPA003524.

MIM

116820. gene.

PharmGKB

PA27033.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P09668.

HOVERGEN

P09668.

Enzyme and pathway databases

BRENDA

3.4.22.16. 247.

Gene expression databases

ArrayExpress

P09668.

Bgee

P09668.

CleanEx

HS_CTSH.

GermOnline

ENSG00000103811. 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

SOURCE

Search...

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Entry information

Entry name

CATH_HUMAN

Accession

Primary (citable) accession number: P09668
Secondary accession number(s): B2RBK0, Q9BUM7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	May 27, 2002
Last modified:	June 16, 2009
This is version 108 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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