P00786 (CATH_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pro-cathepsin H

Cleaved into the following 4 chains:

1. Cathepsin H mini chain
2. Cathepsin H
   EC=3.4.22.16
3. Cathepsin H heavy chain
4. Cathepsin H light chain

Gene names

Name:

Ctsh

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	333 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	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.
Sequence caution	The sequence AAA63484.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Lysosome
Domain	Signal
Molecular function	Hydrolase Protease Thiol protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ERK1 and ERK2 cascade Inferred from sequence or structural similarity. Source: UniProtKB T cell mediated cytotoxicity Inferred from sequence or structural similarity. Source: UniProtKB bradykinin catabolic process Inferred from sequence or structural similarity. Source: UniProtKB cellular response to thyroid hormone stimulus Inferred from expression pattern PubMed 21217776. Source: UniProtKB dichotomous subdivision of terminal units involved in lung branching Inferred from sequence or structural similarity. Source: UniProtKB immune response-regulating signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB membrane protein proteolysis Inferred from sequence or structural similarity. Source: UniProtKB metanephros development Inferred from expression pattern PubMed 16153003. Source: UniProtKB negative regulation of apoptotic process Inferred from sequence or structural similarity. Source: UniProtKB neuropeptide catabolic process Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of angiogenesis Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of cell proliferation Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of epithelial cell migration Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of gene expression Inferred from sequence or structural similarity. Source: UniProtKB protein destabilization Inferred from sequence or structural similarity. Source: UniProtKB response to retinoic acid Inferred from sequence or structural similarity. Source: UniProtKB spermatogenesis Inferred from expression pattern PubMed 9238520. Source: RGD surfactant homeostasis Inferred from sequence or structural similarity. Source: UniProtKB zymogen activation Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	acrosomal vesicle Inferred from direct assay PubMed 12838426. Source: RGD alveolar lamellar body Inferred from sequence or structural similarity. Source: UniProtKB cilium axoneme Inferred from direct assay PubMed 12838426. Source: RGD cytosol Inferred from sequence or structural similarity. Source: UniProtKB extracellular space Inferred from sequence or structural similarity. Source: UniProtKB lysosome Inferred from sequence or structural similarity. Source: UniProtKB outer dense fiber Inferred from direct assay PubMed 12838426. Source: RGD
Molecular_function	HLA-A specific activating MHC class I receptor activity Inferred from sequence or structural similarity. Source: UniProtKB aminopeptidase activity Inferred from direct assay PubMed 1483460. Source: RGD apoptotic protease activator activity Inferred from sequence or structural similarity. Source: UniProtKB cysteine-type endopeptidase activity Inferred from sequence or structural similarity. Source: UniProtKB protein self-association Inferred from direct assay PubMed 7550115. Source: RGD serine-type endopeptidase activity Inferred from sequence or structural similarity. Source: UniProtKB thyroid hormone binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Potential
	Propeptide	21 – 95	75	Activation peptide		PRO_0000026224
	Chain	96 – 103	8	Cathepsin H mini chain		PRO_0000026225
	Propeptide	104 – 113	10	Potential		PRO_0000026226
	Chain	114 – 333	220	Cathepsin H		PRO_0000026227
	Chain	114 – 290	177	Cathepsin H heavy chain		PRO_0000026228
	Chain	291 – 333	43	Cathepsin H light chain		PRO_0000026229
Sites
	Active site	139	1	By similarity
	Active site	279	1	By similarity
	Active site	299	1	By similarity
Amino acid modifications
	Glycosylation	228	1	N-linked (GlcNAc...) Ref.5
	Disulfide bond	100 ↔ 325		By similarity
	Disulfide bond	136 ↔ 179		By similarity
	Disulfide bond	170 ↔ 212		By similarity
	Disulfide bond	270 ↔ 320		By similarity
Natural variations
	Natural variant	287	1	G → A.

Sequences

	Sequence		Length	Mass (Da)
	P00786 [UniParc]. Last modified August 1, 1988. Version 1. Checksum: A90AC66338F0B744	FASTA	333	37,104
	10 20 30 40 50 60 MWTALPLLCA GAWLLSAGAT AELTVNAIEK FHFTSWMKQH QKTYSSREYS HRLQVFANNW 70 80 90 100 110 120 RKIQAHNQRN HTFKMGLNQF SDMSFAEIKH KYLWSEPQNC SATKSNYLRG TGPYPSSMDW 130 140 150 160 170 180 RKKGNVVSPV KNQGACGSCW TFSTTGALES AVAIASGKMM TLAEQQLVDC AQNFNNHGCQ 190 200 210 220 230 240 GGLPSQAFEY ILYNKGIMGE DSYPYIGKNG QCKFNPEKAV AFVKNVVNIT LNDEAAMVEA 250 260 270 280 290 300 VALYNPVSFA FEVTEDFMMY KSGVYSSNSC HKTPDKVNHA VLAVGYGEQN GLLYWIVKNS 310 320 330 WGSNWGNNGY FLIERGKNMC GLAACASYPI PQV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and sequencing of cDNA for rat cathepsin H. Homology in pro-peptide regions of cysteine proteinases." Ishidoh K., Imajoh S., Emori Y., Ohno S., Kawasaki H., Minami Y., Kominami E., Katunuma N., Suzuki K. FEBS Lett. 226:33-37(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Wistar. Tissue: Kidney.
[2]	"Gene structure of rat cathepsin H." Ishidoh K., Kominami E., Katunuma N., Suzuki K. FEBS Lett. 253:103-107(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[4]	"Molecular cloning of rat precursor cathepsin H and the expression of five lysosomal cathepsins in normal tissues and in a rat carcinosarcoma." Qian F., Frankfater A., Miller R.V., Chan S.J., Steiner D.F. Int. J. Biochem. 22:1457-1464(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-333. Tissue: Liver.
[5]	"Homology of amino acid sequences of rat liver cathepsins B and H with that of papain." Takio K., Towatari T., Katunuma N., Teller D.C., Titani K. Proc. Natl. Acad. Sci. U.S.A. 80:3666-3670(1983) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 114-333. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y00708 mRNA. Translation: CAA68699.1. BC085352 mRNA. Translation: AAH85352.1. M38135 mRNA. Translation: AAA63484.1. Different initiation.
IPI	IPI00212809.
PIR	KHRTH. S00211.
RefSeq	NP_037071.1. NM_012939.1.
UniGene	Rn.1997.
3D structure databases
ProteinModelPortal	P00786.
SMR	P00786. Positions 114-333.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000019285.
Protein family/group databases
MEROPS	I29.003.
Proteomic databases
PaxDb	P00786.
PRIDE	P00786.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000019285; ENSRNOP00000019285; ENSRNOG00000014064.
GeneID	25425.
KEGG	rno:25425.
UCSC	RGD:2447. rat.
Organism-specific databases
CTD	1512.
RGD	2447. Ctsh.
Phylogenomic databases
eggNOG	COG4870.
GeneTree	ENSGT00660000095458.
HOGENOM	HOG000230774.
HOVERGEN	HBG011513.
InParanoid	P00786.
KO	K01366.
OMA	STSCHKT.
OrthoDB	EOG4W9J43.
Gene expression databases
Genevestigator	P00786.
GermOnline	ENSRNOG00000014064. Rattus norvegicus.
Family and domain databases
InterPro	IPR025661. Pept_asp_AS. 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. 1 hit. PS00139. THIOL_PROTEASE_CYS. 1 hit. PS00639. THIOL_PROTEASE_HIS. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P00786.
NextBio	606599.

Entry information

Entry name

CATH_RAT

Accession

Primary (citable) accession number: P00786

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	August 1, 1988
Last modified:	April 3, 2013
This is version 120 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program