P49935 (CATH_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pro-cathepsin H

Alternative name(s):
Cathepsin B3
Cathepsin BA

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

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [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 › Mus › Mus

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 transcript 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.
Tissue specificity	Widely expressed with highest expression found in non-skeletal tissues. Low levels found in skeletal tissue. Ref.4
Sequence similarities	Belongs to the peptidase C1 family.

Ontologies

Keywords
Cellular component	Lysosome
Domain	Signal
Molecular function	Hydrolase Protease Thiol protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	Complete proteome 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 genetic interaction PubMed 20435891. Source: UniProtKB bradykinin catabolic process Inferred from sequence or structural similarity. Source: UniProtKB cellular response to thyroid hormone stimulus Inferred from electronic annotation. Source: Compara dichotomous subdivision of terminal units involved in lung branching Inferred from mutant phenotype PubMed 17500053. Source: UniProtKB immune response-regulating signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB membrane protein proteolysis Inferred from mutant phenotype PubMed 14766755. Source: UniProtKB metanephros development Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of apoptotic process Inferred from mutant phenotype PubMed 20731543. Source: UniProtKB neuropeptide catabolic process Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of angiogenesis Inferred from mutant phenotype PubMed 20731543. Source: UniProtKB positive regulation of cell proliferation Inferred from mutant phenotype PubMed 20731543. Source: UniProtKB positive regulation of epithelial cell migration Inferred from mutant phenotype PubMed 17500053. Source: UniProtKB positive regulation of gene expression Inferred from sequence or structural similarity. Source: UniProtKB protein destabilization Inferred from mutant phenotype PubMed 17500053. Source: UniProtKB response to retinoic acid Inferred from direct assay PubMed 17500053. Source: UniProtKB spermatogenesis Inferred from electronic annotation. Source: Compara surfactant homeostasis Inferred from sequence or structural similarity. Source: UniProtKB zymogen activation Inferred from mutant phenotype PubMed 20435891. Source: UniProtKB
Cellular_component	acrosomal vesicle Inferred from electronic annotation. Source: Compara alveolar lamellar body Inferred from sequence or structural similarity. Source: UniProtKB 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 electronic annotation. Source: Compara
Molecular_function	HLA-A specific activating MHC class I receptor activity Inferred from sequence or structural similarity. Source: UniProtKB aminopeptidase activity Inferred from sequence or structural similarity. Source: UniProtKB apoptotic protease activator activity Inferred from genetic interaction PubMed 20435891. Source: UniProtKB cysteine-type endopeptidase activity Inferred from direct assay PubMed 17500053. Source: UniProtKB serine-type endopeptidase activity Inferred from mutant phenotype PubMed 20435891. 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_0000026212
	Chain	96 – 103	8	Cathepsin H mini chain By similarity		PRO_0000026213
	Propeptide	104 – 113	10	Potential		PRO_0000026214
	Chain	114 – 333	220	Cathepsin H By similarity		PRO_0000026215
	Chain	114 – 290	177	Cathepsin H heavy chain By similarity		PRO_0000026216
	Chain	291 – 333	43	Cathepsin H light chain By similarity		PRO_0000026217
Sites
	Active site	139	1	By similarity
	Active site	279	1	By similarity
	Active site	299	1	By similarity
Amino acid modifications
	Glycosylation	70	1	N-linked (GlcNAc...) Potential
	Glycosylation	99	1	N-linked (GlcNAc...) Potential
	Glycosylation	228	1	N-linked (GlcNAc...) Potential
	Disulfide bond	100 ↔ 325		By similarity
	Disulfide bond	136 ↔ 179		By similarity
	Disulfide bond	170 ↔ 212		By similarity
	Disulfide bond	270 ↔ 320		By similarity
Experimental info
	Sequence conflict	137	1	G → A in AAA82966. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P49935 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 96688394A87CCA36	FASTA	333	37,170
	10 20 30 40 50 60 MWAALPLLCA GAWLLSTGAT AELTVNAIEK FHFKSWMKQH QKTYSSVEYN HRLQMFANNW 70 80 90 100 110 120 RKIQAHNQRN HTFKMALNQF SDMSFAEIKH KFLWSEPQNC SATKSNYLRG TGPYPSSMDW 130 140 150 160 170 180 RKKGNVVSPV KNQGACGSCW TFSTTGALES AVAIASGKML SLAEQQLVDC AQAFNNHGCK 190 200 210 220 230 240 GGLPSQAFEY ILYNKGIMEE DSYPYIGKDS SCRFNPQKAV AFVKNVVNIT LNDEAAMVEA 250 260 270 280 290 300 VALYNPVSFA FEVTEDFLMY KSGVYSSKSC HKTPDKVNHA VLAVGYGEQN GLLYWIVKNS 310 320 330 WGSQWGENGY FLIERGKNMC GLAACASYPI PQV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"IFN-gamma increases cathepsin H mRNA levels in mouse macrophages." Lafuse W.P., Brown D., Castle L., Zwilling B.S. J. Leukoc. Biol. 57:663-669(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Bone marrow and Spleen.
[3]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"Cathepsin expression during skeletal development." Soederstroem M., Salminen H., Glumoff V., Kirschke H., Aro H., Vuorio E. Biochim. Biophys. Acta 1446:35-46(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 136-301, TISSUE SPECIFICITY. Strain: C57BL/6. Tissue: Cartilage.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U06119 mRNA. Translation: AAA82966.1. AK149949 mRNA. Translation: BAE29188.1. AK150583 mRNA. Translation: BAE29677.1. AK157376 mRNA. Translation: BAE34071.1. AK160026 mRNA. Translation: BAE35569.1. CH466560 Genomic DNA. Translation: EDL20901.1. Y18464 mRNA. Translation: CAA77182.1.
IPI	IPI00118987.
RefSeq	NP_031827.2. NM_007801.2.
UniGene	Mm.2277.
3D structure databases
ProteinModelPortal	P49935.
SMR	P49935. Positions 32-333.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-4089943.
STRING	10090.ENSMUSP00000034915.
Protein family/group databases
MEROPS	I29.003.
PTM databases
PhosphoSite	P49935.
Proteomic databases
PaxDb	P49935.
PRIDE	P49935.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000034915; ENSMUSP00000034915; ENSMUSG00000032359.
GeneID	13036.
KEGG	mmu:13036.
UCSC	uc009qzv.2. mouse.
Organism-specific databases
CTD	1512.
MGI	MGI:107285. Ctsh.
Phylogenomic databases
eggNOG	COG4870.
GeneTree	ENSGT00660000095458.
HOGENOM	HOG000230774.
HOVERGEN	HBG011513.
InParanoid	Q3UCD6.
KO	K01366.
OMA	STSCHKT.
OrthoDB	EOG4W9J43.
Enzyme and pathway databases
BRENDA	3.4.22.16. 2681.
Gene expression databases
ArrayExpress	P49935.
Bgee	P49935.
CleanEx	MM_CTSH.
Genevestigator	P49935.
GermOnline	ENSMUSG00000032359. Mus musculus.
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
ChEMBL	CHEMBL1949491.
NextBio	282920.
SOURCE	Search...

Entry information

Entry name

CATH_MOUSE

Accession

Primary (citable) accession number: P49935
Secondary accession number(s): Q3UCD6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	July 27, 2011
Last modified:	May 29, 2013
This is version 100 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program