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P49935 (CATH_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pro-cathepsin H
Alternative name(s):
Cathepsin B3
Cathepsin BA
Gene names
Name:Ctsh
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length333 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Disruption phenotype

Mice exhibit markedly abnormal posterior chamber of eyeball with a configuration suggestive of increased axial lengthening, compared to the rounded appearance in wild-type littermates. Ref.5

Sequence similarities

Belongs to the peptidase C1 family.

Ontologies

Keywords
   Cellular componentLysosome
   DomainSignal
   Molecular functionHydrolase
Protease
Thiol protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processERK1 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: Ensembl

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 apoptotic signaling pathway

Inferred from genetic interaction PubMed 20435891. Source: MGI

positive regulation of cell migration

Inferred from sequence or structural similarity. 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

positive regulation of peptidase activity

Inferred from genetic interaction PubMed 20435891. Source: UniProtKB

protein destabilization

Inferred from mutant phenotype PubMed 17500053. Source: UniProtKB

proteolysis

Inferred from mutant phenotype PubMed 20435891. Source: UniProtKB

response to retinoic acid

Inferred from direct assay PubMed 17500053. Source: UniProtKB

spermatogenesis

Inferred from electronic annotation. Source: Ensembl

surfactant homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

zymogen activation

Inferred from mutant phenotype PubMed 20435891. Source: UniProtKB

   Cellular_componentacrosomal vesicle

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

   Molecular_functionHLA-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

cysteine-type endopeptidase activator activity involved in apoptotic process

Inferred from genetic interaction PubMed 20435891. Source: UniProtKB

cysteine-type endopeptidase activity

Inferred from direct assay PubMed 17500053. Source: UniProtKB

cysteine-type peptidase activity

Inferred from sequence or structural similarity. Source: UniProtKB

endopeptidase activity

Inferred from mutant phenotype PubMed 14766755. Source: UniProtKB

peptidase activator activity involved in apoptotic process

Inferred from genetic interaction PubMed 20435891. Source: MGI

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Propeptide21 – 9575Activation peptide
PRO_0000026212
Chain96 – 1038Cathepsin H mini chain By similarity
PRO_0000026213
Propeptide104 – 11310 Potential
PRO_0000026214
Chain114 – 333220Cathepsin H By similarity
PRO_0000026215
Chain114 – 290177Cathepsin H heavy chain By similarity
PRO_0000026216
Chain291 – 33343Cathepsin H light chain By similarity
PRO_0000026217

Sites

Active site1391 By similarity
Active site2791 By similarity
Active site2991 By similarity

Amino acid modifications

Glycosylation701N-linked (GlcNAc...) Potential
Glycosylation991N-linked (GlcNAc...) Potential
Glycosylation2281N-linked (GlcNAc...) Potential
Disulfide bond100 ↔ 325 By similarity
Disulfide bond136 ↔ 179 By similarity
Disulfide bond170 ↔ 212 By similarity
Disulfide bond270 ↔ 320 By similarity

Experimental info

Sequence conflict1371G → A in AAA82966. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P49935 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 96688394A87CCA36

FASTA33337,170
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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.
[5]"Mutations in LRPAP1 are associated with severe myopia in humans."
Aldahmesh M.A., Khan A.O., Alkuraya H., Adly N., Anazi S., Al-Saleh A.A., Mohamed J.Y., Hijazi H., Prabakaran S., Tacke M., Al-Khrashi A., Hashem M., Reinheckel T., Assiri A., Alkuraya F.S.
Am. J. Hum. Genet. 93:313-320(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
+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.
CCDSCCDS23399.1.
RefSeqNP_031827.2. NM_007801.2.
UniGeneMm.2277.

3D structure databases

ProteinModelPortalP49935.
SMRP49935. Positions 32-333.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP49935. 2 interactions.
MINTMINT-4089943.
STRING10090.ENSMUSP00000034915.

Chemistry

ChEMBLCHEMBL1949491.

Protein family/group databases

MEROPSC01.040.

PTM databases

PhosphoSiteP49935.

Proteomic databases

MaxQBP49935.
PaxDbP49935.
PRIDEP49935.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034915; ENSMUSP00000034915; ENSMUSG00000032359.
GeneID13036.
KEGGmmu:13036.
UCSCuc009qzv.2. mouse.

Organism-specific databases

CTD1512.
MGIMGI:107285. Ctsh.

Phylogenomic databases

eggNOGCOG4870.
GeneTreeENSGT00750000117440.
HOGENOMHOG000230774.
HOVERGENHBG011513.
InParanoidQ3UCD6.
KOK01366.
OMAHKYLWSE.
TreeFamTF328985.

Enzyme and pathway databases

BRENDA3.4.22.16. 2681.

Gene expression databases

ArrayExpressP49935.
BgeeP49935.
CleanExMM_CTSH.
GenevestigatorP49935.

Family and domain databases

InterProIPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERPTHR12411. PTHR12411. 1 hit.
PfamPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSPR00705. PAPAIN.
SMARTSM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio282920.
PROP49935.
SOURCESearch...

Entry information

Entry nameCATH_MOUSE
AccessionPrimary (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: July 9, 2014
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot