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P49935

- CATH_MOUSE

UniProt

P49935 - CATH_MOUSE

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Protein

Pro-cathepsin H

Gene

Ctsh

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

Important for the overall degradation of proteins in lysosomes.

Catalytic activityi

Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-|-Xaa bonds) as well as an endopeptidase.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei139 – 1391By similarity
Active sitei279 – 2791By similarity
Active sitei299 – 2991By similarity

GO - Molecular functioni

  1. aminopeptidase activity Source: UniProtKB
  2. cysteine-type endopeptidase activator activity involved in apoptotic process Source: UniProtKB
  3. cysteine-type endopeptidase activity Source: UniProtKB
  4. cysteine-type peptidase activity Source: UniProtKB
  5. endopeptidase activity Source: UniProtKB
  6. HLA-A specific activating MHC class I receptor activity Source: UniProtKB
  7. peptidase activator activity involved in apoptotic process Source: MGI
  8. serine-type endopeptidase activity Source: UniProtKB
  9. thyroid hormone binding Source: UniProtKB

GO - Biological processi

  1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: GOC
  2. apoptotic process Source: GOC
  3. bradykinin catabolic process Source: UniProtKB
  4. cellular response to thyroid hormone stimulus Source: Ensembl
  5. dichotomous subdivision of terminal units involved in lung branching Source: UniProtKB
  6. ERK1 and ERK2 cascade Source: UniProtKB
  7. immune response-regulating signaling pathway Source: UniProtKB
  8. membrane protein proteolysis Source: UniProtKB
  9. metanephros development Source: UniProtKB
  10. negative regulation of apoptotic process Source: UniProtKB
  11. neuropeptide catabolic process Source: UniProtKB
  12. positive regulation of angiogenesis Source: UniProtKB
  13. positive regulation of apoptotic signaling pathway Source: MGI
  14. positive regulation of cell migration Source: UniProtKB
  15. positive regulation of cell proliferation Source: UniProtKB
  16. positive regulation of epithelial cell migration Source: UniProtKB
  17. positive regulation of gene expression Source: UniProtKB
  18. positive regulation of peptidase activity Source: UniProtKB
  19. protein destabilization Source: UniProtKB
  20. proteolysis Source: UniProtKB
  21. response to retinoic acid Source: UniProtKB
  22. spermatogenesis Source: Ensembl
  23. surfactant homeostasis Source: UniProtKB
  24. T cell mediated cytotoxicity Source: UniProtKB
  25. zymogen activation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Enzyme and pathway databases

BRENDAi3.4.22.16. 2681.

Protein family/group databases

MEROPSiC01.040.

Names & Taxonomyi

Protein namesi
Recommended name:
Pro-cathepsin H
Alternative name(s):
Cathepsin B3
Cathepsin BA
Cleaved into the following 4 chains:
Gene namesi
Name:Ctsh
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:107285. Ctsh.

Subcellular locationi

GO - Cellular componenti

  1. acrosomal vesicle Source: Ensembl
  2. alveolar lamellar body Source: UniProtKB
  3. cytosol Source: UniProtKB
  4. extracellular space Source: UniProtKB
  5. extracellular vesicular exosome Source: Ensembl
  6. lysosome Source: UniProtKB
  7. outer dense fiber Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Propeptidei21 – 9575Activation peptidePRO_0000026212Add
BLAST
Chaini96 – 1038Cathepsin H mini chainBy similarityPRO_0000026213
Propeptidei104 – 11310Sequence AnalysisPRO_0000026214
Chaini114 – 333220Cathepsin HBy similarityPRO_0000026215Add
BLAST
Chaini114 – 290177Cathepsin H heavy chainBy similarityPRO_0000026216Add
BLAST
Chaini291 – 33343Cathepsin H light chainBy similarityPRO_0000026217Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi70 – 701N-linked (GlcNAc...)Sequence Analysis
Glycosylationi99 – 991N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi100 ↔ 325By similarity
Disulfide bondi136 ↔ 179By similarity
Disulfide bondi170 ↔ 212By similarity
Glycosylationi228 – 2281N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi270 ↔ 320By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQBiP49935.
PaxDbiP49935.
PRIDEiP49935.

PTM databases

PhosphoSiteiP49935.

Expressioni

Tissue specificityi

Widely expressed with highest expression found in non-skeletal tissues. Low levels found in skeletal tissue.1 Publication

Gene expression databases

BgeeiP49935.
CleanExiMM_CTSH.
ExpressionAtlasiP49935. baseline and differential.
GenevestigatoriP49935.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

IntActiP49935. 2 interactions.
MINTiMINT-4089943.
STRINGi10090.ENSMUSP00000034915.

Structurei

3D structure databases

ProteinModelPortaliP49935.
SMRiP49935. Positions 32-333.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG4870.
GeneTreeiENSGT00760000118871.
HOGENOMiHOG000230774.
HOVERGENiHBG011513.
InParanoidiP49935.
KOiK01366.
OMAiHKYLWSE.
TreeFamiTF328985.

Family and domain databases

InterProiIPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PfamiPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSiPR00705. PAPAIN.
SMARTiSM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P49935-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MWAALPLLCA GAWLLSTGAT AELTVNAIEK FHFKSWMKQH QKTYSSVEYN
60 70 80 90 100
HRLQMFANNW RKIQAHNQRN HTFKMALNQF SDMSFAEIKH KFLWSEPQNC
110 120 130 140 150
SATKSNYLRG TGPYPSSMDW RKKGNVVSPV KNQGACGSCW TFSTTGALES
160 170 180 190 200
AVAIASGKML SLAEQQLVDC AQAFNNHGCK GGLPSQAFEY ILYNKGIMEE
210 220 230 240 250
DSYPYIGKDS SCRFNPQKAV AFVKNVVNIT LNDEAAMVEA VALYNPVSFA
260 270 280 290 300
FEVTEDFLMY KSGVYSSKSC HKTPDKVNHA VLAVGYGEQN GLLYWIVKNS
310 320 330
WGSQWGENGY FLIERGKNMC GLAACASYPI PQV
Length:333
Mass (Da):37,170
Last modified:July 27, 2011 - v2
Checksum:i96688394A87CCA36
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti137 – 1371G → A in AAA82966. (PubMed:7722423)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS23399.1.
RefSeqiNP_031827.2. NM_007801.2.
UniGeneiMm.2277.

Genome annotation databases

EnsembliENSMUST00000034915; ENSMUSP00000034915; ENSMUSG00000032359.
GeneIDi13036.
KEGGimmu:13036.
UCSCiuc009qzv.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS23399.1.
RefSeqi NP_031827.2. NM_007801.2.
UniGenei Mm.2277.

3D structure databases

ProteinModelPortali P49935.
SMRi P49935. Positions 32-333.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P49935. 2 interactions.
MINTi MINT-4089943.
STRINGi 10090.ENSMUSP00000034915.

Chemistry

ChEMBLi CHEMBL1949491.

Protein family/group databases

MEROPSi C01.040.

PTM databases

PhosphoSitei P49935.

Proteomic databases

MaxQBi P49935.
PaxDbi P49935.
PRIDEi P49935.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000034915 ; ENSMUSP00000034915 ; ENSMUSG00000032359 .
GeneIDi 13036.
KEGGi mmu:13036.
UCSCi uc009qzv.2. mouse.

Organism-specific databases

CTDi 1512.
MGIi MGI:107285. Ctsh.

Phylogenomic databases

eggNOGi COG4870.
GeneTreei ENSGT00760000118871.
HOGENOMi HOG000230774.
HOVERGENi HBG011513.
InParanoidi P49935.
KOi K01366.
OMAi HKYLWSE.
TreeFami TF328985.

Enzyme and pathway databases

BRENDAi 3.4.22.16. 2681.

Miscellaneous databases

NextBioi 282920.
PROi P49935.
SOURCEi Search...

Gene expression databases

Bgeei P49935.
CleanExi MM_CTSH.
ExpressionAtlasi P49935. baseline and differential.
Genevestigatori P49935.

Family and domain databases

InterProi 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 ]
PANTHERi PTHR12411. PTHR12411. 1 hit.
Pfami PF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view ]
PRINTSi PR00705. PAPAIN.
SMARTi SM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view ]
PROSITEi PS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
  5. Cited for: DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiCATH_MOUSE
AccessioniPrimary (citable) accession number: P49935
Secondary accession number(s): Q3UCD6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3