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P49935

- CATH_MOUSE

UniProt

P49935 - CATH_MOUSE

Protein

Pro-cathepsin H

Gene

Ctsh

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    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. bradykinin catabolic process Source: UniProtKB
    2. cellular response to thyroid hormone stimulus Source: Ensembl
    3. dichotomous subdivision of terminal units involved in lung branching Source: UniProtKB
    4. ERK1 and ERK2 cascade Source: UniProtKB
    5. immune response-regulating signaling pathway Source: UniProtKB
    6. membrane protein proteolysis Source: UniProtKB
    7. metanephros development Source: UniProtKB
    8. negative regulation of apoptotic process Source: UniProtKB
    9. neuropeptide catabolic process Source: UniProtKB
    10. positive regulation of angiogenesis Source: UniProtKB
    11. positive regulation of apoptotic signaling pathway Source: MGI
    12. positive regulation of cell migration Source: UniProtKB
    13. positive regulation of cell proliferation Source: UniProtKB
    14. positive regulation of epithelial cell migration Source: UniProtKB
    15. positive regulation of gene expression Source: UniProtKB
    16. positive regulation of peptidase activity Source: UniProtKB
    17. protein destabilization Source: UniProtKB
    18. proteolysis Source: UniProtKB
    19. response to retinoic acid Source: UniProtKB
    20. spermatogenesis Source: Ensembl
    21. surfactant homeostasis Source: UniProtKB
    22. T cell mediated cytotoxicity Source: UniProtKB
    23. zymogen activation Source: UniProtKB

    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. lysosome Source: UniProtKB
    6. outer dense fiber Source: Ensembl

    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

    ArrayExpressiP49935.
    BgeeiP49935.
    CleanExiMM_CTSH.
    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.
    GeneTreeiENSGT00750000117440.
    HOGENOMiHOG000230774.
    HOVERGENiHBG011513.
    InParanoidiQ3UCD6.
    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

    MWAALPLLCA GAWLLSTGAT AELTVNAIEK FHFKSWMKQH QKTYSSVEYN    50
    HRLQMFANNW RKIQAHNQRN HTFKMALNQF SDMSFAEIKH KFLWSEPQNC 100
    SATKSNYLRG TGPYPSSMDW RKKGNVVSPV KNQGACGSCW TFSTTGALES 150
    AVAIASGKML SLAEQQLVDC AQAFNNHGCK GGLPSQAFEY ILYNKGIMEE 200
    DSYPYIGKDS SCRFNPQKAV AFVKNVVNIT LNDEAAMVEA VALYNPVSFA 250
    FEVTEDFLMY KSGVYSSKSC HKTPDKVNHA VLAVGYGEQN GLLYWIVKNS 300
    WGSQWGENGY FLIERGKNMC GLAACASYPI PQV 333
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 ENSGT00750000117440.
    HOGENOMi HOG000230774.
    HOVERGENi HBG011513.
    InParanoidi Q3UCD6.
    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

    ArrayExpressi P49935.
    Bgeei P49935.
    CleanExi MM_CTSH.
    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

    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 1, 2014
    This is version 112 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