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Protein

Pro-cathepsin H

Gene

Ctsh

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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: RGD
  2. cysteine-type endopeptidase activator activity involved in apoptotic process Source: UniProtKB
  3. cysteine-type endopeptidase activity Source: UniProtKB
  4. HLA-A specific activating MHC class I receptor activity Source: UniProtKB
  5. kininogen binding Source: RGD
  6. protein complex binding Source: RGD
  7. protein self-association Source: RGD
  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. bradykinin catabolic process Source: UniProtKB
  3. cellular response to thyroid hormone stimulus Source: UniProtKB
  4. dichotomous subdivision of terminal units involved in lung branching Source: UniProtKB
  5. ERK1 and ERK2 cascade Source: UniProtKB
  6. immune response-regulating signaling pathway Source: UniProtKB
  7. membrane protein proteolysis Source: UniProtKB
  8. metanephros development Source: UniProtKB
  9. negative regulation of apoptotic process Source: UniProtKB
  10. neuropeptide catabolic process Source: UniProtKB
  11. positive regulation of angiogenesis Source: UniProtKB
  12. positive regulation of apoptotic signaling pathway Source: Ensembl
  13. positive regulation of cell migration Source: UniProtKB
  14. positive regulation of cell proliferation Source: UniProtKB
  15. positive regulation of epithelial cell migration Source: UniProtKB
  16. positive regulation of gene expression Source: UniProtKB
  17. positive regulation of peptidase activity Source: UniProtKB
  18. protein destabilization Source: UniProtKB
  19. proteolysis Source: RGD
  20. response to retinoic acid Source: UniProtKB
  21. spermatogenesis Source: RGD
  22. surfactant homeostasis Source: UniProtKB
  23. T cell mediated cytotoxicity Source: UniProtKB
  24. zymogen activation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Protein family/group databases

MEROPSiC01.040.

Names & Taxonomyi

Protein namesi
Recommended name:
Pro-cathepsin H
Cleaved into the following 4 chains:
Gene namesi
Name:Ctsh
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 8

Organism-specific databases

RGDi2447. Ctsh.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Propeptidei21 – 9575Activation peptidePRO_0000026224Add
BLAST
Chaini96 – 1038Cathepsin H mini chainPRO_0000026225
Propeptidei104 – 11310Sequence AnalysisPRO_0000026226
Chaini114 – 333220Cathepsin HPRO_0000026227Add
BLAST
Chaini114 – 290177Cathepsin H heavy chainPRO_0000026228Add
BLAST
Chaini291 – 33343Cathepsin H light chainPRO_0000026229Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi100 ↔ 325By similarity
Disulfide bondi136 ↔ 179By similarity
Disulfide bondi170 ↔ 212By similarity
Glycosylationi228 – 2281N-linked (GlcNAc...)1 Publication
Disulfide bondi270 ↔ 320By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP00786.
PRIDEiP00786.

Expressioni

Gene expression databases

GenevestigatoriP00786.

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

STRINGi10116.ENSRNOP00000019285.

Structurei

3D structure databases

ProteinModelPortaliP00786.
SMRiP00786. Positions 114-333.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG4870.
GeneTreeiENSGT00760000118871.
HOGENOMiHOG000230774.
HOVERGENiHBG011513.
InParanoidiP00786.
KOiK01366.
OMAiHKYLWSE.
OrthoDBiEOG70KGPX.
PhylomeDBiP00786.
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.

P00786-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MWTALPLLCA GAWLLSAGAT AELTVNAIEK FHFTSWMKQH QKTYSSREYS
60 70 80 90 100
HRLQVFANNW RKIQAHNQRN HTFKMGLNQF SDMSFAEIKH KYLWSEPQNC
110 120 130 140 150
SATKSNYLRG TGPYPSSMDW RKKGNVVSPV KNQGACGSCW TFSTTGALES
160 170 180 190 200
AVAIASGKMM TLAEQQLVDC AQNFNNHGCQ GGLPSQAFEY ILYNKGIMGE
210 220 230 240 250
DSYPYIGKNG QCKFNPEKAV AFVKNVVNIT LNDEAAMVEA VALYNPVSFA
260 270 280 290 300
FEVTEDFMMY KSGVYSSNSC HKTPDKVNHA VLAVGYGEQN GLLYWIVKNS
310 320 330
WGSNWGNNGY FLIERGKNMC GLAACASYPI PQV
Length:333
Mass (Da):37,104
Last modified:August 1, 1988 - v1
Checksum:iA90AC66338F0B744
GO

Sequence cautioni

The sequence AAA63484.1 differs from that shown. Reason: Erroneous initiation. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti287 – 2871G → A.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00708 mRNA. Translation: CAA68699.1.
BC085352 mRNA. Translation: AAH85352.1.
M38135 mRNA. Translation: AAA63484.1. Different initiation.
PIRiS00211. KHRTH.
RefSeqiNP_037071.1. NM_012939.1.
XP_008764662.1. XM_008766440.1.
UniGeneiRn.1997.

Genome annotation databases

EnsembliENSRNOT00000019285; ENSRNOP00000019285; ENSRNOG00000014064.
GeneIDi25425.
KEGGirno:25425.
UCSCiRGD:2447. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00708 mRNA. Translation: CAA68699.1.
BC085352 mRNA. Translation: AAH85352.1.
M38135 mRNA. Translation: AAA63484.1. Different initiation.
PIRiS00211. KHRTH.
RefSeqiNP_037071.1. NM_012939.1.
XP_008764662.1. XM_008766440.1.
UniGeneiRn.1997.

3D structure databases

ProteinModelPortaliP00786.
SMRiP00786. Positions 114-333.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000019285.

Chemistry

BindingDBiP00786.

Protein family/group databases

MEROPSiC01.040.

Proteomic databases

PaxDbiP00786.
PRIDEiP00786.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000019285; ENSRNOP00000019285; ENSRNOG00000014064.
GeneIDi25425.
KEGGirno:25425.
UCSCiRGD:2447. rat.

Organism-specific databases

CTDi1512.
RGDi2447. Ctsh.

Phylogenomic databases

eggNOGiCOG4870.
GeneTreeiENSGT00760000118871.
HOGENOMiHOG000230774.
HOVERGENiHBG011513.
InParanoidiP00786.
KOiK01366.
OMAiHKYLWSE.
OrthoDBiEOG70KGPX.
PhylomeDBiP00786.
TreeFamiTF328985.

Miscellaneous databases

NextBioi606599.
PROiP00786.

Gene expression databases

GenevestigatoriP00786.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiCATH_RAT
AccessioniPrimary (citable) accession number: P00786
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 1, 1988
Last modified: January 7, 2015
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.