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P00786 (CATH_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
Gene names
Name:Ctsh
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

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

Sequence similarities

Belongs to the peptidase C1 family.

Sequence caution

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

Ontologies

Keywords
   Cellular componentLysosome
   DomainSignal
   Molecular functionHydrolase
Protease
Thiol protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processERK1 and ERK2 cascade

Inferred from sequence or structural similarity. Source: UniProtKB

T cell mediated cytotoxicity

Inferred from sequence or structural similarity. Source: UniProtKB

bradykinin catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to thyroid hormone stimulus

Inferred from expression pattern PubMed 21217776. Source: UniProtKB

dichotomous subdivision of terminal units involved in lung branching

Inferred from sequence or structural similarity. Source: UniProtKB

immune response-regulating signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

membrane protein proteolysis

Inferred from sequence or structural similarity. Source: UniProtKB

metanephros development

Inferred from expression pattern PubMed 16153003. Source: UniProtKB

negative regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

neuropeptide catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of angiogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of epithelial cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of gene expression

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of peptidase activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein destabilization

Inferred from sequence or structural similarity. Source: UniProtKB

proteolysis

Inferred from expression pattern PubMed 11788364. Source: RGD

response to retinoic acid

Inferred from sequence or structural similarity. Source: UniProtKB

spermatogenesis

Inferred from expression pattern PubMed 9238520. Source: RGD

surfactant homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

zymogen activation

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentacrosomal vesicle

Inferred from direct assay PubMed 12838426. Source: RGD

alveolar lamellar body

Inferred from sequence or structural similarity. Source: UniProtKB

axoneme

Inferred from direct assay PubMed 12838426. Source: RGD

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 direct assay PubMed 12838426. Source: RGD

   Molecular_functionHLA-A specific activating MHC class I receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

aminopeptidase activity

Inferred from direct assay PubMed 1483460. Source: RGD

cysteine-type endopeptidase activator activity involved in apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

cysteine-type endopeptidase activity

Inferred from sequence or structural similarity. Source: UniProtKB

kininogen binding

Inferred from physical interaction PubMed 3356189. Source: RGD

protein complex binding

Inferred from physical interaction PubMed 2470410. Source: RGD

protein self-association

Inferred from direct assay PubMed 7550115. Source: RGD

serine-type endopeptidase activity

Inferred from sequence or structural similarity. 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_0000026224
Chain96 – 1038Cathepsin H mini chain
PRO_0000026225
Propeptide104 – 11310 Potential
PRO_0000026226
Chain114 – 333220Cathepsin H
PRO_0000026227
Chain114 – 290177Cathepsin H heavy chain
PRO_0000026228
Chain291 – 33343Cathepsin H light chain
PRO_0000026229

Sites

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

Amino acid modifications

Glycosylation2281N-linked (GlcNAc...) Ref.5
Disulfide bond100 ↔ 325 By similarity
Disulfide bond136 ↔ 179 By similarity
Disulfide bond170 ↔ 212 By similarity
Disulfide bond270 ↔ 320 By similarity

Natural variations

Natural variant2871G → A.

Sequences

Sequence LengthMass (Da)Tools
P00786 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: A90AC66338F0B744

FASTA33337,104
        10         20         30         40         50         60 
MWTALPLLCA GAWLLSAGAT AELTVNAIEK FHFTSWMKQH QKTYSSREYS HRLQVFANNW 

        70         80         90        100        110        120 
RKIQAHNQRN HTFKMGLNQF SDMSFAEIKH KYLWSEPQNC SATKSNYLRG TGPYPSSMDW 

       130        140        150        160        170        180 
RKKGNVVSPV KNQGACGSCW TFSTTGALES AVAIASGKMM TLAEQQLVDC AQNFNNHGCQ 

       190        200        210        220        230        240 
GGLPSQAFEY ILYNKGIMGE DSYPYIGKNG QCKFNPEKAV AFVKNVVNIT LNDEAAMVEA 

       250        260        270        280        290        300 
VALYNPVSFA FEVTEDFMMY KSGVYSSNSC HKTPDKVNHA VLAVGYGEQN GLLYWIVKNS 

       310        320        330 
WGSNWGNNGY FLIERGKNMC GLAACASYPI PQV 

« Hide

References

« Hide 'large scale' references
[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]"Gene structure of rat cathepsin H."
Ishidoh K., Kominami E., Katunuma N., Suzuki K.
FEBS Lett. 253:103-107(1989) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00708 mRNA. Translation: CAA68699.1.
BC085352 mRNA. Translation: AAH85352.1.
M38135 mRNA. Translation: AAA63484.1. Different initiation.
PIRKHRTH. S00211.
RefSeqNP_037071.1. NM_012939.1.
UniGeneRn.1997.

3D structure databases

ProteinModelPortalP00786.
SMRP00786. Positions 114-333.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000019285.

Chemistry

BindingDBP00786.

Protein family/group databases

MEROPSC01.040.

Proteomic databases

PaxDbP00786.
PRIDEP00786.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000019285; ENSRNOP00000019285; ENSRNOG00000014064.
GeneID25425.
KEGGrno:25425.
UCSCRGD:2447. rat.

Organism-specific databases

CTD1512.
RGD2447. Ctsh.

Phylogenomic databases

eggNOGCOG4870.
GeneTreeENSGT00750000117440.
HOGENOMHOG000230774.
HOVERGENHBG011513.
InParanoidP00786.
KOK01366.
OMASTSCHKT.
OrthoDBEOG70KGPX.
PhylomeDBP00786.
TreeFamTF328985.

Gene expression databases

GenevestigatorP00786.

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

NextBio606599.
PROP00786.

Entry information

Entry nameCATH_RAT
AccessionPrimary (citable) accession number: P00786
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 1, 1988
Last modified: April 16, 2014
This is version 128 of the entry and version 1 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