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Reviewed, UniProtKB/Swiss-Prot P00786 (CATH_RAT)

Last modified June 16, 2009. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Cathepsin H
    EC=3.4.22.16
Alternative name(s):
    Cathepsin B3
    Cathepsin BA
Cleaved into the following 3 chains:
    1- Recommended name:
            Cathepsin H mini chain
    2- Recommended name:
            Cathepsin H heavy chain
    3- Recommended name:
            Cathepsin H light chain
Gene names
Name: Ctsh
OrganismRattus norvegicus (Rat)
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.

Ontologies

Keywords
   Cellular componentLysosome
   DomainSignal
   Molecular functionHydrolase
Protease
Thiol protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processproteolysis Ref.4

Inferred from expression pattern. Source: RGD

   Cellular componentlysosome Ref.4

Traceable author statement. Source: RGD

   Molecular functioncysteine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

kininogen binding

Inferred from physical interaction. Source: RGD

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
P00786-1 [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: 3691815] [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: 2759235] [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: 15489334] [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: 2276418] [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: 6574504] [Abstract]
Cited for: PROTEIN SEQUENCE OF 114-333.
Tissue: Liver.

Cross-references

Sequence databases

Y00708 mRNA. Translation: CAA68699.1.
BC085352 mRNA. Translation: AAH85352.1.
M38135 mRNA. Translation: AAA63484.1. Different initiation.
IPIIPI00212809.
PIRKHRTH. S00211.
RefSeqNP_037071.1.
UniGeneRn.1997

3D structure databases

HSSPHSSP built from PDB template 8PCH based on UniProtKB O46427.
SMRP00786. Positions 114-333.
ModBaseSearch...

Protein family/group databases

MEROPSC01.040.
I29.003.

Proteomic databases

PRIDEP00786.

Genome annotation databases

EnsemblENSRNOG00000014064. Rattus norvegicus. [Contig view]
GeneID25425.
KEGGrno:25425.

Organism-specific databases

RGD2447. Ctsh.

Phylogenomic databases

HOVERGENP00786.
OMAP00786. HHRLQTF.

Enzyme and pathway databases

BRENDA3.4.22.16. 248.

Gene expression databases

ArrayExpressP00786.
GermOnlineENSRNOG00000014064. Rattus norvegicus.

Family and domain databases

InterProIPR000169. Pept_cys_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERPTHR12411. Peptidase_C1A. 1 hit.
PfamPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSPR00705. PAPAIN.
ProDomPD000158. Peptidase_C1. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00645. 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 Resources

NextBio606599.

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: June 16, 2009
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents