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Reviewed, UniProtKB/Swiss-Prot P80067 (CATC_RAT)

Last modified June 16, 2009. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

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Names and origin

Protein namesRecommended name:
    Dipeptidyl-peptidase 1
    EC=3.4.14.1
Alternative name(s):
    Dipeptidyl-peptidase I
      Short name=DPP-I
      Short name=DPPI
    Cathepsin C
    Cathepsin J
    Dipeptidyl transferase
Cleaved into the following 3 chains:
    1- Recommended name:
            Dipeptidyl-peptidase 1 exclusion domain chain
        Alternative name(s):
            Dipeptidyl-peptidase I exclusion domain chain
    2- Recommended name:
            Dipeptidyl-peptidase 1 heavy chain
        Alternative name(s):
            Dipeptidyl-peptidase I heavy chain
    3- Recommended name:
            Dipeptidyl-peptidase 1 light chain
        Alternative name(s):
            Dipeptidyl-peptidase I light chain
Gene names
Name: Ctsc
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length462 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Thiol protease. Has dipeptidylpeptidase activity. Can act as both an exopeptidase and endopeptidase By similarity.

Catalytic activity

Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, except when Xaa is Arg or Lys, or Yaa or Zaa is Pro.

Cofactor

Binds 1 chloride ion per heavy chain By similarity.

Subunit structure

Tetramer of heterotrimers consisting of exclusion domain, heavy- and light chains. Ref.4

Subcellular location

Lysosome.

Tissue specificity

Broadly distributed, but higher levels found in liver, spleen, intestine, lung and kidney.

Post-translational modification

N-glycosylated. Ref.4

Sequence similarities

Belongs to the peptidase C1 family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Ref.3
Chain25 – 134110Dipeptidyl-peptidase 1 exclusion domain chain By similarity
PRO_0000026350
Propeptide135 – 22995 By similarity
PRO_0000026351
Chain230 – 393164Dipeptidyl-peptidase 1 heavy chain
PRO_0000026352
Chain394 – 46269Dipeptidyl-peptidase 1 light chain
PRO_0000026353

Sites

Active site2571 By similarity
Active site4041 By similarity
Active site4261 By similarity
Binding site3011Chloride By similarity
Binding site3031Chloride; via amide nitrogen By similarity
Binding site3461Chloride By similarity

Amino acid modifications

Glycosylation291N-linked (GlcNAc...) Ref.4
Glycosylation531N-linked (GlcNAc...) Potential
Glycosylation1441N-linked (GlcNAc...) Potential
Glycosylation2751N-linked (GlcNAc...) Ref.4
Disulfide bond30 ↔ 118 Ref.4
Disulfide bond54 ↔ 136 Ref.4
Disulfide bond254 ↔ 297 Ref.4
Disulfide bond290 ↔ 330 Ref.4
Disulfide bond320 ↔ 336 Ref.4

Experimental info

Sequence conflict301C → E AA sequence Ref.3
Sequence conflict1291V → Y Ref.2
Sequence conflict1711N → H Ref.2
Sequence conflict191 – 1922EE → RR Ref.2
Sequence conflict2631L → I Ref.2

Secondary structure

1 .......................................................... 462
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P80067-1 [UniParc].

Last modified September 5, 2006. Version 3.
Checksum: F25F3953AA115D3C

FASTA46252,235
        10         20         30         40         50         60 
MGPWTHSLRA ALLLVLLGVC TVSSDTPANC TYPDLLGTWV FQVGPRHPRS HINCSVMEPT 

        70         80         90        100        110        120 
EEKVVIHLKK LDTAYDEVGN SGYFTLIYNQ GFEIVLNDYK WFAFFKYEVK GSRAISYCHE 

       130        140        150        160        170        180 
TMTGWVHDVL GRNWACFVGK KMANHSEKVY VNVAHLGGLQ EKYSERLYSH NHNFVKAINS 

       190        200        210        220        230        240 
VQKSWTATTY EEYEKLSIRD LIRRSGHSGR ILRPKPAPIT DEIQQQILSL PESWDWRNVR 

       250        260        270        280        290        300 
GINFVSPVRN QESCGSCYSF ASLGMLEARI RILTNNSQTP ILSPQEVVSC SPYAQGCDGG 

       310        320        330        340        350        360 
FPYLIAGKYA QDFGVVEENC FPYTATDAPC KPKENCLRYY SSEYYYVGGF YGGCNEALMK 

       370        380        390        400        410        420 
LELVKHGPMA VAFEVHDDFL HYHSGIYHHT GLSDPFNPFE LTNHAVLLVG YGKDPVTGLD 

       430        440        450        460 
YWIVKNSWGS QWGESGYFRI RRGTDECAIE SIAMAAIPIP KL

« Hide

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References

[1]"Molecular cloning of cDNA for rat cathepsin C. Cathepsin C, a cysteine proteinase with an extremely long propeptide."
Ishidoh K., Muno D., Sato N., Kominami E.
J. Biol. Chem. 266:16312-16317(1991) [PubMed: 1885565] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The primary structure and tissue distribution of cathepsin C."
Kominami E., Ishidoh K., Muno D., Sato N.
Biol. Chem. Hoppe-Seyler 373:367-373(1992) [PubMed: 1515062] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
Tissue: Kidney.
[3]"Purification and characterization of cathepsin J from rat liver."
Nikawa T., Towatari T., Katunuma N.
Eur. J. Biochem. 204:381-393(1992) [PubMed: 1740150] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-47; 230-251 AND 393-427.
Tissue: Liver.
[4]"Tetrameric dipeptidyl peptidase I directs substrate specificity by use of the residual pro-part domain."
Olsen J.G., Kadziola A., Lauritzen C., Pedersen J., Larsen S., Dahl S.W.
FEBS Lett. 506:201-206(2001) [PubMed: 11602245] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 25-462, SUBUNIT, GLYCOSYLATION AT ASN-29 AND ASN-275, DISULFIDE BONDS.

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Cross-references

Sequence databases

D90404 mRNA. Translation: BAA14400.1.
IPIIPI00193765.
PIRA41158.
RefSeqNP_058793.1.
UniGeneRn.203177

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1JQPX-ray2.40A25-462[»]
ModBaseSearch...

Protein family/group databases

MEROPSC01.070.

Proteomic databases

PRIDEP80067.

Genome annotation databases

EnsemblENSRNOG00000016496. Rattus norvegicus. [Contig view]
GeneID25423.
KEGGrno:25423.

Organism-specific databases

RGD2445. Ctsc.

Phylogenomic databases

HOVERGENP80067.
OMAP80067. ELTNHAV.

Enzyme and pathway databases

BRENDA3.4.14.1. 248.

Gene expression databases

ArrayExpressP80067.
GermOnlineENSRNOG00000016496. Rattus norvegicus.

Family and domain databases

InterProIPR014882. CathepsinC_exc.
IPR000169. Pept_cys_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
[Graphical view]
PANTHERPTHR12411. Peptidase_C1A. 1 hit.
PfamPF08773. CathepsinC_exc. 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

NextBio606591.

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Entry information

Entry nameCATC_RAT
AccessionPrimary (citable) accession number: P80067
Secondary accession number(s): P80068
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: September 5, 2006
Last modified: June 16, 2009
This is version 93 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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