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P80067 (CATC_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Dipeptidyl peptidase 1

EC=3.4.14.1
Alternative name(s):
Cathepsin C
Cathepsin J
Dipeptidyl peptidase I
Short name=DPP-I
Short name=DPPI
Dipeptidyl transferase

Cleaved into the following 3 chains:

  1. Dipeptidyl peptidase 1 exclusion domain chain
    Alternative name(s):
    Dipeptidyl peptidase I exclusion domain chain
  2. Dipeptidyl peptidase 1 heavy chain
    Alternative name(s):
    Dipeptidyl peptidase I heavy chain
  3. Dipeptidyl peptidase 1 light chain
    Alternative name(s):
    Dipeptidyl peptidase I light chain
Gene names
Name:Ctsc
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

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

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.

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

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P80067 [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

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 25-462, SUBUNIT, GLYCOSYLATION AT ASN-29 AND ASN-275, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D90404 mRNA. Translation: BAA14400.1.
PIRA41158.
RefSeqNP_058793.1. NM_017097.1.
UniGeneRn.203177.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JQPX-ray2.40A25-462[»]
ProteinModelPortalP80067.
SMRP80067. Positions 25-462.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000022342.

Protein family/group databases

MEROPSC01.070.

PTM databases

PhosphoSiteP80067.

Proteomic databases

PaxDbP80067.
PRIDEP80067.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000022342; ENSRNOP00000022342; ENSRNOG00000016496.
GeneID25423.
KEGGrno:25423.

Organism-specific databases

CTD1075.
RGD2445. Ctsc.

Phylogenomic databases

eggNOGCOG4870.
GeneTreeENSGT00750000117660.
HOGENOMHOG000068022.
HOVERGENHBG005248.
InParanoidP80067.
KOK01275.
OMAYDDFLHY.
OrthoDBEOG74R1QK.
PhylomeDBP80067.
TreeFamTF313225.

Enzyme and pathway databases

SABIO-RKP80067.

Gene expression databases

GenevestigatorP80067.

Family and domain databases

Gene3D2.40.128.80. 1 hit.
InterProIPR014882. CathepsinC_exc.
IPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
[Graphical view]
PANTHERPTHR12411. PTHR12411. 1 hit.
PfamPF08773. CathepsinC_exc. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSPR00705. PAPAIN.
SMARTSM00645. Pept_C1. 1 hit.
[Graphical view]
SUPFAMSSF75001. SSF75001. 1 hit.
PROSITEPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP80067.
NextBio606591.
PROP80067.

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: April 16, 2014
This is version 127 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references