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P97821 (CATC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

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

General annotation (Comments)

Function

Thiol protease. Has dipeptidylpeptidase activity. Can act as both an exopeptidase and endopeptidase. Can degrade glucagon. Plays a role in the generation of cytotoxic lymphocyte effector function.

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 By similarity.

Subcellular location

Lysosome.

Tissue specificity

Broadly distributed, but higher levels found in lung, liver, kidney and spleen. Lower levels found in testis and brain.

Sequence similarities

Belongs to the peptidase C1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 134110Dipeptidyl peptidase 1 exclusion domain chain By similarity
PRO_0000026346
Propeptide135 – 23096 By similarity
PRO_0000026347
Chain231 – 393163Dipeptidyl peptidase 1 heavy chain
PRO_0000026348
Chain394 – 46269Dipeptidyl peptidase 1 light chain
PRO_0000026349

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...) Potential
Glycosylation531N-linked (GlcNAc...) Potential
Glycosylation2751N-linked (GlcNAc...) Potential
Disulfide bond30 ↔ 118 By similarity
Disulfide bond54 ↔ 136 By similarity
Disulfide bond254 ↔ 297 By similarity
Disulfide bond290 ↔ 330 By similarity
Disulfide bond320 ↔ 336 By similarity

Sequences

Sequence LengthMass (Da)Tools
P97821 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 56574B38D7DF4710

FASTA46252,376
        10         20         30         40         50         60 
MGPWTHSLRA VLLLVLLGVC TVRSDTPANC TYPDLLGTWV FQVGPRSSRS DINCSVMEAT 

        70         80         90        100        110        120 
EEKVVVHLKK LDTAYDELGN SGHFTLIYNQ GFEIVLNDYK WFAFFKYEVR GHTAISYCHE 

       130        140        150        160        170        180 
TMTGWVHDVL GRNWACFVGK KVESHIEKVN MNAAHLGGLQ ERYSERLYTH NHNFVKAINT 

       190        200        210        220        230        240 
VQKSWTATAY KEYEKMSLRD LIRRSGHSQR IPRPKPAPMT DEIQQQILNL PESWDWRNVQ 

       250        260        270        280        290        300 
GVNYVSPVRN QESCGSCYSF ASMGMLEARI RILTNNSQTP ILSPQEVVSC SPYAQGCDGG 

       310        320        330        340        350        360 
FPYLIAGKYA QDFGVVEESC FPYTAKDSPC KPRENCLRYY SSDYYYVGGF YGGCNEALMK 

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

       430        440        450        460 
YWIIKNSWGS NWGESGYFRI RRGTDECAIE SIAVAAIPIP KL 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning, chromosomal localization, and expression of murine dipeptidyl peptidase I."
Pham C.T.N., Armstrong R.J., Zimonjic D.B., Popescu N.C., Payan D.G., Ley T.J.
J. Biol. Chem. 272:10695-10703(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: 129/SvJ.
[2]"Cloning and characterization of the cDNA encoding mouse dipeptidyl peptidase I (cathepsin C)."
McGuire M.J., Lipsky P.E., Thiele D.L.
Biochim. Biophys. Acta 1351:267-273(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
[3]McGuire M.J., Lipsky P.E., Francisco N.M.C., Thiele D.L.
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[4]"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].
Strain: C57BL/6.
Tissue: Eye.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U89269 mRNA. Translation: AAB49457.1.
U74683 mRNA. Translation: AAB58400.3.
BC067063 mRNA. Translation: AAH67063.1.
RefSeqNP_034112.3. NM_009982.4.
UniGeneMm.322945.

3D structure databases

ProteinModelPortalP97821.
SMRP97821. Positions 25-462.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP97821. 1 interaction.

Chemistry

BindingDBP97821.
ChEMBLCHEMBL3454.

Protein family/group databases

MEROPSC01.070.

PTM databases

PhosphoSiteP97821.

Proteomic databases

PaxDbP97821.
PRIDEP97821.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000032779; ENSMUSP00000032779; ENSMUSG00000030560.
GeneID13032.
KEGGmmu:13032.
UCSCuc009ifu.2. mouse.

Organism-specific databases

CTD1075.
MGIMGI:109553. Ctsc.

Phylogenomic databases

eggNOGCOG4870.
HOGENOMHOG000068022.
HOVERGENHBG005248.
InParanoidP97821.
KOK01275.
OMAYDDFLHY.
OrthoDBEOG74R1QK.
PhylomeDBP97821.
TreeFamTF313225.

Gene expression databases

ArrayExpressP97821.
BgeeP97821.
CleanExMM_CTSC.
GenevestigatorP97821.

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

ChiTaRSCTSC. mouse.
NextBio282904.
PROP97821.
SOURCESearch...

Entry information

Entry nameCATC_MOUSE
AccessionPrimary (citable) accession number: P97821
Secondary accession number(s): O08853
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 1, 1997
Last modified: April 16, 2014
This is version 120 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot