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O97578 (CATC_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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 6 chains:

  1. Dipeptidyl peptidase 1 exclusion domain chain
    Alternative name(s):
    Dipeptidyl peptidase I exclusion domain chain
  2. Dipeptidyl peptidase 1 heavy chain 1
    Alternative name(s):
    Dipeptidyl peptidase I heavy chain 1
  3. Dipeptidyl peptidase 1 heavy chain 2
    Alternative name(s):
    Dipeptidyl peptidase I heavy chain 2
  4. Dipeptidyl peptidase 1 heavy chain 3
    Alternative name(s):
    Dipeptidyl peptidase I heavy chain 3
  5. Dipeptidyl peptidase 1 heavy chain 4
    Alternative name(s):
    Dipeptidyl peptidase I heavy chain 4
  6. Dipeptidyl peptidase 1 light chain
    Alternative name(s):
    Dipeptidyl peptidase I light chain
Gene names
Name:CTSC
OrganismCanis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis ›

Protein attributes

Sequence length435 AA.
Sequence statusFragment.
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 By similarity.

Subcellular location

Lysosome By similarity.

Post-translational modification

The N-terminus of the heavy chain is heterogeneously processed to produce four different chains.

Sequence similarities

Belongs to the peptidase C1 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 6.5. Active over a broad pH range.

Ontologies

Keywords
   Cellular componentLysosome
   LigandChloride
   Molecular functionHydrolase
Protease
Thiol protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentlysosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncysteine-type peptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 109109Dipeptidyl peptidase 1 exclusion domain chain By similarity
PRO_0000026331
Propeptide110 – 19990 By similarity
PRO_0000026332
Chain200 – 366167Dipeptidyl peptidase 1 heavy chain 1
PRO_0000026333
Chain201 – 366166Dipeptidyl peptidase 1 heavy chain 2
PRO_0000026334
Chain203 – 366164Dipeptidyl peptidase 1 heavy chain 3
PRO_0000026335
Chain204 – 366163Dipeptidyl peptidase 1 heavy chain 4
PRO_0000026336
Chain367 – 43569Dipeptidyl peptidase 1 light chain
PRO_0000026337

Sites

Active site2311 By similarity
Active site3771 By similarity
Active site3991 By similarity
Binding site2751Chloride By similarity
Binding site2771Chloride; via amide nitrogen By similarity
Binding site3191Chloride By similarity

Amino acid modifications

Glycosylation51N-linked (GlcNAc...) By similarity
Glycosylation281N-linked (GlcNAc...) By similarity
Glycosylation941N-linked (GlcNAc...) By similarity
Glycosylation2491N-linked (GlcNAc...) Potential
Disulfide bond6 ↔ 93 By similarity
Disulfide bond29 ↔ 111 By similarity
Disulfide bond228 ↔ 271 By similarity
Disulfide bond264 ↔ 304 By similarity
Disulfide bond294 ↔ 309 By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
O97578 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: A80BC7C68CAB0727

FASTA43549,412
        10         20         30         40         50         60 
DTPANCTHPE LLGTWVFQVG PAGSRSVNCS VMGPPEKKVV VHLEKLDTAY DNFGNTGHFT 

        70         80         90        100        110        120 
IIYNQGFEIV LNDYKWFAFF KYKEEGHKVT SYCNETMTGW VHDVLGRNWA CFTGTKMGTT 

       130        140        150        160        170        180 
SEKAKVNTKH IERLQENNSN RLYKYNYEFV KAINTIQKSW TATRYIEYET LTLRDMMTRV 

       190        200        210        220        230        240 
GGRKIPRPKP TPLTAEIHEE ISRLPTSWDW RNVRGTNFVS PVRNQASCGS CYAFASTAML 

       250        260        270        280        290        300 
EARIRILTNN TQTPILSPQE IVSCSQYAQG CEGGFPYLIA GKYAQDFGLV EEACFPYAGS 

       310        320        330        340        350        360 
DSPCKPNDCF RYYSSEYYYV GGFYGACNEA LMKLELVRHG PMAVAFEVYD DFFHYQKGIY 

       370        380        390        400        410        420 
YHTGLRDPFN PFELTNHAVL LVGYGTDSAS GMDYWIVKNS WGSRWGEDGY FRIRRGTDEC 

       430 
AIESIAVAAT PIPKL

« Hide

References

[1]"Regulated expression, processing, and secretion of dog mast cell dipeptidyl peptidase I."
Wolters P.J., Raymond W.W., Blount J.L., Caughey G.H.
J. Biol. Chem. 273:15514-15520(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-8 AND 199-208.
Tissue: Mast cell.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF060171 mRNA. Translation: AAD02704.1.
RefSeqNP_001182763.1. NM_001195834.1.
UniGeneCfa.28653.

3D structure databases

ProteinModelPortalO97578.
SMRO97578. Positions 1-118.
ModBaseSearch...

Protein family/group databases

MEROPSC01.070.

Proteomic databases

PaxDbO97578.
PRIDEO97578.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID403458.
KEGGcfa:403458.

Organism-specific databases

CTD1075.

Phylogenomic databases

eggNOGCOG4870.
HOGENOMHOG000068022.
HOVERGENHBG005248.
InParanoidO97578.
KOK01275.
OrthoDBEOG4H19VZ.

Family and domain databases

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]
PROSITEPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20816976.

Entry information

Entry nameCATC_CANFA
AccessionPrimary (citable) accession number: O97578
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: May 1, 1999
Last modified: April 3, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

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