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Q5RB02 (CATC_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length463 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 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.

Sequence similarities

Belongs to the peptidase C1 family.

Ontologies

Keywords
   Cellular componentLysosome
   DomainSignal
   LigandChloride
   Molecular functionHydrolase
Protease
Thiol protease
   PTMGlycoprotein
Zymogen
   Technical termComplete proteome
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

Signal peptide1 – 2424 By similarity
Chain25 – 134110Dipeptidyl peptidase 1 exclusion domain chain
PRO_0000260307
Propeptide135 – 23096 By similarity
PRO_0000260308
Chain231 – 394164Dipeptidyl peptidase 1 heavy chain By similarity
PRO_0000260309
Chain395 – 46369Dipeptidyl peptidase 1 light chain By similarity
PRO_0000260310

Sites

Active site2581 By similarity
Active site4051 By similarity
Active site4271 By similarity
Binding site3021Chloride By similarity
Binding site3041Chloride; via amide nitrogen By similarity
Binding site3471Chloride By similarity

Amino acid modifications

Glycosylation291N-linked (GlcNAc...) Potential
Glycosylation531N-linked (GlcNAc...) Potential
Glycosylation1191N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q5RB02 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: EAB7D3A7CF82C09E

FASTA46351,870
        10         20         30         40         50         60 
MGPGPASLLA ALLLLLSGDR AVRCDTPANC TYLDLLGTWV FQVGSSGSQR DVNCSVMGPQ 

        70         80         90        100        110        120 
EKKVVVHLQK LDTAYDDLGN SGHFTIIYNQ GFEIVLNDYK WFAFFKYKEE GSKVTTYCNE 

       130        140        150        160        170        180 
TMTGWVHDVL GRNWACFTGK KVGTASENVY VNTAHLKNSQ EKYSNRLYKY DHNFVKAINA 

       190        200        210        220        230        240 
IQKSWTATTY KEYETLTLGD MIRRSGGHSR KIPRPKPAPL TAEIQQKVLH LPTSWDWRNI 

       250        260        270        280        290        300 
HGINFVSPVR NQASCGSCYS FASMGMLEAR IRILTSNSQT PILSPQEVVS CSQYAQGCEG 

       310        320        330        340        350        360 
GFPYLIAGKY AQDFGLVEEA CFPYTGTDSP CKMKEDCFRY YSSEYHYVGG FYGGCNEALM 

       370        380        390        400        410        420 
KLELVHHGPM AVAFEVYDDF LHYKKGIYHH TGLRDPFNPF ELTNHAVLLV GYGTDSASGM 

       430        440        450        460 
DYWIVKNSWG TGWGEDGYFR IRRGTDECAI ESIAVAATPI PKL 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Heart.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR858858 mRNA. Translation: CAH91058.1.
RefSeqNP_001125612.1. NM_001132140.1.

3D structure databases

ProteinModelPortalQ5RB02.
SMRQ5RB02. Positions 25-463.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100172530.
KEGGpon:100172530.

Organism-specific databases

CTD1075.

Phylogenomic databases

HOVERGENHBG005248.
InParanoidQ5RB02.
KOK01275.

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...

Entry information

Entry nameCATC_PONAB
AccessionPrimary (citable) accession number: Q5RB02
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: December 21, 2004
Last modified: March 19, 2014
This is version 46 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