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Protein

Dipeptidyl peptidase 1

Gene

CTSC

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Cofactori

chlorideBy similarityNote: Binds 1 Cl- ion per heavy chain.By similarity

pH dependencei

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei231By similarity1
Binding sitei275ChlorideBy similarity1
Binding sitei277Chloride; via amide nitrogenBy similarity1
Binding sitei319ChlorideBy similarity1
Active sitei377By similarity1
Active sitei399By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Ligandi

Chloride

Protein family/group databases

MEROPSiC01.070.

Names & Taxonomyi

Protein namesi
Recommended 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:
Alternative name(s):
Dipeptidyl peptidase I exclusion domain chain
Alternative name(s):
Dipeptidyl peptidase I heavy chain 1
Alternative name(s):
Dipeptidyl peptidase I heavy chain 2
Alternative name(s):
Dipeptidyl peptidase I heavy chain 3
Alternative name(s):
Dipeptidyl peptidase I heavy chain 4
Alternative name(s):
Dipeptidyl peptidase I light chain
Gene namesi
Name:CTSC
OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
Proteomesi
  • UP000002254 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000263311 – 109Dipeptidyl peptidase 1 exclusion domain chainBy similarityAdd BLAST109
PropeptideiPRO_0000026332110 – 199By similarityAdd BLAST90
ChainiPRO_0000026333200 – 366Dipeptidyl peptidase 1 heavy chain 1Add BLAST167
ChainiPRO_0000026334201 – 366Dipeptidyl peptidase 1 heavy chain 2Add BLAST166
ChainiPRO_0000026335203 – 366Dipeptidyl peptidase 1 heavy chain 3Add BLAST164
ChainiPRO_0000026336204 – 366Dipeptidyl peptidase 1 heavy chain 4Add BLAST163
ChainiPRO_0000026337367 – 435Dipeptidyl peptidase 1 light chainAdd BLAST69

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi5N-linked (GlcNAc...)By similarity1
Disulfide bondi6 ↔ 93By similarity
Glycosylationi28N-linked (GlcNAc...)By similarity1
Disulfide bondi29 ↔ 111By similarity
Glycosylationi94N-linked (GlcNAc...)By similarity1
Disulfide bondi228 ↔ 271By similarity
Glycosylationi249N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi264 ↔ 304By similarity
Disulfide bondi294 ↔ 309By similarity

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiO97578.
PRIDEiO97578.

Interactioni

Subunit structurei

Tetramer of heterotrimers consisting of exclusion domain, heavy- and light chains.By similarity

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000037626.

Structurei

3D structure databases

ProteinModelPortaliO97578.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1543. Eukaryota.
COG4870. LUCA.
HOGENOMiHOG000068022.
HOVERGENiHBG005248.
InParanoidiO97578.
KOiK01275.

Family and domain databases

Gene3Di2.40.128.80. 1 hit.
InterProiIPR014882. CathepsinC_exc.
IPR033161. DPP_I.
IPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PTHR12411:SF354. PTHR12411:SF354. 1 hit.
PfamiPF08773. CathepsinC_exc. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSiPR00705. PAPAIN.
SMARTiSM00645. Pept_C1. 1 hit.
[Graphical view]
SUPFAMiSSF75001. SSF75001. 1 hit.
PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Sequence processingi: The displayed sequence is further processed into a mature form.

O97578-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
DTPANCTHPE LLGTWVFQVG PAGSRSVNCS VMGPPEKKVV VHLEKLDTAY
60 70 80 90 100
DNFGNTGHFT IIYNQGFEIV LNDYKWFAFF KYKEEGHKVT SYCNETMTGW
110 120 130 140 150
VHDVLGRNWA CFTGTKMGTT SEKAKVNTKH IERLQENNSN RLYKYNYEFV
160 170 180 190 200
KAINTIQKSW TATRYIEYET LTLRDMMTRV GGRKIPRPKP TPLTAEIHEE
210 220 230 240 250
ISRLPTSWDW RNVRGTNFVS PVRNQASCGS CYAFASTAML EARIRILTNN
260 270 280 290 300
TQTPILSPQE IVSCSQYAQG CEGGFPYLIA GKYAQDFGLV EEACFPYAGS
310 320 330 340 350
DSPCKPNDCF RYYSSEYYYV GGFYGACNEA LMKLELVRHG PMAVAFEVYD
360 370 380 390 400
DFFHYQKGIY YHTGLRDPFN PFELTNHAVL LVGYGTDSAS GMDYWIVKNS
410 420 430
WGSRWGEDGY FRIRRGTDEC AIESIAVAAT PIPKL
Length:435
Mass (Da):49,412
Last modified:May 1, 1999 - v1
Checksum:iA80BC7C68CAB0727
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF060171 mRNA. Translation: AAD02704.1.
RefSeqiNP_001182763.1. NM_001195834.1.
UniGeneiCfa.28653.

Genome annotation databases

GeneIDi403458.
KEGGicfa:403458.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF060171 mRNA. Translation: AAD02704.1.
RefSeqiNP_001182763.1. NM_001195834.1.
UniGeneiCfa.28653.

3D structure databases

ProteinModelPortaliO97578.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000037626.

Protein family/group databases

MEROPSiC01.070.

Proteomic databases

PaxDbiO97578.
PRIDEiO97578.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi403458.
KEGGicfa:403458.

Organism-specific databases

CTDi1075.

Phylogenomic databases

eggNOGiKOG1543. Eukaryota.
COG4870. LUCA.
HOGENOMiHOG000068022.
HOVERGENiHBG005248.
InParanoidiO97578.
KOiK01275.

Family and domain databases

Gene3Di2.40.128.80. 1 hit.
InterProiIPR014882. CathepsinC_exc.
IPR033161. DPP_I.
IPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PTHR12411:SF354. PTHR12411:SF354. 1 hit.
PfamiPF08773. CathepsinC_exc. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSiPR00705. PAPAIN.
SMARTiSM00645. Pept_C1. 1 hit.
[Graphical view]
SUPFAMiSSF75001. SSF75001. 1 hit.
PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCATC_CANLF
AccessioniPrimary (citable) accession number: O97578
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: May 1, 1999
Last modified: October 5, 2016
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.