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Protein

Dipeptidyl peptidase 1

Gene

Ctsc

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei257By similarity1
Binding sitei301ChlorideBy similarity1
Binding sitei303Chloride; via amide nitrogenBy similarity1
Binding sitei346ChlorideBy similarity1
Active sitei404By similarity1
Active sitei426By similarity1

GO - Molecular functioni

  • chaperone binding Source: ParkinsonsUK-UCL
  • chloride ion binding Source: RGD
  • cysteine-type endopeptidase activity Source: GO_Central
  • cysteine-type peptidase activity Source: RGD
  • identical protein binding Source: RGD
  • peptidase activator activity involved in apoptotic process Source: RGD
  • phosphatase binding Source: ParkinsonsUK-UCL
  • protein self-association Source: RGD
  • serine-type endopeptidase activity Source: RGD

GO - Biological processi

  • aging Source: RGD
  • positive regulation of apoptotic signaling pathway Source: RGD
  • positive regulation of proteolysis involved in cellular protein catabolic process Source: ParkinsonsUK-UCL
  • proteolysis Source: RGD
  • response to organic substance Source: RGD
  • T cell mediated cytotoxicity Source: RGD

Keywordsi

Molecular functionHydrolase, Protease, Thiol protease
LigandChloride

Enzyme and pathway databases

ReactomeiR-RNO-204005 COPII (Coat Protein 2) Mediated Vesicle Transport
R-RNO-2132295 MHC class II antigen presentation
R-RNO-5694530 Cargo concentration in the ER
R-RNO-6798695 Neutrophil degranulation
SABIO-RKiP80067

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 3 chains:
Alternative name(s):
Dipeptidyl peptidase I exclusion domain chain
Alternative name(s):
Dipeptidyl peptidase I heavy chain
Alternative name(s):
Dipeptidyl peptidase I light chain
Gene namesi
Name:Ctsc
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi2445 Ctsc

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Chemistry databases

GuidetoPHARMACOLOGYi2344

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 241 PublicationAdd BLAST24
ChainiPRO_000002635025 – 134Dipeptidyl peptidase 1 exclusion domain chainBy similarityAdd BLAST110
PropeptideiPRO_0000026351135 – 229By similarityAdd BLAST95
ChainiPRO_0000026352230 – 393Dipeptidyl peptidase 1 heavy chainAdd BLAST164
ChainiPRO_0000026353394 – 462Dipeptidyl peptidase 1 light chainAdd BLAST69

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi29N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi30 ↔ 1181 Publication
Glycosylationi53N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi54 ↔ 1361 Publication
Glycosylationi144N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi254 ↔ 2971 Publication
Glycosylationi275N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi290 ↔ 3301 Publication
Disulfide bondi320 ↔ 3361 Publication

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP80067
PRIDEiP80067

PTM databases

iPTMnetiP80067
PhosphoSitePlusiP80067

Expressioni

Tissue specificityi

Broadly distributed, but higher levels found in liver, spleen, intestine, lung and kidney.

Gene expression databases

BgeeiENSRNOG00000016496
GenevisibleiP80067 RN

Interactioni

Subunit structurei

Tetramer of heterotrimers consisting of exclusion domain, heavy- and light chains.1 Publication

GO - Molecular functioni

  • chaperone binding Source: ParkinsonsUK-UCL
  • identical protein binding Source: RGD
  • phosphatase binding Source: ParkinsonsUK-UCL
  • protein self-association Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000022342

Structurei

Secondary structure

1462
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi32 – 35Combined sources4
Beta strandi36 – 43Combined sources8
Beta strandi62 – 69Combined sources8
Turni70 – 72Combined sources3
Beta strandi73 – 75Combined sources3
Beta strandi77 – 79Combined sources3
Beta strandi81 – 87Combined sources7
Turni88 – 90Combined sources3
Beta strandi91 – 96Combined sources6
Beta strandi99 – 110Combined sources12
Beta strandi113 – 121Combined sources9
Beta strandi123 – 128Combined sources6
Beta strandi133 – 141Combined sources9
Beta strandi253 – 255Combined sources3
Helixi257 – 273Combined sources17
Turni274 – 276Combined sources3
Helixi284 – 290Combined sources7
Helixi302 – 305Combined sources4
Helixi308 – 312Combined sources5
Beta strandi315 – 317Combined sources3
Helixi318 – 320Combined sources3
Beta strandi338 – 346Combined sources9
Helixi356 – 366Combined sources11
Beta strandi369 – 373Combined sources5
Helixi377 – 380Combined sources4
Beta strandi384 – 387Combined sources4
Beta strandi404 – 413Combined sources10
Turni415 – 417Combined sources3
Beta strandi420 – 425Combined sources6
Beta strandi437 – 441Combined sources5
Helixi446 – 448Combined sources3
Beta strandi454 – 459Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JQPX-ray2.40A25-462[»]
ProteinModelPortaliP80067
SMRiP80067
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80067

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1543 Eukaryota
COG4870 LUCA
GeneTreeiENSGT00900000140859
HOGENOMiHOG000068022
HOVERGENiHBG005248
InParanoidiP80067
KOiK01275
OMAiYDDFLHY
OrthoDBiEOG091G06TT
PhylomeDBiP80067
TreeFamiTF313225

Family and domain databases

Gene3Di2.40.128.80, 1 hit
InterProiView protein in InterPro
IPR014882 CathepsinC_exc
IPR036496 CathepsinC_exc_dom_sf
IPR025661 Pept_asp_AS
IPR000169 Pept_cys_AS
IPR025660 Pept_his_AS
IPR013128 Peptidase_C1A
IPR000668 Peptidase_C1A_C
PANTHERiPTHR12411 PTHR12411, 1 hit
PfamiView protein in Pfam
PF08773 CathepsinC_exc, 1 hit
PF00112 Peptidase_C1, 1 hit
PRINTSiPR00705 PAPAIN
SMARTiView protein in SMART
SM00645 Pept_C1, 1 hit
SUPFAMiSSF75001 SSF75001, 1 hit
PROSITEiView protein in PROSITE
PS00640 THIOL_PROTEASE_ASN, 1 hit
PS00139 THIOL_PROTEASE_CYS, 1 hit
PS00639 THIOL_PROTEASE_HIS, 1 hit

Sequencei

Sequence statusi: Complete.

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

P80067-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGPWTHSLRA ALLLVLLGVC TVSSDTPANC TYPDLLGTWV FQVGPRHPRS
60 70 80 90 100
HINCSVMEPT EEKVVIHLKK LDTAYDEVGN SGYFTLIYNQ GFEIVLNDYK
110 120 130 140 150
WFAFFKYEVK GSRAISYCHE TMTGWVHDVL GRNWACFVGK KMANHSEKVY
160 170 180 190 200
VNVAHLGGLQ EKYSERLYSH NHNFVKAINS VQKSWTATTY EEYEKLSIRD
210 220 230 240 250
LIRRSGHSGR ILRPKPAPIT DEIQQQILSL PESWDWRNVR GINFVSPVRN
260 270 280 290 300
QESCGSCYSF ASLGMLEARI RILTNNSQTP ILSPQEVVSC SPYAQGCDGG
310 320 330 340 350
FPYLIAGKYA QDFGVVEENC FPYTATDAPC KPKENCLRYY SSEYYYVGGF
360 370 380 390 400
YGGCNEALMK LELVKHGPMA VAFEVHDDFL HYHSGIYHHT GLSDPFNPFE
410 420 430 440 450
LTNHAVLLVG YGKDPVTGLD YWIVKNSWGS QWGESGYFRI RRGTDECAIE
460
SIAMAAIPIP KL
Length:462
Mass (Da):52,235
Last modified:September 5, 2006 - v3
Checksum:iF25F3953AA115D3C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti30C → E AA sequence (PubMed:1740150).Curated1
Sequence conflicti129V → Y (PubMed:1515062).Curated1
Sequence conflicti171N → H (PubMed:1515062).Curated1
Sequence conflicti191 – 192EE → RR (PubMed:1515062).Curated2
Sequence conflicti263L → I (PubMed:1515062).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90404 mRNA Translation: BAA14400.1
PIRiA41158
RefSeqiNP_058793.1, NM_017097.1
UniGeneiRn.203177

Genome annotation databases

EnsembliENSRNOT00000022342; ENSRNOP00000022342; ENSRNOG00000016496
GeneIDi25423
KEGGirno:25423

Similar proteinsi

Entry informationi

Entry nameiCATC_RAT
AccessioniPrimary (citable) accession number: P80067
Secondary accession number(s): P80068
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: September 5, 2006
Last modified: March 28, 2018
This is version 156 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health