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P80067

- CATC_RAT

UniProt

P80067 - CATC_RAT

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Protein
Dipeptidyl peptidase 1
Gene
Ctsc
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Thiol protease. Has dipeptidylpeptidase activity. Can act as both an exopeptidase and endopeptidase 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

Binds 1 chloride ion per heavy chain By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei257 – 2571 By similarity
Binding sitei301 – 3011Chloride By similarity
Binding sitei303 – 3031Chloride; via amide nitrogen By similarity
Binding sitei346 – 3461Chloride By similarity
Active sitei404 – 4041 By similarity
Active sitei426 – 4261 By similarity

GO - Molecular functioni

  1. chaperone binding Source: ParkinsonsUK-UCL
  2. chloride ion binding Source: RGD
  3. cysteine-type endopeptidase activity Source: RGD
  4. identical protein binding Source: RGD
  5. peptidase activator activity involved in apoptotic process Source: Ensembl
  6. phosphatase binding Source: ParkinsonsUK-UCL
  7. protein self-association Source: RGD
  8. serine-type endopeptidase activity Source: Ensembl

GO - Biological processi

  1. T cell mediated cytotoxicity Source: Ensembl
  2. aging Source: RGD
  3. positive regulation of apoptotic signaling pathway Source: Ensembl
  4. positive regulation of proteolysis involved in cellular protein catabolic process Source: ParkinsonsUK-UCL
  5. proteolysis Source: RGD
  6. response to organic substance Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Ligandi

Chloride

Enzyme and pathway databases

SABIO-RKP80067.

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 1

Organism-specific databases

RGDi2445. Ctsc.

Subcellular locationi

GO - Cellular componenti

  1. Golgi apparatus Source: RGD
  2. endoplasmic reticulum Source: RGD
  3. lysosome Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 24241 Publication
Add
BLAST
Chaini25 – 134110Dipeptidyl peptidase 1 exclusion domain chain By similarity
PRO_0000026350Add
BLAST
Propeptidei135 – 22995 By similarity
PRO_0000026351Add
BLAST
Chaini230 – 393164Dipeptidyl peptidase 1 heavy chain
PRO_0000026352Add
BLAST
Chaini394 – 46269Dipeptidyl peptidase 1 light chain
PRO_0000026353Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi29 – 291N-linked (GlcNAc...)1 Publication
Disulfide bondi30 ↔ 1181 Publication
Glycosylationi53 – 531N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi54 ↔ 1361 Publication
Glycosylationi144 – 1441N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi254 ↔ 2971 Publication
Glycosylationi275 – 2751N-linked (GlcNAc...)1 Publication
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

PhosphoSiteiP80067.

Expressioni

Tissue specificityi

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

Gene expression databases

GenevestigatoriP80067.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000022342.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi32 – 354
Beta strandi36 – 438
Beta strandi62 – 698
Turni70 – 723
Beta strandi73 – 753
Beta strandi77 – 793
Beta strandi81 – 877
Turni88 – 903
Beta strandi91 – 966
Beta strandi99 – 11012
Beta strandi113 – 1219
Beta strandi123 – 1286
Beta strandi133 – 1419
Beta strandi253 – 2553
Helixi257 – 27317
Turni274 – 2763
Helixi284 – 2907
Helixi302 – 3054
Helixi308 – 3125
Beta strandi315 – 3173
Helixi318 – 3203
Beta strandi338 – 3469
Helixi356 – 36611
Beta strandi369 – 3735
Helixi377 – 3804
Beta strandi384 – 3874
Beta strandi404 – 41310
Turni415 – 4173
Beta strandi420 – 4256
Beta strandi437 – 4415
Helixi446 – 4483
Beta strandi454 – 4596

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JQPX-ray2.40A25-462[»]
ProteinModelPortaliP80067.
SMRiP80067. Positions 25-462.

Miscellaneous databases

EvolutionaryTraceiP80067.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG4870.
GeneTreeiENSGT00750000117660.
HOGENOMiHOG000068022.
HOVERGENiHBG005248.
InParanoidiP80067.
KOiK01275.
OMAiYDDFLHY.
OrthoDBiEOG74R1QK.
PhylomeDBiP80067.
TreeFamiTF313225.

Family and domain databases

Gene3Di2.40.128.80. 1 hit.
InterProiIPR014882. CathepsinC_exc.
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.
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: Complete.

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

P80067-1 [UniParc]FASTAAdd to Basket

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MGPWTHSLRA ALLLVLLGVC TVSSDTPANC TYPDLLGTWV FQVGPRHPRS    50
HINCSVMEPT EEKVVIHLKK LDTAYDEVGN SGYFTLIYNQ GFEIVLNDYK 100
WFAFFKYEVK GSRAISYCHE TMTGWVHDVL GRNWACFVGK KMANHSEKVY 150
VNVAHLGGLQ EKYSERLYSH NHNFVKAINS VQKSWTATTY EEYEKLSIRD 200
LIRRSGHSGR ILRPKPAPIT DEIQQQILSL PESWDWRNVR GINFVSPVRN 250
QESCGSCYSF ASLGMLEARI RILTNNSQTP ILSPQEVVSC SPYAQGCDGG 300
FPYLIAGKYA QDFGVVEENC FPYTATDAPC KPKENCLRYY SSEYYYVGGF 350
YGGCNEALMK LELVKHGPMA VAFEVHDDFL HYHSGIYHHT GLSDPFNPFE 400
LTNHAVLLVG YGKDPVTGLD YWIVKNSWGS QWGESGYFRI RRGTDECAIE 450
SIAMAAIPIP KL 462
Length:462
Mass (Da):52,235
Last modified:September 5, 2006 - v3
Checksum:iF25F3953AA115D3C
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 301C → E AA sequence 1 Publication
Sequence conflicti129 – 1291V → Y1 Publication
Sequence conflicti171 – 1711N → H1 Publication
Sequence conflicti191 – 1922EE → RR1 Publication
Sequence conflicti263 – 2631L → I1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D90404 mRNA. Translation: BAA14400.1 .
PIRi A41158.
RefSeqi NP_058793.1. NM_017097.1.
UniGenei Rn.203177.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1JQP X-ray 2.40 A 25-462 [» ]
ProteinModelPortali P80067.
SMRi P80067. Positions 25-462.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000022342.

Protein family/group databases

MEROPSi C01.070.

PTM databases

PhosphoSitei P80067.

Proteomic databases

PaxDbi P80067.
PRIDEi P80067.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000022342 ; ENSRNOP00000022342 ; ENSRNOG00000016496 .
GeneIDi 25423.
KEGGi rno:25423.

Organism-specific databases

CTDi 1075.
RGDi 2445. Ctsc.

Phylogenomic databases

eggNOGi COG4870.
GeneTreei ENSGT00750000117660.
HOGENOMi HOG000068022.
HOVERGENi HBG005248.
InParanoidi P80067.
KOi K01275.
OMAi YDDFLHY.
OrthoDBi EOG74R1QK.
PhylomeDBi P80067.
TreeFami TF313225.

Enzyme and pathway databases

SABIO-RK P80067.

Miscellaneous databases

EvolutionaryTracei P80067.
NextBioi 606591.
PROi P80067.

Gene expression databases

Genevestigatori P80067.

Family and domain databases

Gene3Di 2.40.128.80. 1 hit.
InterProi IPR014882. CathepsinC_exc.
IPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
[Graphical view ]
PANTHERi PTHR12411. PTHR12411. 1 hit.
Pfami PF08773. CathepsinC_exc. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view ]
PRINTSi PR00705. PAPAIN.
SMARTi SM00645. Pept_C1. 1 hit.
[Graphical view ]
SUPFAMi SSF75001. SSF75001. 1 hit.
PROSITEi PS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Molecular cloning of cDNA for rat cathepsin C. Cathepsin C, a cysteine proteinase with an extremely long propeptide."
    Ishidoh K., Muno D., Sato N., Kominami E.
    J. Biol. Chem. 266:16312-16317(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The primary structure and tissue distribution of cathepsin C."
    Kominami E., Ishidoh K., Muno D., Sato N.
    Biol. Chem. Hoppe-Seyler 373:367-373(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.
    Tissue: Kidney.
  3. "Purification and characterization of cathepsin J from rat liver."
    Nikawa T., Towatari T., Katunuma N.
    Eur. J. Biochem. 204:381-393(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 25-47; 230-251 AND 393-427.
    Tissue: Liver.
  4. "Tetrameric dipeptidyl peptidase I directs substrate specificity by use of the residual pro-part domain."
    Olsen J.G., Kadziola A., Lauritzen C., Pedersen J., Larsen S., Dahl S.W.
    FEBS Lett. 506:201-206(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 25-462, SUBUNIT, GLYCOSYLATION AT ASN-29 AND ASN-275, DISULFIDE BONDS.

Entry informationi

Entry nameiCATC_RAT
AccessioniPrimary (citable) accession number: P80067
Secondary accession number(s): P80068
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: September 5, 2006
Last modified: September 3, 2014
This is version 128 of the entry and version 3 of the sequence. [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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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