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P80067

- CATC_RAT

UniProt

P80067 - CATC_RAT

Protein

Dipeptidyl peptidase 1

Gene

Ctsc

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 3 (05 Sep 2006)
      Previous versions | rss
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    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

    Binds 1 chloride ion per heavy chain.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei257 – 2571By similarity
    Binding sitei301 – 3011ChlorideBy similarity
    Binding sitei303 – 3031Chloride; via amide nitrogenBy similarity
    Binding sitei346 – 3461ChlorideBy similarity
    Active sitei404 – 4041By similarity
    Active sitei426 – 4261By 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. aging Source: RGD
    2. positive regulation of apoptotic signaling pathway Source: Ensembl
    3. positive regulation of proteolysis involved in cellular protein catabolic process Source: ParkinsonsUK-UCL
    4. proteolysis Source: RGD
    5. response to organic substance Source: RGD
    6. T cell mediated cytotoxicity Source: Ensembl

    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. endoplasmic reticulum Source: RGD
    2. Golgi apparatus Source: RGD
    3. lysosome Source: ParkinsonsUK-UCL

    Keywords - Cellular componenti

    Lysosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 24241 PublicationAdd
    BLAST
    Chaini25 – 134110Dipeptidyl peptidase 1 exclusion domain chainBy similarityPRO_0000026350Add
    BLAST
    Propeptidei135 – 22995By similarityPRO_0000026351Add
    BLAST
    Chaini230 – 393164Dipeptidyl peptidase 1 heavy chainPRO_0000026352Add
    BLAST
    Chaini394 – 46269Dipeptidyl peptidase 1 light chainPRO_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...)Sequence Analysis
    Disulfide bondi54 ↔ 1361 Publication
    Glycosylationi144 – 1441N-linked (GlcNAc...)Sequence Analysis
    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

    1
    462
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP80067.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase C1 family.PROSITE-ProRule annotation

    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

    « Hide

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti30 – 301C → E AA sequence (PubMed:1740150)Curated
    Sequence conflicti129 – 1291V → Y(PubMed:1515062)Curated
    Sequence conflicti171 – 1711N → H(PubMed:1515062)Curated
    Sequence conflicti191 – 1922EE → RR(PubMed:1515062)Curated
    Sequence conflicti263 – 2631L → I(PubMed:1515062)Curated

    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: October 1, 2014
    This is version 129 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