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P53634

- CATC_HUMAN

UniProt

P53634 - CATC_HUMAN

Protein

Dipeptidyl peptidase 1

Gene

CTSC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 2 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII.1 Publication

    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.

    Enzyme regulationi

    Strongly inhibited by the cysteine peptidase inhibitors mersalyl acid, iodoacetic acid and cystatin. Inhibited by N-ethylmaleimide, Gly-Phe-diazomethane, TLCK, TPCK and, at low pH, by dithiodipyridine. Not inhibited by the serine peptidase inhibitor PMSF, the aminopeptidase inhibitor bestatin, or metal ion chelators.1 Publication

    pH dependencei

    High activity at pH 4.5-6.8.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei258 – 2581
    Binding sitei302 – 3021Chloride
    Binding sitei304 – 3041Chloride; via amide nitrogen
    Binding sitei347 – 3471Chloride
    Active sitei405 – 4051
    Active sitei427 – 4271

    GO - Molecular functioni

    1. chaperone binding Source: BHF-UCL
    2. chloride ion binding Source: Ensembl
    3. cysteine-type peptidase activity Source: UniProtKB
    4. peptidase activator activity involved in apoptotic process Source: Ensembl
    5. phosphatase binding Source: BHF-UCL
    6. protein binding Source: IntAct
    7. serine-type endopeptidase activity Source: Ensembl

    GO - Biological processi

    1. aging Source: Ensembl
    2. immune response Source: ProtInc
    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: UniProtKB
    6. response to organic substance Source: Ensembl
    7. T cell mediated cytotoxicity Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Ligandi

    Chloride

    Enzyme and pathway databases

    BioCyciMetaCyc:HS03265-MONOMER.
    ReactomeiREACT_121399. MHC class II antigen presentation.
    SABIO-RKP53634.

    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
    Synonyms:CPPI
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:2528. CTSC.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: Ensembl
    2. extracellular space Source: UniProt
    3. extracellular vesicular exosome Source: UniProt
    4. Golgi apparatus Source: Ensembl
    5. lysosome Source: UniProtKB
    6. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Lysosome

    Pathology & Biotechi

    Involvement in diseasei

    Papillon-Lefevre syndrome (PLS) [MIM:245000]: An autosomal recessive disorder characterized by palmoplantar keratosis and severe periodontitis affecting deciduous and permanent dentitions and resulting in premature tooth loss. The palmoplantar keratotic phenotype vary from mild psoriasiform scaly skin to overt hyperkeratosis. Keratosis also affects other sites such as elbows and knees.12 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti39 – 391W → S in PLS. 1 Publication
    VAR_016933
    Natural varianti67 – 748Missing in PLS.
    VAR_019035
    Natural varianti127 – 1271H → P in PLS. 1 Publication
    VAR_016934
    Natural varianti129 – 1291V → E in PLS. 1 Publication
    VAR_019036
    Natural varianti139 – 1391G → R in PLS. 2 Publications
    VAR_019037
    Natural varianti236 – 2361D → Y in PLS. 2 Publications
    VAR_019038
    Natural varianti249 – 2491V → F in PLS. 2 Publications
    VAR_009541
    Natural varianti252 – 2521Q → L in PLS. 2 Publications
    VAR_009542
    Natural varianti272 – 2721R → H in PLS. 1 Publication
    VAR_019039
    Natural varianti272 – 2721R → P in PLS. 5 Publications
    VAR_009543
    Natural varianti286 – 2861Q → R in HMS and PLS. 2 Publications
    VAR_016935
    Natural varianti291 – 2911C → Y in PLS. 1 Publication
    VAR_019040
    Natural varianti294 – 2941Y → H in PLS. 1 Publication
    VAR_039686
    Natural varianti300 – 3001G → D in PLS. 1 Publication
    VAR_019041
    Natural varianti300 – 3001G → S in PLS. 1 Publication
    VAR_019042
    Natural varianti301 – 3011G → S in PLS. 4 Publications
    VAR_009544
    Natural varianti301 – 3011G → V in PLS. 1 Publication
    VAR_019043
    Natural varianti304 – 3041Y → N in PLS. 1 Publication
    VAR_019044
    Natural varianti312 – 3121Q → R in PLS. 1 Publication
    VAR_019045
    Natural varianti319 – 3191E → G in PLS. 1 Publication
    VAR_019046
    Natural varianti339 – 3391R → C in PLS. 5 Publications
    VAR_009545
    Natural varianti340 – 3401Y → C in PLS. 2 Publications
    VAR_016944
    Natural varianti347 – 3471Y → C in PLS and AP1. 3 Publications
    VAR_009546
    Natural varianti405 – 4051H → N in PLS. 1 Publication
    VAR_027249
    Natural varianti405 – 4051H → R in PLS. 1 Publication
    Corresponds to variant rs151269219 [ dbSNP | Ensembl ].
    VAR_027250
    Natural varianti429 – 4291W → C in PLS. 1 Publication
    VAR_016936
    Natural varianti447 – 4471E → G in PLS. 2 Publications
    VAR_019048
    Haim-Munk syndrome (HMS) [MIM:245010]: An autosomal recessive disorder characterized by palmoplantar keratosis, onychogryphosis and periodontitis. Additional features are pes planus, arachnodactyly, and acroosteolysis.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti286 – 2861Q → R in HMS and PLS. 2 Publications
    VAR_016935
    Periodontititis, aggressive, 1 (AP1) [MIM:170650]: A disease characterized by severe and protracted gingival infections, generalized or localized, leading to tooth loss. Amounts of microbial deposits are generally inconsistent with the severity of periodontal tissue destruction and the progression of attachment and bone loss may be self arresting.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti347 – 3471Y → C in PLS and AP1. 3 Publications
    VAR_009546
    Natural varianti412 – 4121Y → C in AP1. 1 Publication
    Corresponds to variant rs28937571 [ dbSNP | Ensembl ].
    VAR_019047

    Keywords - Diseasei

    Disease mutation, Palmoplantar keratoderma

    Organism-specific databases

    MIMi170650. phenotype.
    245000. phenotype.
    245010. phenotype.
    Orphaneti2342. Haim-Munk syndrome.
    678. Papillon-Lefevre syndrome.
    PharmGKBiPA27028.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 24243 PublicationsAdd
    BLAST
    Chaini25 – 134110Dipeptidyl peptidase 1 exclusion domain chainPRO_0000026338Add
    BLAST
    Propeptidei135 – 230963 PublicationsPRO_0000026339Add
    BLAST
    Chaini231 – 394164Dipeptidyl peptidase 1 heavy chainPRO_0000026340Add
    BLAST
    Chaini395 – 46369Dipeptidyl peptidase 1 light chainPRO_0000026341Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi29 – 291N-linked (GlcNAc...)2 Publications
    Disulfide bondi30 ↔ 118
    Glycosylationi53 – 531N-linked (GlcNAc...)2 Publications
    Disulfide bondi54 ↔ 136
    Glycosylationi119 – 1191N-linked (GlcNAc...)1 Publication
    Disulfide bondi255 ↔ 298
    Glycosylationi276 – 2761N-linked (GlcNAc...)1 Publication
    Disulfide bondi291 ↔ 331
    Disulfide bondi321 ↔ 337

    Post-translational modificationi

    N-glycosylated. While glycosylation at Asn-53, Asn-119 and Asn-276 is mediated by STT3A-containing complexes, glycosylation at Asn-29 is mediated STT3B-containing complexes.5 Publications
    In approximately 50% of the complexes the exclusion domain is cleaved at position 58 or 61. The two parts of the exclusion domain are held together by a disulfide bond.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    MaxQBiP53634.
    PaxDbiP53634.
    PRIDEiP53634.

    PTM databases

    PhosphoSiteiP53634.

    Miscellaneous databases

    PMAP-CutDBP53634.

    Expressioni

    Tissue specificityi

    Ubiquitous. Highly expressed in lung, kidney and placenta. Detected at intermediate levels in colon, small intestine, spleen and pancreas.1 Publication

    Inductioni

    Up-regulated in lymphocytes by IL2/interleukin-2.1 Publication

    Gene expression databases

    ArrayExpressiP53634.
    BgeeiP53634.
    GenevestigatoriP53634.

    Organism-specific databases

    HPAiCAB025364.

    Interactioni

    Subunit structurei

    Tetramer of heterotrimers consisting of exclusion domain, heavy- and light chains.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CST7O760962EBI-1047323,EBI-2807448

    Protein-protein interaction databases

    BioGridi107502. 12 interactions.
    IntActiP53634. 8 interactions.
    MINTiMINT-4655964.

    Structurei

    Secondary structure

    1
    463
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi32 – 354
    Beta strandi36 – 4813
    Turni49 – 513
    Helixi54 – 563
    Beta strandi60 – 6910
    Turni70 – 723
    Beta strandi73 – 764
    Beta strandi81 – 877
    Turni88 – 903
    Beta strandi91 – 966
    Beta strandi99 – 11012
    Beta strandi113 – 1219
    Beta strandi123 – 1286
    Beta strandi133 – 1419
    Beta strandi254 – 2563
    Helixi258 – 27518
    Helixi285 – 2917
    Helixi297 – 2993
    Helixi303 – 3064
    Helixi309 – 3135
    Helixi319 – 3213
    Beta strandi342 – 3476
    Helixi357 – 36711
    Beta strandi370 – 3745
    Helixi378 – 3825
    Beta strandi385 – 3884
    Beta strandi405 – 41410
    Turni416 – 4183
    Beta strandi421 – 4266
    Beta strandi431 – 4333
    Beta strandi438 – 4425
    Turni443 – 4464
    Helixi447 – 4493
    Beta strandi455 – 4595

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1K3BX-ray2.15A25-143[»]
    B231-394[»]
    C395-463[»]
    2DJFX-ray2.00A25-143[»]
    B231-394[»]
    C395-463[»]
    2DJGX-ray2.05A25-143[»]
    B231-394[»]
    C395-463[»]
    3PDFX-ray1.85A25-463[»]
    4CDCX-ray2.40A/D/G/J25-143[»]
    B/E/H/K230-394[»]
    C/F/I/L395-463[»]
    4CDDX-ray2.35A/D25-144[»]
    B/E230-394[»]
    C/F395-463[»]
    4CDEX-ray2.40A/D25-143[»]
    B/E230-394[»]
    C/F395-463[»]
    4CDFX-ray2.20A/D25-144[»]
    B/E229-394[»]
    C/F395-463[»]
    ProteinModelPortaliP53634.
    SMRiP53634. Positions 25-142, 174-463.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP53634.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase C1 family.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG4870.
    HOGENOMiHOG000127503.
    HOVERGENiHBG005248.
    InParanoidiP53634.
    KOiK01275.
    OMAiYDDFLHY.
    OrthoDBiEOG74R1QK.
    PhylomeDBiP53634.
    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]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P53634-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MGAGPSLLLA ALLLLLSGDG AVRCDTPANC TYLDLLGTWV FQVGSSGSQR    50
    DVNCSVMGPQ EKKVVVYLQK LDTAYDDLGN SGHFTIIYNQ GFEIVLNDYK 100
    WFAFFKYKEE GSKVTTYCNE TMTGWVHDVL GRNWACFTGK KVGTASENVY 150
    VNIAHLKNSQ EKYSNRLYKY DHNFVKAINA IQKSWTATTY MEYETLTLGD 200
    MIRRSGGHSR KIPRPKPAPL TAEIQQKILH LPTSWDWRNV HGINFVSPVR 250
    NQASCGSCYS FASMGMLEAR IRILTNNSQT PILSPQEVVS CSQYAQGCEG 300
    GFPYLIAGKY AQDFGLVEEA CFPYTGTDSP CKMKEDCFRY YSSEYHYVGG 350
    FYGGCNEALM KLELVHHGPM AVAFEVYDDF LHYKKGIYHH TGLRDPFNPF 400
    ELTNHAVLLV GYGTDSASGM DYWIVKNSWG TGWGENGYFR IRRGTDECAI 450
    ESIAVAATPI PKL 463
    Length:463
    Mass (Da):51,854
    Last modified:January 11, 2011 - v2
    Checksum:i4C9C7C24D900CEE6
    GO
    Isoform 2 (identifier: P53634-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         107-137: YKEEGSKVTTYCNETMTGWVHDVLGRNWACF → DVTDFISHLFMQLGTVGIYDLPHLRNKLVIK
         138-463: Missing.

    Show »
    Length:137
    Mass (Da):15,169
    Checksum:iC68FC076FCB30601
    GO
    Isoform 3 (identifier: P53634-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         107-141: YKEEGSKVTTYCNETMTGWVHDVLGRNWACFTGKK → DVTDFISHLFMQLGTVGIYDLPHLRNKLAMNRRWG
         142-463: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:141
    Mass (Da):15,700
    Checksum:iFAD4B1B511F91F66
    GO

    Sequence cautioni

    The sequence CAD97897.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti63 – 631K → I in BAD96758. 1 PublicationCurated
    Sequence conflicti237 – 2371W → V AA sequence (PubMed:1586157)Curated
    Sequence conflicti321 – 3211C → S AA sequence (PubMed:1586157)Curated
    Sequence conflicti355 – 3551C → M AA sequence (PubMed:1586157)Curated
    Sequence conflicti366 – 3661H → R AA sequence (PubMed:1586157)Curated
    Sequence conflicti376 – 3783VYD → YVY AA sequence (PubMed:1586157)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti39 – 391W → S in PLS. 1 Publication
    VAR_016933
    Natural varianti67 – 748Missing in PLS.
    VAR_019035
    Natural varianti127 – 1271H → P in PLS. 1 Publication
    VAR_016934
    Natural varianti129 – 1291V → E in PLS. 1 Publication
    VAR_019036
    Natural varianti139 – 1391G → R in PLS. 2 Publications
    VAR_019037
    Natural varianti153 – 1531I → T.12 Publications
    Corresponds to variant rs217086 [ dbSNP | Ensembl ].
    VAR_016943
    Natural varianti236 – 2361D → Y in PLS. 2 Publications
    VAR_019038
    Natural varianti249 – 2491V → F in PLS. 2 Publications
    VAR_009541
    Natural varianti252 – 2521Q → L in PLS. 2 Publications
    VAR_009542
    Natural varianti272 – 2721R → H in PLS. 1 Publication
    VAR_019039
    Natural varianti272 – 2721R → P in PLS. 5 Publications
    VAR_009543
    Natural varianti286 – 2861Q → R in HMS and PLS. 2 Publications
    VAR_016935
    Natural varianti291 – 2911C → Y in PLS. 1 Publication
    VAR_019040
    Natural varianti294 – 2941Y → H in PLS. 1 Publication
    VAR_039686
    Natural varianti300 – 3001G → D in PLS. 1 Publication
    VAR_019041
    Natural varianti300 – 3001G → S in PLS. 1 Publication
    VAR_019042
    Natural varianti301 – 3011G → S in PLS. 4 Publications
    VAR_009544
    Natural varianti301 – 3011G → V in PLS. 1 Publication
    VAR_019043
    Natural varianti304 – 3041Y → N in PLS. 1 Publication
    VAR_019044
    Natural varianti312 – 3121Q → R in PLS. 1 Publication
    VAR_019045
    Natural varianti319 – 3191E → G in PLS. 1 Publication
    VAR_019046
    Natural varianti339 – 3391R → C in PLS. 5 Publications
    VAR_009545
    Natural varianti340 – 3401Y → C in PLS. 2 Publications
    VAR_016944
    Natural varianti347 – 3471Y → C in PLS and AP1. 3 Publications
    VAR_009546
    Natural varianti401 – 4011E → K.1 Publication
    VAR_016945
    Natural varianti405 – 4051H → N in PLS. 1 Publication
    VAR_027249
    Natural varianti405 – 4051H → R in PLS. 1 Publication
    Corresponds to variant rs151269219 [ dbSNP | Ensembl ].
    VAR_027250
    Natural varianti412 – 4121Y → C in AP1. 1 Publication
    Corresponds to variant rs28937571 [ dbSNP | Ensembl ].
    VAR_019047
    Natural varianti429 – 4291W → C in PLS. 1 Publication
    VAR_016936
    Natural varianti447 – 4471E → G in PLS. 2 Publications
    VAR_019048
    Natural varianti453 – 4531I → V Rare polymorphism. 1 Publication
    Corresponds to variant rs3888798 [ dbSNP | Ensembl ].
    VAR_016946

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei107 – 14135YKEEG…FTGKK → DVTDFISHLFMQLGTVGIYD LPHLRNKLAMNRRWG in isoform 3. 1 PublicationVSP_043232Add
    BLAST
    Alternative sequencei107 – 13731YKEEG…NWACF → DVTDFISHLFMQLGTVGIYD LPHLRNKLVIK in isoform 2. 3 PublicationsVSP_039123Add
    BLAST
    Alternative sequencei138 – 463326Missing in isoform 2. 3 PublicationsVSP_039124Add
    BLAST
    Alternative sequencei142 – 463322Missing in isoform 3. 1 PublicationVSP_043233Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X87212 mRNA. Translation: CAA60671.1.
    U79415 Genomic DNA. Translation: AAC51341.1.
    AF234263 mRNA. Translation: AAL48191.1.
    AF234264 mRNA. Translation: AAL48192.1.
    AF254757 mRNA. Translation: AAL48195.1.
    AF525032 mRNA. Translation: AAQ08887.1.
    AF525033 mRNA. Translation: AAQ08888.1.
    AK292117 mRNA. Translation: BAF84806.1.
    AK311923 mRNA. Translation: BAG34864.1.
    AK223038 mRNA. Translation: BAD96758.1.
    BX537913 mRNA. Translation: CAD97897.1. Different initiation.
    AC011088 Genomic DNA. No translation available.
    CH471185 Genomic DNA. Translation: EAW59364.1.
    BC054028 mRNA. Translation: AAH54028.1.
    BC100891 mRNA. Translation: AAI00892.1.
    BC100892 mRNA. Translation: AAI00893.1.
    BC100893 mRNA. Translation: AAI00894.1.
    BC100894 mRNA. Translation: AAI00895.1.
    BC109386 mRNA. Translation: AAI09387.1.
    BC110071 mRNA. Translation: AAI10072.1.
    BC113850 mRNA. Translation: AAI13851.1.
    BC113897 mRNA. Translation: AAI13898.1.
    CCDSiCCDS31654.1. [P53634-2]
    CCDS44693.1. [P53634-3]
    CCDS8282.1. [P53634-1]
    PIRiS23941.
    S66504.
    RefSeqiNP_001107645.1. NM_001114173.1. [P53634-3]
    NP_001805.3. NM_001814.4.
    NP_680475.1. NM_148170.3. [P53634-2]
    UniGeneiHs.128065.

    Genome annotation databases

    EnsembliENST00000227266; ENSP00000227266; ENSG00000109861. [P53634-1]
    ENST00000524463; ENSP00000432541; ENSG00000109861. [P53634-2]
    ENST00000529974; ENSP00000433539; ENSG00000109861. [P53634-3]
    GeneIDi1075.
    KEGGihsa:1075.
    UCSCiuc001pck.4. human. [P53634-1]
    uc001pcm.4. human. [P53634-2]
    uc001pcn.4. human. [P53634-3]

    Polymorphism databases

    DMDMi317373330.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    CTSCbase

    CTSC mutation db

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X87212 mRNA. Translation: CAA60671.1 .
    U79415 Genomic DNA. Translation: AAC51341.1 .
    AF234263 mRNA. Translation: AAL48191.1 .
    AF234264 mRNA. Translation: AAL48192.1 .
    AF254757 mRNA. Translation: AAL48195.1 .
    AF525032 mRNA. Translation: AAQ08887.1 .
    AF525033 mRNA. Translation: AAQ08888.1 .
    AK292117 mRNA. Translation: BAF84806.1 .
    AK311923 mRNA. Translation: BAG34864.1 .
    AK223038 mRNA. Translation: BAD96758.1 .
    BX537913 mRNA. Translation: CAD97897.1 . Different initiation.
    AC011088 Genomic DNA. No translation available.
    CH471185 Genomic DNA. Translation: EAW59364.1 .
    BC054028 mRNA. Translation: AAH54028.1 .
    BC100891 mRNA. Translation: AAI00892.1 .
    BC100892 mRNA. Translation: AAI00893.1 .
    BC100893 mRNA. Translation: AAI00894.1 .
    BC100894 mRNA. Translation: AAI00895.1 .
    BC109386 mRNA. Translation: AAI09387.1 .
    BC110071 mRNA. Translation: AAI10072.1 .
    BC113850 mRNA. Translation: AAI13851.1 .
    BC113897 mRNA. Translation: AAI13898.1 .
    CCDSi CCDS31654.1. [P53634-2 ]
    CCDS44693.1. [P53634-3 ]
    CCDS8282.1. [P53634-1 ]
    PIRi S23941.
    S66504.
    RefSeqi NP_001107645.1. NM_001114173.1. [P53634-3 ]
    NP_001805.3. NM_001814.4.
    NP_680475.1. NM_148170.3. [P53634-2 ]
    UniGenei Hs.128065.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1K3B X-ray 2.15 A 25-143 [» ]
    B 231-394 [» ]
    C 395-463 [» ]
    2DJF X-ray 2.00 A 25-143 [» ]
    B 231-394 [» ]
    C 395-463 [» ]
    2DJG X-ray 2.05 A 25-143 [» ]
    B 231-394 [» ]
    C 395-463 [» ]
    3PDF X-ray 1.85 A 25-463 [» ]
    4CDC X-ray 2.40 A/D/G/J 25-143 [» ]
    B/E/H/K 230-394 [» ]
    C/F/I/L 395-463 [» ]
    4CDD X-ray 2.35 A/D 25-144 [» ]
    B/E 230-394 [» ]
    C/F 395-463 [» ]
    4CDE X-ray 2.40 A/D 25-143 [» ]
    B/E 230-394 [» ]
    C/F 395-463 [» ]
    4CDF X-ray 2.20 A/D 25-144 [» ]
    B/E 229-394 [» ]
    C/F 395-463 [» ]
    ProteinModelPortali P53634.
    SMRi P53634. Positions 25-142, 174-463.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107502. 12 interactions.
    IntActi P53634. 8 interactions.
    MINTi MINT-4655964.

    Chemistry

    BindingDBi P53634.
    ChEMBLi CHEMBL2252.

    Protein family/group databases

    MEROPSi C01.070.

    PTM databases

    PhosphoSitei P53634.

    Polymorphism databases

    DMDMi 317373330.

    Proteomic databases

    MaxQBi P53634.
    PaxDbi P53634.
    PRIDEi P53634.

    Protocols and materials databases

    DNASUi 1075.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000227266 ; ENSP00000227266 ; ENSG00000109861 . [P53634-1 ]
    ENST00000524463 ; ENSP00000432541 ; ENSG00000109861 . [P53634-2 ]
    ENST00000529974 ; ENSP00000433539 ; ENSG00000109861 . [P53634-3 ]
    GeneIDi 1075.
    KEGGi hsa:1075.
    UCSCi uc001pck.4. human. [P53634-1 ]
    uc001pcm.4. human. [P53634-2 ]
    uc001pcn.4. human. [P53634-3 ]

    Organism-specific databases

    CTDi 1075.
    GeneCardsi GC11M088026.
    HGNCi HGNC:2528. CTSC.
    HPAi CAB025364.
    MIMi 170650. phenotype.
    245000. phenotype.
    245010. phenotype.
    602365. gene.
    neXtProti NX_P53634.
    Orphaneti 2342. Haim-Munk syndrome.
    678. Papillon-Lefevre syndrome.
    PharmGKBi PA27028.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4870.
    HOGENOMi HOG000127503.
    HOVERGENi HBG005248.
    InParanoidi P53634.
    KOi K01275.
    OMAi YDDFLHY.
    OrthoDBi EOG74R1QK.
    PhylomeDBi P53634.
    TreeFami TF313225.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS03265-MONOMER.
    Reactomei REACT_121399. MHC class II antigen presentation.
    SABIO-RK P53634.

    Miscellaneous databases

    EvolutionaryTracei P53634.
    GeneWikii Cathepsin_C.
    GenomeRNAii 1075.
    NextBioi 4488.
    PMAP-CutDB P53634.
    PROi P53634.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P53634.
    Bgeei P53634.
    Genevestigatori P53634.

    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 and sequence analysis of human preprocathepsin C."
      Paris A., Strukelj B., Pungercar J., Renko M., Dolenc I., Turk V.
      FEBS Lett. 369:326-330(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-153.
      Tissue: Ileum.
    2. "Human dipeptidyl-peptidase I. Gene characterization, localization, and expression."
      Rao N.V., Rao G.V., Hoidal J.R.
      J. Biol. Chem. 272:10260-10265(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, TISSUE SPECIFICITY, VARIANT THR-153.
    3. "Cathepsin C gene: first compound heterozygous patient with Papillon-Lefevre syndrome and a novel symptomless mutation."
      Allende L.M., Garcia-Perez M.A., Moreno A., Corell A., Carasol M., Martinez-Canut P., Arnaiz-Villena A.
      Hum. Mutat. 17:152-153(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS PLS TYR-236; ARG-286 AND TYR-291, VARIANT THR-153.
      Tissue: Blood.
    4. "A genetic study of cathepsin C gene in two families with Papillon-Lefevre syndrome."
      Allende L.M., Moreno A., de Unamuno P.
      Mol. Genet. Metab. 79:146-148(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS THR-153 AND PLS HIS-294.
      Tissue: Blood.
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT THR-153.
      Tissue: Cerebellum and Rheumatoid arthritic synovial fluid.
    6. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT THR-153.
      Tissue: Thyroid.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Fetal kidney.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT THR-153.
    10. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
      Tissue: Pancreas.
    11. "Stoichiometry and heterogeneity of the pro-region chain in tetrameric human cathepsin C."
      Cigic B., Krizaj I., Kralj B., Turk V., Pain R.H.
      Biochim. Biophys. Acta 1382:143-150(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 25-71; 122-143; 231-235 AND 395-399, CHARACTERIZATION OF EXCLUSION DOMAIN, GLYCOSYLATION.
    12. "Oligomeric structure and substrate induced inhibition of human cathepsin C."
      Dolenc I., Turk B., Pungercic G., Ritonja A., Turk V.
      J. Biol. Chem. 270:21626-21631(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 25-34; 231-239 AND 395-404, CHARACTERIZATION.
    13. "The residual pro-part of cathepsin C fulfills the criteria required for an intramolecular chaperone in folding and stabilizing the human proenzyme."
      Cigic B., Dahl S.W., Pain R.H.
      Biochemistry 39:12382-12390(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 25-28; 51-61; 114-117 AND 133-139, CHARACTERIZATION OF EXCLUSION DOMAIN, DISULFIDE BONDS.
    14. "Purification and characterization of dipeptidyl peptidase I from human spleen."
      McGuire M.J., Lipsky P.E., Thiele D.L.
      Arch. Biochem. Biophys. 295:280-288(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 231-290; 310-328 AND 340-383, FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, GLYCOSYLATION, VARIANT THR-153.
      Tissue: Spleen.
    15. "Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms."
      Ruiz-Canada C., Kelleher D.J., Gilmore R.
      Cell 136:272-283(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-29; ASN-53; ASN-119 AND ASN-276.
    16. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-53.
      Tissue: Liver.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Structure of human dipeptidyl peptidase I (cathepsin C): exclusion domain added to an endopeptidase framework creates the machine for activation of granular serine proteases."
      Turk D., Janjic V., Stern I., Podobnik M., Lamba D., Dahl S.W., Lauritzen C., Pedersen J., Turk V., Turk B.
      EMBO J. 20:6570-6582(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 25-143 AND 231-463 IN COMPLEX WITH CHLORIDE IONS, SUBUNIT, DISULFIDE BONDS, GLYCOSYLATION AT ASN-29.
    19. Cited for: VARIANTS PLS PHE-249; LEU-252; PRO-272; SER-301; CYS-339 AND CYS-347.
    20. "Haim-Munk syndrome and Papillon-Lefevre syndrome are allelic mutations in cathepsin C."
      Hart T.C., Hart P.S., Michalec M.D., Zhang Y., Firatli E., Van Dyke T.E., Stabholz A., Zlotogorski A., Shapira L., Soskolne W.A.
      J. Med. Genet. 37:88-94(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HMS ARG-286.
    21. "Localisation of a gene for prepubertal periodontitis to chromosome 11q14 and identification of a cathepsin C gene mutation."
      Hart T.C., Hart P.S., Michalec M.D., Zhang Y., Marazita M.L., Cooper M., Yassin O.M., Nusier M., Walker S.
      J. Med. Genet. 37:95-101(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PLS CYS-339 AND CYS-340, VARIANT AP1 CYS-347.
    22. "Identification of cathepsin C mutations in ethnically diverse Papillon-Lefevre syndrome patients."
      Hart P.S., Zhang Y., Firatli E., Uygur C., Lotfazar M., Michalec M.D., Marks J.J., Lu X., Coates B.J., Seow W.K., Marshall R., Williams D., Reed J.B., Wright J.T., Hart T.C.
      J. Med. Genet. 37:927-932(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PLS 67-TYR--ALA-74 DEL; PRO-272; SER-300; VAL-301; SER-301; ASN-304; GLY-319; CYS-339; CYS-340 AND GLY-447, VARIANT THR-153.
    23. "Papillon-Lefevre syndrome: mutations and polymorphisms in the cathepsin C gene."
      Nakano A., Nomura K., Nakano H., Ono Y., LaForgia S., Pulkkinen L., Hashimoto I., Uitto J.
      J. Invest. Dermatol. 116:339-343(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PLS SER-39 AND SER-301, VARIANT VAL-453.
    24. "Novel point mutations, deletions, and polymorphisms in the cathepsin C gene in nine families from Europe and North Africa with Papillon-Lefevre syndrome."
      Lefevre C., Blanchet-Bardon C., Jobard F., Bouadjar B., Stalder J.-F., Cure S., Hoffmann A., Prud'Homme J.-F., Fischer J.
      J. Invest. Dermatol. 117:1657-1661(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PLS PRO-127; PRO-272; CYS-339 AND CYS-429, VARIANTS THR-153 AND LYS-401.
    25. "Evidence of a founder effect for four cathepsin C gene mutations in Papillon-Lefevre syndrome patients."
      Zhang Y., Lundgren T., Renvert S., Tatakis D.N., Firatli E., Uygur C., Hart P.S., Gorry M.C., Marks J.J., Hart T.C.
      J. Med. Genet. 38:96-101(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PLS PRO-272 AND ASP-300.
    26. "Biochemical and mutational analyses of the cathepsin c gene (CTSC) in three North American families with Papillon Lefevre syndrome."
      Zhang Y., Hart P.S., Moretti A.J., Bouwsma O.J., Fisher E.M., Dudlicek L., Pettenati M.J., Hart T.C.
      Hum. Mutat. 20:75-75(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PLS ARG-139 AND PRO-272, VARIANT THR-153.
    27. Cited for: VARIANTS PLS GLU-129; ARG-139; TYR-236; PHE-249; LEU-252; HIS-272; SER-301; ARG-312; CYS-339; CYS-347 AND GLY-447, VARIANTS AP1 HIS-272 AND CYS-412, VARIANT THR-153.
    28. "Loss-of-function mutations in cathepsin C in two families with Papillon-Lefevre syndrome are associated with deficiency of serine proteinases in PMNs."
      de Haar S.F., Jansen D.C., Schoenmaker T., De Vree H., Everts V., Beertsen W.
      Hum. Mutat. 23:524-524(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PLS ASN-405.
    29. "Gene symbol: CTSC. Disease: Papillon-Lefevre syndrome."
      de Haar S.F., Mir M., Nguyen M., Kazemi B., Ramezani G.H., Everts V.
      Hum. Genet. 116:545-545(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PLS ARG-405.
    30. Erratum
      de Haar S.F., Mir M., Nguyen M., Kazemi B., Ramezani G.H., Everts V.
      Hum. Genet. 118:533-533(2005)

    Entry informationi

    Entry nameiCATC_HUMAN
    AccessioniPrimary (citable) accession number: P53634
    Secondary accession number(s): A8K7V2
    , B5MDD5, Q2HIY8, Q53G93, Q71E75, Q71E76, Q7M4N9, Q7Z3G7, Q7Z5U7, Q8WY99, Q8WYA7, Q8WYA8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 156 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Peptidase families
      Classification of peptidase families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3