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P53634 (CATC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:

  1. Dipeptidyl peptidase 1 exclusion domain chain
    Alternative name(s):
    Dipeptidyl peptidase I exclusion domain chain
  2. Dipeptidyl peptidase 1 heavy chain
    Alternative name(s):
    Dipeptidyl peptidase I heavy chain
  3. Dipeptidyl peptidase 1 light chain
    Alternative name(s):
    Dipeptidyl peptidase I light chain
Gene names
Name:CTSC
Synonyms:CPPI
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length463 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.14

Catalytic activity

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

Cofactor

Binds 1 chloride ion per heavy chain.

Enzyme regulation

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. Ref.14

Subunit structure

Tetramer of heterotrimers consisting of exclusion domain, heavy- and light chains. Ref.14 Ref.18

Subcellular location

Lysosome.

Tissue specificity

Ubiquitous. Highly expressed in lung, kidney and placenta. Detected at intermediate levels in colon, small intestine, spleen and pancreas. Ref.2

Induction

Up-regulated in lymphocytes by IL2/interleukin-2. Ref.2 Ref.14

Post-translational modification

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. Ref.11 Ref.14 Ref.15 Ref.18

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.

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.3 Ref.4 Ref.19 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.20

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.21 Ref.27

Sequence similarities

Belongs to the peptidase C1 family.

Biophysicochemical properties

pH dependence:

High activity at pH 4.5-6.8. Ref.14

Sequence caution

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

Ontologies

Keywords
   Cellular componentLysosome
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Palmoplantar keratoderma
   DomainSignal
   LigandChloride
   Molecular functionHydrolase
Protease
Thiol protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processT cell mediated cytotoxicity

Inferred from electronic annotation. Source: Ensembl

aging

Inferred from electronic annotation. Source: Ensembl

immune response

Traceable author statement Ref.2. Source: ProtInc

positive regulation of apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

proteolysis

Inferred from direct assay PubMed 8811434. Source: UniProtKB

response to organic substance

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 19199708PubMed 23376485. Source: UniProt

lysosome

Traceable author statement Ref.12. Source: UniProtKB

   Molecular_functionchloride ion binding

Inferred from electronic annotation. Source: Ensembl

cysteine-type peptidase activity

Inferred from direct assay PubMed 8811434. Source: UniProtKB

peptidase activator activity involved in apoptotic process

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 18256700. Source: IntAct

serine-type endopeptidase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CST7O760962EBI-1047323,EBI-2807448

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P53634-1)

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.
Isoform 2 (identifier: P53634-2)

The sequence of this isoform differs from the canonical sequence as follows:
     107-137: YKEEGSKVTTYCNETMTGWVHDVLGRNWACF → DVTDFISHLFMQLGTVGIYDLPHLRNKLVIK
     138-463: Missing.
Isoform 3 (identifier: P53634-3)

The sequence of this isoform differs from the canonical sequence as follows:
     107-141: YKEEGSKVTTYCNETMTGWVHDVLGRNWACFTGKK → DVTDFISHLFMQLGTVGIYDLPHLRNKLAMNRRWG
     142-463: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Ref.11 Ref.12 Ref.13
Chain25 – 134110Dipeptidyl peptidase 1 exclusion domain chain
PRO_0000026338
Propeptide135 – 23096
PRO_0000026339
Chain231 – 394164Dipeptidyl peptidase 1 heavy chain
PRO_0000026340
Chain395 – 46369Dipeptidyl peptidase 1 light chain
PRO_0000026341

Sites

Active site2581
Active site4051
Active site4271
Binding site3021Chloride
Binding site3041Chloride; via amide nitrogen
Binding site3471Chloride

Amino acid modifications

Glycosylation291N-linked (GlcNAc...) Ref.15 Ref.18
Glycosylation531N-linked (GlcNAc...) Ref.15 Ref.16
Glycosylation1191N-linked (GlcNAc...) Ref.15
Glycosylation2761N-linked (GlcNAc...) Ref.15
Disulfide bond30 ↔ 118 Ref.13 Ref.18
Disulfide bond54 ↔ 136 Ref.13 Ref.18
Disulfide bond255 ↔ 298 Ref.13 Ref.18
Disulfide bond291 ↔ 331 Ref.13 Ref.18
Disulfide bond321 ↔ 337 Ref.13 Ref.18

Natural variations

Alternative sequence107 – 14135YKEEG…FTGKK → DVTDFISHLFMQLGTVGIYD LPHLRNKLAMNRRWG in isoform 3.
VSP_043232
Alternative sequence107 – 13731YKEEG…NWACF → DVTDFISHLFMQLGTVGIYD LPHLRNKLVIK in isoform 2.
VSP_039123
Alternative sequence138 – 463326Missing in isoform 2.
VSP_039124
Alternative sequence142 – 463322Missing in isoform 3.
VSP_043233
Natural variant391W → S in PLS. Ref.23
VAR_016933
Natural variant67 – 748Missing in PLS.
VAR_019035
Natural variant1271H → P in PLS. Ref.24
VAR_016934
Natural variant1291V → E in PLS. Ref.27
VAR_019036
Natural variant1391G → R in PLS. Ref.26 Ref.27
VAR_019037
Natural variant1531I → T. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.9 Ref.14 Ref.22 Ref.24 Ref.26 Ref.27
Corresponds to variant rs217086 [ dbSNP | Ensembl ].
VAR_016943
Natural variant2361D → Y in PLS. Ref.3 Ref.27
VAR_019038
Natural variant2491V → F in PLS. Ref.19 Ref.27
VAR_009541
Natural variant2521Q → L in PLS. Ref.19 Ref.27
VAR_009542
Natural variant2721R → H in PLS. Ref.27
VAR_019039
Natural variant2721R → P in PLS. Ref.19 Ref.22 Ref.24 Ref.25 Ref.26
VAR_009543
Natural variant2861Q → R in HMS and PLS. Ref.3 Ref.20
VAR_016935
Natural variant2911C → Y in PLS. Ref.3
VAR_019040
Natural variant2941Y → H in PLS. Ref.4
VAR_039686
Natural variant3001G → D in PLS. Ref.25
VAR_019041
Natural variant3001G → S in PLS. Ref.22
VAR_019042
Natural variant3011G → S in PLS. Ref.19 Ref.22 Ref.23 Ref.27
VAR_009544
Natural variant3011G → V in PLS. Ref.22
VAR_019043
Natural variant3041Y → N in PLS. Ref.22
VAR_019044
Natural variant3121Q → R in PLS. Ref.27
VAR_019045
Natural variant3191E → G in PLS. Ref.22
VAR_019046
Natural variant3391R → C in PLS. Ref.19 Ref.21 Ref.22 Ref.24 Ref.27
VAR_009545
Natural variant3401Y → C in PLS. Ref.21 Ref.22
VAR_016944
Natural variant3471Y → C in PLS and AP1. Ref.19 Ref.21 Ref.27
VAR_009546
Natural variant4011E → K. Ref.24
VAR_016945
Natural variant4051H → N in PLS. Ref.28
VAR_027249
Natural variant4051H → R in PLS. Ref.29
Corresponds to variant rs151269219 [ dbSNP | Ensembl ].
VAR_027250
Natural variant4121Y → C in AP1. Ref.27
Corresponds to variant rs28937571 [ dbSNP | Ensembl ].
VAR_019047
Natural variant4291W → C in PLS. Ref.24
VAR_016936
Natural variant4471E → G in PLS. Ref.22 Ref.27
VAR_019048
Natural variant4531I → V Rare polymorphism. Ref.23
Corresponds to variant rs3888798 [ dbSNP | Ensembl ].
VAR_016946

Experimental info

Sequence conflict631K → I in BAD96758. Ref.6
Sequence conflict2371W → V AA sequence Ref.14
Sequence conflict3211C → S AA sequence Ref.14
Sequence conflict3551C → M AA sequence Ref.14
Sequence conflict3661H → R AA sequence Ref.14
Sequence conflict376 – 3783VYD → YVY AA sequence Ref.14

Secondary structure

............................................................. 463
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 11, 2011. Version 2.
Checksum: 4C9C7C24D900CEE6

FASTA46351,854
        10         20         30         40         50         60 
MGAGPSLLLA ALLLLLSGDG AVRCDTPANC TYLDLLGTWV FQVGSSGSQR DVNCSVMGPQ 

        70         80         90        100        110        120 
EKKVVVYLQK LDTAYDDLGN SGHFTIIYNQ GFEIVLNDYK WFAFFKYKEE GSKVTTYCNE 

       130        140        150        160        170        180 
TMTGWVHDVL GRNWACFTGK KVGTASENVY VNIAHLKNSQ EKYSNRLYKY DHNFVKAINA 

       190        200        210        220        230        240 
IQKSWTATTY MEYETLTLGD MIRRSGGHSR KIPRPKPAPL TAEIQQKILH LPTSWDWRNV 

       250        260        270        280        290        300 
HGINFVSPVR NQASCGSCYS FASMGMLEAR IRILTNNSQT PILSPQEVVS CSQYAQGCEG 

       310        320        330        340        350        360 
GFPYLIAGKY AQDFGLVEEA CFPYTGTDSP CKMKEDCFRY YSSEYHYVGG FYGGCNEALM 

       370        380        390        400        410        420 
KLELVHHGPM AVAFEVYDDF LHYKKGIYHH TGLRDPFNPF ELTNHAVLLV GYGTDSASGM 

       430        440        450        460 
DYWIVKNSWG TGWGENGYFR IRRGTDECAI ESIAVAATPI PKL 

« Hide

Isoform 2 [UniParc].

Checksum: C68FC076FCB30601
Show »

FASTA13715,169
Isoform 3 [UniParc].

Checksum: FAD4B1B511F91F66
Show »

FASTA14115,700

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Fetal kidney.
[8]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"Loss-of-function mutations in the cathepsin C gene result in periodontal disease and palmoplantar keratosis."
Toomes C., James J., Wood A.J., Wu C.L., McCormick D., Lench N., Hewitt C., Moynihan L., Roberts E., Woods C.G., Markham A., Wong M., Widmer R., Ghaffar K.A., Pemberton M., Hussein I.R., Temtamy S.A., Davies R. expand/collapse author list , Read A.P., Sloan P., Dixon M.J., Thakker N.S.
Nat. Genet. 23:421-424(1999) [PubMed] [Europe PMC] [Abstract]
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]"The role of cathepsin C in Papillon-Lefevre syndrome, prepubertal periodontitis, and aggressive periodontitis."
Hewitt C., McCormick D., Linden G., Turk D., Stern I., Wallace I., Southern L., Zhang L., Howard R., Bullon P., Wong M., Widmer R., Gaffar K.A., Awawdeh L., Briggs J., Yaghmai R., Jabs E.W., Hoeger P. expand/collapse author list , Bleck O., Rudiger S.G., Petersilka G., Battino M., Brett P., Hattab F., Al-Hamed M., Sloan P., Toomes C., Dixon M.J., James J., Read A.P., Thakker N.S.
Hum. Mutat. 23:222-228(2004) [PubMed] [Europe PMC] [Abstract]
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)
+Additional computationally mapped references.

Web resources

CTSCbase

CTSC mutation db

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS31654.1. [P53634-2]
CCDS44693.1. [P53634-3]
CCDS8282.1. [P53634-1]
PIRS23941.
S66504.
RefSeqNP_001107645.1. NM_001114173.1. [P53634-3]
NP_001805.3. NM_001814.4.
NP_680475.1. NM_148170.3. [P53634-2]
UniGeneHs.128065.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP53634.
SMRP53634. Positions 25-142, 174-463.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107502. 10 interactions.
IntActP53634. 8 interactions.
MINTMINT-4655964.

Chemistry

BindingDBP53634.
ChEMBLCHEMBL2252.

Protein family/group databases

MEROPSC01.070.

PTM databases

PhosphoSiteP53634.

Polymorphism databases

DMDM317373330.

Proteomic databases

MaxQBP53634.
PaxDbP53634.
PRIDEP53634.

Protocols and materials databases

DNASU1075.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000227266; ENSP00000227266; ENSG00000109861. [P53634-1]
ENST00000524463; ENSP00000432541; ENSG00000109861. [P53634-2]
ENST00000529974; ENSP00000433539; ENSG00000109861. [P53634-3]
GeneID1075.
KEGGhsa:1075.
UCSCuc001pck.4. human. [P53634-1]
uc001pcm.4. human. [P53634-2]
uc001pcn.4. human. [P53634-3]

Organism-specific databases

CTD1075.
GeneCardsGC11M088026.
HGNCHGNC:2528. CTSC.
HPACAB025364.
MIM170650. phenotype.
245000. phenotype.
245010. phenotype.
602365. gene.
neXtProtNX_P53634.
Orphanet2342. Haim-Munk syndrome.
678. Papillon-Lefevre syndrome.
PharmGKBPA27028.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4870.
HOGENOMHOG000127503.
HOVERGENHBG005248.
InParanoidP53634.
KOK01275.
OMAYDDFLHY.
OrthoDBEOG74R1QK.
PhylomeDBP53634.
TreeFamTF313225.

Enzyme and pathway databases

BioCycMetaCyc:HS03265-MONOMER.
ReactomeREACT_6900. Immune System.
SABIO-RKP53634.

Gene expression databases

ArrayExpressP53634.
BgeeP53634.
GenevestigatorP53634.

Family and domain databases

Gene3D2.40.128.80. 1 hit.
InterProIPR014882. CathepsinC_exc.
IPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
[Graphical view]
PANTHERPTHR12411. PTHR12411. 1 hit.
PfamPF08773. CathepsinC_exc. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSPR00705. PAPAIN.
SMARTSM00645. Pept_C1. 1 hit.
[Graphical view]
SUPFAMSSF75001. SSF75001. 1 hit.
PROSITEPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP53634.
GeneWikiCathepsin_C.
GenomeRNAi1075.
NextBio4488.
PMAP-CutDBP53634.
PROP53634.
SOURCESearch...

Entry information

Entry nameCATC_HUMAN
AccessionPrimary (citable) accession number: P53634
Secondary accession number(s): A8K7V2 expand/collapse secondary AC list , B5MDD5, Q2HIY8, Q53G93, Q71E75, Q71E76, Q7M4N9, Q7Z3G7, Q7Z5U7, Q8WY99, Q8WYA7, Q8WYA8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 11, 2011
Last modified: July 9, 2014
This is version 154 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM