P53634 (CATC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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:

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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	463 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.17
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. Ref.11 Ref.14 Ref.15 Ref.17 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	Defects in CTSC are a cause of Papillon-Lefevre syndrome (PLS) [MIM:245000]; also known as keratosis palmoplantaris with periodontopathia. PLS is 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. Ref.3 Ref.4 Ref.18 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Defects in CTSC are a cause of Haim-Munk syndrome (HMS) [MIM:245010]; also known as keratosis palmoplantaris with periodontopathia and onychogryposis or Cochin Jewish disorder. HMS is an autosomal recessive disorder characterized by palmoplantar keratosis, onychogryphosis and periodontitis. Additional features are pes planus, arachnodactyly, and acroosteolysis. Ref.19 Defects in CTSC are a cause of aggressive periodontititis type 1 (AP1) [MIM:170650]; also known as juvenile periodontitis (JPD) and prepubertal periodontitis (PPP). AP1 is characterized by severe and protracted gingival infections, leading to tooth loss. AP1 inheritance is autosomal dominant. Ref.20 Ref.26
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 component	Lysosome
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Palmoplantar keratoderma
Domain	Signal
Ligand	Chloride
Molecular function	Hydrolase Protease Thiol protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	immune response Traceable author statement. Source: ProtInc proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	lysosome Traceable author statement Ref.12. Source: UniProtKB
Molecular function	cysteine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

24

Ref.11 Ref.12 Ref.13

Chain

25 – 134

110

Dipeptidyl peptidase 1 exclusion domain chain

PRO_0000026338

Propeptide

135 – 230

96

PRO_0000026339

Chain

231 – 394

164

Dipeptidyl peptidase 1 heavy chain

PRO_0000026340

Chain

395 – 463

69

Dipeptidyl peptidase 1 light chain

PRO_0000026341

Sites

Active site

258

1

Active site

405

1

Active site

427

1

Binding site

302

1

Chloride

Binding site

304

1

Chloride; via amide nitrogen

Binding site

347

1

Chloride

Amino acid modifications

Glycosylation

29

1

N-linked (GlcNAc...) Ref.17

Glycosylation

53

1

N-linked (GlcNAc...) Ref.15

Glycosylation

119

1

N-linked (GlcNAc...)

Glycosylation

276

1

N-linked (GlcNAc...)

Disulfide bond

30 ↔ 118

Ref.13 Ref.17

Disulfide bond

54 ↔ 136

Ref.13 Ref.17

Disulfide bond

255 ↔ 298

Ref.13 Ref.17

Disulfide bond

291 ↔ 331

Ref.13 Ref.17

Disulfide bond

321 ↔ 337

Ref.13 Ref.17

Natural variations

Alternative sequence

107 – 137

31

YKEEG…NWACF → DVTDFISHLFMQLGTVGIYD LPHLRNKLVIK in isoform 2.

VSP_039123

Alternative sequence

138 – 463

326

Missing in isoform 2.

VSP_039124

Natural variant

39

1

W → S in PLS. Ref.22

VAR_016933

Natural variant

67 – 74

8

Missing in PLS.

VAR_019035

Natural variant

127

1

H → P in PLS. Ref.23

VAR_016934

Natural variant

129

1

V → E in PLS. Ref.26

VAR_019036

Natural variant

139

1

G → R in PLS. Ref.25 Ref.26

VAR_019037

Natural variant

153

1

I → T. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.9 Ref.14 Ref.21 Ref.23 Ref.25 Ref.26
Corresponds to variant rs217086 [ dbSNP | Ensembl ].

VAR_016943

Natural variant

236

1

D → Y in PLS. Ref.3 Ref.26

VAR_019038

Natural variant

249

1

V → F in PLS. Ref.18 Ref.26

VAR_009541

Natural variant

252

1

Q → L in PLS. Ref.18 Ref.26

VAR_009542

Natural variant

272

1

R → H in PLS. Ref.26

VAR_019039

Natural variant

272

1

R → P in PLS. Ref.18 Ref.21 Ref.23 Ref.24 Ref.25

VAR_009543

Natural variant

286

1

Q → R in HMS and PLS. Ref.3 Ref.19

VAR_016935

Natural variant

291

1

C → Y in PLS. Ref.3

VAR_019040

Natural variant

294

1

Y → H in PLS. Ref.4

VAR_039686

Natural variant

300

1

G → D in PLS. Ref.24

VAR_019041

Natural variant

300

1

G → S in PLS. Ref.21

VAR_019042

Natural variant

301

1

G → S in PLS. Ref.18 Ref.21 Ref.22 Ref.26

VAR_009544

Natural variant

301

1

G → V in PLS. Ref.21

VAR_019043

Natural variant

304

1

Y → N in PLS. Ref.21

VAR_019044

Natural variant

312

1

Q → R in PLS. Ref.26

VAR_019045

Natural variant

319

1

E → G in PLS. Ref.21

VAR_019046

Natural variant

339

1

R → C in PLS. Ref.18 Ref.20 Ref.21 Ref.23 Ref.26

VAR_009545

Natural variant

340

1

Y → C in PLS. Ref.20 Ref.21

VAR_016944

Natural variant

347

1

Y → C in PLS and AP1. Ref.18 Ref.20 Ref.26

VAR_009546

Natural variant

401

1

E → K. Ref.23

VAR_016945

Natural variant

405

1

H → N in PLS. Ref.27

VAR_027249

Natural variant

405

1

H → R in PLS. Ref.28

VAR_027250

Natural variant

412

1

Y → C in AP1. Ref.26
Corresponds to variant rs28937571 [ dbSNP | Ensembl ].

VAR_019047

Natural variant

429

1

W → C in PLS. Ref.23

VAR_016936

Natural variant

447

1

E → G in PLS. Ref.21 Ref.26

VAR_019048

Natural variant

453

1

I → V Rare polymorphism. Ref.22
Corresponds to variant rs3888798 [ dbSNP | Ensembl ].

VAR_016946

Experimental info

Sequence conflict

63

1

K → I in BAD96758. Ref.6

Sequence conflict

237

1

W → V AA sequence Ref.14

Sequence conflict

321

1

C → S AA sequence Ref.14

Sequence conflict

355

1

C → M AA sequence Ref.14

Sequence conflict

366

1

H → R AA sequence Ref.14

Sequence conflict

376 – 378

3

VYD → YVY AA sequence Ref.14

Secondary structure

1

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463

Helix Strand Turn

Details...

Helix

32 – 35

4

Beta strand

36 – 43

8

Turn

49 – 51

3

Beta strand

62 – 69

8

Turn

70 – 72

3

Beta strand

73 – 76

4

Beta strand

81 – 87

7

Turn

88 – 90

3

Beta strand

91 – 96

6

Beta strand

99 – 112

14

Beta strand

114 – 121

8

Beta strand

123 – 128

6

Beta strand

133 – 141

9

Helix

258 – 274

17

Turn

275 – 277

3

Helix

285 – 291

7

Helix

303 – 306

4

Helix

309 – 313

5

Turn

319 – 321

3

Beta strand

342 – 347

6

Helix

357 – 367

11

Beta strand

370 – 374

5

Helix

378 – 381

4

Beta strand

385 – 388

4

Beta strand

405 – 414

10

Turn

416 – 418

3

Beta strand

421 – 426

6

Beta strand

438 – 442

5

Helix

447 – 449

3

Beta strand

455 – 459

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 11, 2011. Version 2. Checksum: 4C9C7C24D900CEE6	FASTA	463	51,854
	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
	Isoform 2 [UniParc]. Checksum: C68FC076FCB30601	FASTA	137	15,169
	10 20 30 40 50 60 MGAGPSLLLA ALLLLLSGDG AVRCDTPANC TYLDLLGTWV FQVGSSGSQR DVNCSVMGPQ 70 80 90 100 110 120 EKKVVVYLQK LDTAYDDLGN SGHFTIIYNQ GFEIVLNDYK WFAFFKDVTD FISHLFMQLG 130 TVGIYDLPHL RNKLVIK

References

	« Hide 'large scale' referencesShow '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: 7649281] [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: 9092576] [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: 11180601] [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: 12809647] [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: 14702039] [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: 17974005] [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. , 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: 16554811] [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. , 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). 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: 9507095] [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: 7665576] [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: 11015218] [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: 1586157] [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]	"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: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-53, MASS SPECTROMETRY. Tissue: Liver.
[16]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]	"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: 11726493] [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.
[18]	"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. , Read A.P., Sloan P., Dixon M.J., Thakker N.S. Nat. Genet. 23:421-424(1999) [PubMed: 10581027] [Abstract] Cited for: VARIANTS PLS PHE-249; LEU-252; PRO-272; SER-301; CYS-339 AND CYS-347.
[19]	"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: 10662807] [Abstract] Cited for: VARIANT HMS ARG-286.
[20]	"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: 10662808] [Abstract] Cited for: VARIANTS PLS CYS-339 AND CYS-340, VARIANT AP1 CYS-347.
[21]	"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: 11106356] [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.
[22]	"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: 11180012] [Abstract] Cited for: VARIANTS PLS SER-39 AND SER-301, VARIANT VAL-453.
[23]	"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: 11886537] [Abstract] Cited for: VARIANTS PLS PRO-127; PRO-272; CYS-339 AND CYS-429, VARIANTS THR-153 AND LYS-401.
[24]	"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: 11158173] [Abstract] Cited for: VARIANTS PLS PRO-272 AND ASP-300.
[25]	"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: 12112662] [Abstract] Cited for: VARIANTS PLS ARG-139 AND PRO-272, VARIANT THR-153.
[26]	"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. , 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: 14974080] [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.
[27]	"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: 15108292] [Abstract] Cited for: VARIANT PLS ASN-405.
[28]	"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: 15991336] [Abstract] Cited for: VARIANT PLS ARG-405.
[29]	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.
BC113897 mRNA. Translation: AAI13898.1.

IPI

IPI00022810.
IPI00171323.

PIR

S23941.
S66504.

RefSeq

NP_001805.3. NM_001814.4.
NP_680475.1. NM_148170.3.

UniGene

Hs.128065.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P53634.

SMR

P53634. Positions 25-463.

ModBase

Search...

Protein-protein interaction databases

IntAct

P53634. 7 interactions.

MINT

MINT-4655964.

STRING

P53634.

Protein family/group databases

MEROPS

C01.070.

Polymorphism databases

DMDM

1705632.

Proteomic databases

PRIDE

P53634.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000227266; ENSP00000227266; ENSG00000109861.
ENST00000415415; ENSP00000411027; ENSG00000109861.

GeneID

1075.

KEGG

hsa:1075.

UCSC

uc001pck.2. human.

Organism-specific databases

CTD

1075.

GeneCards

GC11M088026.

H-InvDB

HIX0026143.

HGNC

HGNC:2528. CTSC.

HPA

CAB025364.

MIM

170650. phenotype.
245000. phenotype.
245010. phenotype.
602365. gene.

neXtProt

NX_P53634.

Orphanet

2342. Haim-Munk syndrome.
678. Papillon-Lefevre syndrome.

PharmGKB

PA27028.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG11734.

GeneTree

ENSGT00560000076599.

HOVERGEN

HBG005248.

InParanoid

P53634.

OMA

RGTDECA.

OrthoDB

EOG4H19VZ.

PhylomeDB

P53634.

Enzyme and pathway databases

BioCyc

MetaCyc:HS03265-MONOMER.

Gene expression databases

ArrayExpress

P53634.

Bgee

P53634.

Genevestigator

P53634.

GermOnline

ENSG00000109861. Homo sapiens.

Family and domain databases

InterPro

IPR014882. CathepsinC_exc.
IPR000169. Pept_cys_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
[Graphical view]

KO

K01275.

PANTHER

PTHR12411. Peptidase_C1A. 1 hit.

Pfam

PF08773. CathepsinC_exc. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]

PRINTS

PR00705. PAPAIN.

SMART

SM00645. Pept_C1. 1 hit.
[Graphical view]

PROSITE

PS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

4488.

PMAP-CutDB

P53634.

SOURCE

Search...

Entry information

Entry name

CATC_HUMAN

Accession

Primary (citable) accession number: P53634
Secondary accession number(s): A8K7V2 , 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:	January 25, 2012
This is version 126 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.