Reviewed, UniProtKB/Swiss-Prot P53634 (CATC_HUMAN)

Names and origin

Protein names

Recommended name:
    Dipeptidyl-peptidase 1
    EC=3.4.14.1
Alternative name(s):
    Dipeptidyl-peptidase I
      Short name=DPP-I
      Short name=DPPI
    Cathepsin C
    Cathepsin J
    Dipeptidyl transferase
Cleaved into the following 3 chains:
    1- Recommended name:
            Dipeptidyl-peptidase 1 exclusion domain chain
        Alternative name(s):
            Dipeptidyl-peptidase I exclusion domain chain
    2- Recommended name:
            Dipeptidyl-peptidase 1 heavy chain
        Alternative name(s):
            Dipeptidyl-peptidase I heavy chain
    3- Recommended name:
            Dipeptidyl-peptidase 1 light chain
        Alternative name(s):
            Dipeptidyl-peptidase I light chain

Gene names

Name:	CTSC
Synonyms:	CPPI

Organism

Homo sapiens (Human) [Complete proteome]

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.12
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.12
Subunit structure	Tetramer of heterotrimers consisting of exclusion domain, heavy- and light chains. Ref.12 Ref.15
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. Ref.2
Post-translational modification	N-glycosylated. Ref.12 Ref.15 Ref.9 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.16 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 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.17 Defects in CTSC are a cause of juvenile periodontitis (JPD) [MIM:170650]; also known as prepubertal periodontitis (PPP). JPD is characterized by severe and protracted gingival infections, leading to tooth loss. JPD inheritance is autosomal dominant. Ref.18 Ref.24
Sequence similarities	Belongs to the peptidase C1 family.
Biophysicochemical properties	pH dependence: High activity at pH 4.5-6.8.

Ontologies

Keywords
Cellular component	Lysosome
Coding sequence diversity	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
Gene Ontology (GO)
Biological process	immune response Ref.2 Traceable author statement. Source: ProtInc proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	lysosome Ref.10 Traceable author statement. Source: UniProtKB
Molecular function	chloride ion binding Inferred from electronic annotation. Source: UniProtKB-KW cysteine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

24

Ref.9 Ref.10 Ref.11

Chain

25 – 134

110

Dipeptidyl-peptidase 1 exclusion domain chain

PRO_0000026338

Propeptide

135 – 230

96

Ref.12

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.15

Glycosylation

53

1

N-linked (GlcNAc...)

Glycosylation

119

1

N-linked (GlcNAc...)

Glycosylation

276

1

N-linked (GlcNAc...)

Disulfide bond

30 ↔ 118

Ref.15 Ref.11

Disulfide bond

54 ↔ 136

Ref.15 Ref.11

Disulfide bond

255 ↔ 298

Ref.15 Ref.11

Disulfide bond

291 ↔ 331

Ref.15 Ref.11

Disulfide bond

321 ↔ 337

Ref.15 Ref.11

Natural variations

Natural variant

39

1

W → S in PLS. Ref.20

VAR_016933

Natural variant

67 – 74

8

Missing in PLS.

VAR_019035

Natural variant

127

1

H → P in PLS. Ref.21

VAR_016934

Natural variant

129

1

V → E in PLS. Ref.24

VAR_019036

Natural variant

139

1

G → R in PLS. Ref.23 Ref.24

VAR_019037

Natural variant

153

1

T → I: dbSNP rs217086. Ref.3 Ref.19 Ref.21 Ref.23 Ref.24 Ref.7

VAR_016943

Natural variant

236

1

D → Y in PLS. Ref.3 Ref.24

VAR_019038

Natural variant

249

1

V → F in PLS. Ref.16 Ref.24

VAR_009541

Natural variant

252

1

Q → L in PLS. Ref.16 Ref.24

VAR_009542

Natural variant

272

1

R → H in PLS. Ref.16 Ref.19 Ref.21 Ref.22 Ref.23 Ref.24

VAR_019039

Natural variant

272

1

R → P in PLS. Ref.16 Ref.19 Ref.21 Ref.22 Ref.23 Ref.24

VAR_009543

Natural variant

286

1

Q → R in HMS and PLS.

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.19 Ref.22

VAR_019041

Natural variant

300

1

G → S in PLS. Ref.19 Ref.22

VAR_019042

Natural variant

301

1

G → S in PLS. Ref.16 Ref.19 Ref.20 Ref.24

VAR_009544

Natural variant

301

1

G → V in PLS. Ref.16 Ref.19 Ref.20 Ref.24

VAR_019043

Natural variant

304

1

Y → N in PLS. Ref.19

VAR_019044

Natural variant

312

1

Q → R in PLS. Ref.24

VAR_019045

Natural variant

319

1

E → G in PLS. Ref.19

VAR_019046

Natural variant

339

1

R → C in PLS. Ref.16 Ref.18 Ref.19 Ref.21 Ref.24

VAR_009545

Natural variant

340

1

Y → C in PLS. Ref.18 Ref.19

VAR_016944

Natural variant

347

1

Y → C in PLS and JPD.

VAR_009546

Natural variant

401

1

E → K Ref.21

VAR_016945

Natural variant

405

1

H → N in PLS. Ref.25 Ref.26

VAR_027249

Natural variant

405

1

H → R in PLS. Ref.25 Ref.26

VAR_027250

Natural variant

412

1

Y → C in JPD. dbSNP rs28937571. Ref.24

VAR_019047

Natural variant

429

1

W → C in PLS. Ref.21

VAR_016936

Natural variant

447

1

E → G in PLS. Ref.19 Ref.24

VAR_019048

Natural variant

453

1

I → V Rare polymorphism. dbSNP rs3888798. Ref.20

VAR_016946

Experimental info

Sequence conflict

63

1

K → I in BAD96758. Ref.6

Sequence conflict

237

1

W → V AA sequence Ref.12

Sequence conflict

321

1

C → S AA sequence Ref.12

Sequence conflict

355

1

C → M AA sequence Ref.12

Sequence conflict

366

1

H → R AA sequence Ref.12

Sequence conflict

376 – 378

3

VYD → YVY AA sequence Ref.12

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)
	P53634-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 759B5EF1290C3771	FASTA	463	51,842
	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 VNTAHLKNSQ 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

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]. 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.
[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], VARIANT ILE-153, VARIANTS PLS TYR-236; ARG-286 AND TYR-291. 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], VARIANT 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]. Tissue: 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]. Tissue: Thyroid.
[7]	"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], VARIANT ILE-153.
[8]	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].
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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. Tissue: Spleen.
[13]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	"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.
[18]	"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 JPD CYS-347.
[19]	"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 ILE-153.
[20]	"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.
[21]	"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 ILE-153 AND LYS-401.
[22]	"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.
[23]	"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 ILE-153.
[24]	"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 JPD HIS-272 AND CYS-412, VARIANT ILE-153.
[25]	"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.
[26]	"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.
[27]	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

EMBLGenBankDDBJ

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.
AK223038 mRNA. Translation: BAD96758.1.
AC011088 Genomic DNA. No translation available.
CH471185 Genomic DNA. Translation: EAW59364.1.

IPI

IPI00022810.

PIR

S23941.
S66504.

RefSeq

NP_001805.3.

UniGene

Hs.128065
Hs.706874

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P53634. 1 interaction.

Protein family/group databases

MEROPS

C01.070.

Proteomic databases

PRIDE

P53634.

Genome annotation databases

Ensembl

ENSG00000109861. Homo sapiens. [Contig view]

GeneID

1075.

UCSC

uc001pck.2. human.

Organism-specific databases

GeneCards

GC11M087666.

H-InvDB

HIX0026143.

HGNC

HGNC:2528. CTSC.

MIM

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

Orphanet

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

PharmGKB

PA27028.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P53634.

HOVERGEN

P53634.

Enzyme and pathway databases

BRENDA

3.4.14.1. 247.

Gene expression databases

ArrayExpress

P53634.

Bgee

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]

PANTHER

PTHR12411. Peptidase_C1A. 1 hit.

Pfam

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

PRINTS

PR00705. PAPAIN.

ProDom

PD000158. Peptidase_C1. 1 hit.
[Graphical view] [Entries sharing at least one domain]

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 Resources

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, Q8WY99, Q8WYA7, Q8WYA8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	July 7, 2009
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)