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Dipeptidyl peptidase 1 (EC 3.4.14.1) (Cathepsin C) (Cathepsin J) (Dipeptidyl peptidase I) (DPP-I) (DPPI) (Dipeptidyl transferase) [Cleaved into: Dipeptidyl peptidase 1 exclusion domain chain (Dipeptidyl peptidase I exclusion domain chain); Dipeptidyl peptidase 1 heavy chain (Dipeptidyl peptidase I heavy chain); Dipeptidyl peptidase 1 light chain (Dipeptidyl peptidase I light chain)]

 CATC_HUMAN              Reviewed;         463 AA.
P53634; A8K7V2; B5MDD5; Q2HIY8; Q53G93; Q71E75; Q71E76; Q7M4N9;
Q7Z3G7; Q7Z5U7; Q8WY99; Q8WYA7; Q8WYA8;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 2.
25-OCT-2017, entry version 186.
RecName: Full=Dipeptidyl peptidase 1;
EC=3.4.14.1;
AltName: Full=Cathepsin C;
AltName: Full=Cathepsin J;
AltName: Full=Dipeptidyl peptidase I;
Short=DPP-I;
Short=DPPI;
AltName: Full=Dipeptidyl transferase;
Contains:
RecName: Full=Dipeptidyl peptidase 1 exclusion domain chain;
AltName: Full=Dipeptidyl peptidase I exclusion domain chain;
Contains:
RecName: Full=Dipeptidyl peptidase 1 heavy chain;
AltName: Full=Dipeptidyl peptidase I heavy chain;
Contains:
RecName: Full=Dipeptidyl peptidase 1 light chain;
AltName: Full=Dipeptidyl peptidase I light chain;
Flags: Precursor;
Name=CTSC; Synonyms=CPPI;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT THR-153.
TISSUE=Ileum;
PubMed=7649281; DOI=10.1016/0014-5793(95)00777-7;
Paris A., Strukelj B., Pungercar J., Renko M., Dolenc I., Turk V.;
"Molecular cloning and sequence analysis of human preprocathepsin C.";
FEBS Lett. 369:326-330(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, TISSUE SPECIFICITY, AND
VARIANT THR-153.
PubMed=9092576; DOI=10.1074/jbc.272.15.10260;
Rao N.V., Rao G.V., Hoidal J.R.;
"Human dipeptidyl-peptidase I. Gene characterization, localization,
and expression.";
J. Biol. Chem. 272:10260-10265(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS PLS TYR-236; ARG-286
AND TYR-291, AND VARIANT THR-153.
TISSUE=Blood;
PubMed=11180601;
DOI=10.1002/1098-1004(200102)17:2<152::AID-HUMU10>3.3.CO;2-R;
Allende L.M., Garcia-Perez M.A., Moreno A., Corell A., Carasol M.,
Martinez-Canut P., Arnaiz-Villena A.;
"Cathepsin C gene: first compound heterozygous patient with Papillon-
Lefevre syndrome and a novel symptomless mutation.";
Hum. Mutat. 17:152-153(2001).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS THR-153 AND PLS
HIS-294.
TISSUE=Blood;
PubMed=12809647; DOI=10.1016/S1096-7192(03)00070-2;
Allende L.M., Moreno A., de Unamuno P.;
"A genetic study of cathepsin C gene in two families with Papillon-
Lefevre syndrome.";
Mol. Genet. Metab. 79:146-148(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
THR-153.
TISSUE=Cerebellum, and Rheumatoid arthritic synovial fluid;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
THR-153.
TISSUE=Thyroid;
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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Fetal kidney;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
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.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
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.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT THR-153.
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.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
PROTEIN SEQUENCE OF 25-71; 122-143; 231-235 AND 395-399,
CHARACTERIZATION OF EXCLUSION DOMAIN, AND GLYCOSYLATION.
PubMed=9507095; DOI=10.1016/S0167-4838(97)00173-8;
Cigic B., Krizaj I., Kralj B., Turk V., Pain R.H.;
"Stoichiometry and heterogeneity of the pro-region chain in tetrameric
human cathepsin C.";
Biochim. Biophys. Acta 1382:143-150(1998).
[12]
PROTEIN SEQUENCE OF 25-34; 231-239 AND 395-404, AND CHARACTERIZATION.
PubMed=7665576; DOI=10.1074/jbc.270.37.21626;
Dolenc I., Turk B., Pungercic G., Ritonja A., Turk V.;
"Oligomeric structure and substrate induced inhibition of human
cathepsin C.";
J. Biol. Chem. 270:21626-21631(1995).
[13]
PROTEIN SEQUENCE OF 25-28; 51-61; 114-117 AND 133-139,
CHARACTERIZATION OF EXCLUSION DOMAIN, AND DISULFIDE BONDS.
PubMed=11015218; DOI=10.1021/bi0008837;
Cigic B., Dahl S.W., Pain R.H.;
"The residual pro-part of cathepsin C fulfills the criteria required
for an intramolecular chaperone in folding and stabilizing the human
proenzyme.";
Biochemistry 39:12382-12390(2000).
[14]
PROTEIN SEQUENCE OF 231-290; 310-328 AND 340-383, FUNCTION, ENZYME
REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, GLYCOSYLATION, AND
VARIANT THR-153.
TISSUE=Spleen;
PubMed=1586157; DOI=10.1016/0003-9861(92)90519-3;
McGuire M.J., Lipsky P.E., Thiele D.L.;
"Purification and characterization of dipeptidyl peptidase I from
human spleen.";
Arch. Biochem. Biophys. 295:280-288(1992).
[15]
GLYCOSYLATION AT ASN-29; ASN-53; ASN-119 AND ASN-276.
PubMed=19167329; DOI=10.1016/j.cell.2008.11.047;
Ruiz-Canada C., Kelleher D.J., Gilmore R.;
"Cotranslational and posttranslational N-glycosylation of polypeptides
by distinct mammalian OST isoforms.";
Cell 136:272-283(2009).
[16]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-53.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[20]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 25-143 AND 231-463 IN
COMPLEX WITH CHLORIDE IONS, SUBUNIT, DISULFIDE BONDS, AND
GLYCOSYLATION AT ASN-29.
PubMed=11726493; DOI=10.1093/emboj/20.23.6570;
Turk D., Janjic V., Stern I., Podobnik M., Lamba D., Dahl S.W.,
Lauritzen C., Pedersen J., Turk V., Turk B.;
"Structure of human dipeptidyl peptidase I (cathepsin C): exclusion
domain added to an endopeptidase framework creates the machine for
activation of granular serine proteases.";
EMBO J. 20:6570-6582(2001).
[21]
VARIANTS PLS PHE-249; LEU-252; PRO-272; SER-301; CYS-339 AND CYS-347.
PubMed=10581027; DOI=10.1038/70525;
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.;
"Loss-of-function mutations in the cathepsin C gene result in
periodontal disease and palmoplantar keratosis.";
Nat. Genet. 23:421-424(1999).
[22]
VARIANT HMS ARG-286.
PubMed=10662807; DOI=10.1136/jmg.37.2.88;
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.;
"Haim-Munk syndrome and Papillon-Lefevre syndrome are allelic
mutations in cathepsin C.";
J. Med. Genet. 37:88-94(2000).
[23]
VARIANTS PLS CYS-339 AND CYS-340, AND VARIANT AP1 CYS-347.
PubMed=10662808; DOI=10.1136/jmg.37.2.95;
Hart T.C., Hart P.S., Michalec M.D., Zhang Y., Marazita M.L.,
Cooper M., Yassin O.M., Nusier M., Walker S.;
"Localisation of a gene for prepubertal periodontitis to chromosome
11q14 and identification of a cathepsin C gene mutation.";
J. Med. Genet. 37:95-101(2000).
[24]
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, AND VARIANT THR-153.
PubMed=11106356; DOI=10.1136/jmg.37.12.927;
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.;
"Identification of cathepsin C mutations in ethnically diverse
Papillon-Lefevre syndrome patients.";
J. Med. Genet. 37:927-932(2000).
[25]
VARIANTS PLS SER-39 AND SER-301, AND VARIANT VAL-453.
PubMed=11180012; DOI=10.1046/j.1523-1747.2001.01244.x;
Nakano A., Nomura K., Nakano H., Ono Y., LaForgia S., Pulkkinen L.,
Hashimoto I., Uitto J.;
"Papillon-Lefevre syndrome: mutations and polymorphisms in the
cathepsin C gene.";
J. Invest. Dermatol. 116:339-343(2001).
[26]
VARIANTS PLS PRO-127; PRO-272; CYS-339 AND CYS-429, AND VARIANTS
THR-153 AND LYS-401.
PubMed=11886537; DOI=10.1046/j.0022-202x.2001.01595.x;
Lefevre C., Blanchet-Bardon C., Jobard F., Bouadjar B., Stalder J.-F.,
Cure S., Hoffmann A., Prud'Homme J.-F., Fischer J.;
"Novel point mutations, deletions, and polymorphisms in the cathepsin
C gene in nine families from Europe and North Africa with Papillon-
Lefevre syndrome.";
J. Invest. Dermatol. 117:1657-1661(2001).
[27]
VARIANTS PLS PRO-272 AND ASP-300.
PubMed=11158173; DOI=10.1136/jmg.38.2.96;
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.;
"Evidence of a founder effect for four cathepsin C gene mutations in
Papillon-Lefevre syndrome patients.";
J. Med. Genet. 38:96-101(2001).
[28]
VARIANTS PLS ARG-139 AND PRO-272, AND VARIANT THR-153.
PubMed=12112662; DOI=10.1002/humu.9040;
Zhang Y., Hart P.S., Moretti A.J., Bouwsma O.J., Fisher E.M.,
Dudlicek L., Pettenati M.J., Hart T.C.;
"Biochemical and mutational analyses of the cathepsin c gene (CTSC) in
three North American families with Papillon Lefevre syndrome.";
Hum. Mutat. 20:75-75(2002).
[29]
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, AND VARIANT THR-153.
PubMed=14974080; DOI=10.1002/humu.10314;
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.;
"The role of cathepsin C in Papillon-Lefevre syndrome, prepubertal
periodontitis, and aggressive periodontitis.";
Hum. Mutat. 23:222-228(2004).
[30]
VARIANT PLS ASN-405.
PubMed=15108292; DOI=10.1002/humu.9243;
de Haar S.F., Jansen D.C., Schoenmaker T., De Vree H., Everts V.,
Beertsen W.;
"Loss-of-function mutations in cathepsin C in two families with
Papillon-Lefevre syndrome are associated with deficiency of serine
proteinases in PMNs.";
Hum. Mutat. 23:524-524(2004).
[31]
VARIANT PLS ARG-405.
PubMed=15991336;
de Haar S.F., Mir M., Nguyen M., Kazemi B., Ramezani G.H., Everts V.;
"Gene symbol: CTSC. Disease: Papillon-Lefevre syndrome.";
Hum. Genet. 116:545-545(2005).
[32]
ERRATUM.
de Haar S.F., Mir M., Nguyen M., Kazemi B., Ramezani G.H., Everts V.;
Hum. Genet. 118:533-533(2005).
[33]
VARIANT PLS ASP-300.
PubMed=25799584; DOI=10.1371/journal.pone.0121351;
Erzurumluoglu A.M., Alsaadi M.M., Rodriguez S., Alotaibi T.S.,
Guthrie P.A., Lewis S., Ginwalla A., Gaunt T.R., Alharbi K.K.,
Alsaif F.M., Alsaadi B.M., Day I.N.;
"Proxy molecular diagnosis from whole-exome sequencing reveals
Papillon-Lefevre syndrome caused by a missense mutation in CTSC.";
PLoS ONE 10:E0121351-E0121351(2015).
-!- 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. {ECO:0000269|PubMed:1586157}.
-!- 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:
Name=chloride; Xref=ChEBI:CHEBI:17996;
Note=Binds 1 Cl(-) 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. {ECO:0000269|PubMed:1586157}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
High activity at pH 4.5-6.8. {ECO:0000269|PubMed:1586157};
-!- SUBUNIT: Tetramer of heterotrimers consisting of exclusion domain,
heavy- and light chains. {ECO:0000269|PubMed:11726493,
ECO:0000269|PubMed:1586157}.
-!- INTERACTION:
O76096:CST7; NbExp=2; IntAct=EBI-1047323, EBI-2807448;
-!- SUBCELLULAR LOCATION: Lysosome.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P53634-1; Sequence=Displayed;
Name=2;
IsoId=P53634-2; Sequence=VSP_039123, VSP_039124;
Name=3;
IsoId=P53634-3; Sequence=VSP_043232, VSP_043233;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in lung, kidney
and placenta. Detected at intermediate levels in colon, small
intestine, spleen and pancreas. {ECO:0000269|PubMed:9092576}.
-!- INDUCTION: Up-regulated in lymphocytes by IL2/interleukin-2.
{ECO:0000269|PubMed:9092576}.
-!- PTM: 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.
{ECO:0000269|PubMed:11726493, ECO:0000269|PubMed:1586157,
ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19167329,
ECO:0000269|PubMed:9507095}.
-!- PTM: 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.
-!- 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. {ECO:0000269|PubMed:10581027,
ECO:0000269|PubMed:10662808, ECO:0000269|PubMed:11106356,
ECO:0000269|PubMed:11158173, ECO:0000269|PubMed:11180012,
ECO:0000269|PubMed:11180601, ECO:0000269|PubMed:11886537,
ECO:0000269|PubMed:12112662, ECO:0000269|PubMed:12809647,
ECO:0000269|PubMed:14974080, ECO:0000269|PubMed:15108292,
ECO:0000269|PubMed:15991336, ECO:0000269|PubMed:25799584}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: 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.
{ECO:0000269|PubMed:10662807}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: 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.
{ECO:0000269|PubMed:10662808, ECO:0000269|PubMed:14974080}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the peptidase C1 family.
{ECO:0000255|PROSITE-ProRule:PRU10088, ECO:0000255|PROSITE-
ProRule:PRU10089, ECO:0000255|PROSITE-ProRule:PRU10090}.
-!- SEQUENCE CAUTION:
Sequence=CAD97897.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=CTSCbase; Note=CTSC mutation db;
URL="http://structure.bmc.lu.se/idbase/CTSCbase/";
-----------------------------------------------------------------------
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EMBL; X87212; CAA60671.1; -; mRNA.
EMBL; U79415; AAC51341.1; -; Genomic_DNA.
EMBL; AF234263; AAL48191.1; -; mRNA.
EMBL; AF234264; AAL48192.1; -; mRNA.
EMBL; AF254757; AAL48195.1; -; mRNA.
EMBL; AF525032; AAQ08887.1; -; mRNA.
EMBL; AF525033; AAQ08888.1; -; mRNA.
EMBL; AK292117; BAF84806.1; -; mRNA.
EMBL; AK311923; BAG34864.1; -; mRNA.
EMBL; AK223038; BAD96758.1; -; mRNA.
EMBL; BX537913; CAD97897.1; ALT_INIT; mRNA.
EMBL; AC011088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471185; EAW59364.1; -; Genomic_DNA.
EMBL; BC054028; AAH54028.1; -; mRNA.
EMBL; BC100891; AAI00892.1; -; mRNA.
EMBL; BC100892; AAI00893.1; -; mRNA.
EMBL; BC100893; AAI00894.1; -; mRNA.
EMBL; BC100894; AAI00895.1; -; mRNA.
EMBL; BC109386; AAI09387.1; -; mRNA.
EMBL; BC110071; AAI10072.1; -; mRNA.
EMBL; BC113850; AAI13851.1; -; mRNA.
EMBL; BC113897; AAI13898.1; -; mRNA.
CCDS; CCDS31654.1; -. [P53634-2]
CCDS; CCDS44693.1; -. [P53634-3]
CCDS; CCDS8282.1; -. [P53634-1]
PIR; S23941; S23941.
PIR; S66504; S66504.
RefSeq; NP_001107645.1; NM_001114173.2. [P53634-3]
RefSeq; NP_001805.3; NM_001814.5.
RefSeq; NP_680475.1; NM_148170.4. [P53634-2]
UniGene; Hs.128065; -.
PDB; 1K3B; X-ray; 2.15 A; A=25-143, B=231-394, C=395-463.
PDB; 2DJF; X-ray; 2.00 A; A=25-143, B=231-394, C=395-463.
PDB; 2DJG; X-ray; 2.05 A; A=25-143, B=231-394, C=395-463.
PDB; 3PDF; X-ray; 1.85 A; A=25-463.
PDB; 4CDC; X-ray; 2.40 A; A/D/G/J=25-143, B/E/H/K=230-394, C/F/I/L=395-463.
PDB; 4CDD; X-ray; 2.35 A; A/D=25-144, B/E=230-394, C/F=395-463.
PDB; 4CDE; X-ray; 2.40 A; A/D=25-143, B/E=230-394, C/F=395-463.
PDB; 4CDF; X-ray; 2.20 A; A/D=25-144, B/E=229-394, C/F=395-463.
PDB; 4OEL; X-ray; 1.40 A; A=25-394, B=395-463.
PDB; 4OEM; X-ray; 1.52 A; A=25-394, B=395-463.
PDBsum; 1K3B; -.
PDBsum; 2DJF; -.
PDBsum; 2DJG; -.
PDBsum; 3PDF; -.
PDBsum; 4CDC; -.
PDBsum; 4CDD; -.
PDBsum; 4CDE; -.
PDBsum; 4CDF; -.
PDBsum; 4OEL; -.
PDBsum; 4OEM; -.
ProteinModelPortal; P53634; -.
SMR; P53634; -.
BioGrid; 107502; 25.
IntAct; P53634; 22.
MINT; MINT-4655964; -.
STRING; 9606.ENSP00000227266; -.
BindingDB; P53634; -.
ChEMBL; CHEMBL2252; -.
GuidetoPHARMACOLOGY; 2344; -.
MEROPS; C01.070; -.
iPTMnet; P53634; -.
PhosphoSitePlus; P53634; -.
SwissPalm; P53634; -.
BioMuta; CTSC; -.
DMDM; 317373330; -.
EPD; P53634; -.
MaxQB; P53634; -.
PaxDb; P53634; -.
PeptideAtlas; P53634; -.
PRIDE; P53634; -.
TopDownProteomics; P53634-1; -. [P53634-1]
DNASU; 1075; -.
Ensembl; ENST00000227266; ENSP00000227266; ENSG00000109861. [P53634-1]
Ensembl; ENST00000524463; ENSP00000432541; ENSG00000109861. [P53634-2]
Ensembl; ENST00000529974; ENSP00000433539; ENSG00000109861. [P53634-3]
GeneID; 1075; -.
KEGG; hsa:1075; -.
UCSC; uc001pck.5; human. [P53634-1]
CTD; 1075; -.
DisGeNET; 1075; -.
EuPathDB; HostDB:ENSG00000109861.15; -.
GeneCards; CTSC; -.
HGNC; HGNC:2528; CTSC.
HPA; CAB025364; -.
HPA; HPA066610; -.
HPA; HPA068434; -.
MalaCards; CTSC; -.
MIM; 170650; phenotype.
MIM; 245000; phenotype.
MIM; 245010; phenotype.
MIM; 602365; gene.
neXtProt; NX_P53634; -.
OpenTargets; ENSG00000109861; -.
Orphanet; 2342; Haim-Munk syndrome.
Orphanet; 678; Papillon-Lefevre syndrome.
PharmGKB; PA27028; -.
eggNOG; KOG1543; Eukaryota.
eggNOG; COG4870; LUCA.
GeneTree; ENSGT00900000140859; -.
HOGENOM; HOG000127503; -.
HOVERGEN; HBG005248; -.
InParanoid; P53634; -.
KO; K01275; -.
OMA; YHHTGLR; -.
OrthoDB; EOG091G06TT; -.
PhylomeDB; P53634; -.
TreeFam; TF313225; -.
BioCyc; MetaCyc:HS03265-MONOMER; -.
BRENDA; 3.4.14.1; 2681.
Reactome; R-HSA-204005; COPII (Coat Protein 2) Mediated Vesicle Transport.
Reactome; R-HSA-2132295; MHC class II antigen presentation.
Reactome; R-HSA-5694530; Cargo concentration in the ER.
Reactome; R-HSA-6798695; Neutrophil degranulation.
SABIO-RK; P53634; -.
ChiTaRS; CTSC; human.
EvolutionaryTrace; P53634; -.
GeneWiki; Cathepsin_C; -.
GenomeRNAi; 1075; -.
PMAP-CutDB; P53634; -.
PRO; PR:P53634; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000109861; -.
ExpressionAtlas; P53634; baseline and differential.
Genevisible; P53634; HS.
GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
GO; GO:0005813; C:centrosome; IDA:HPA.
GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; TAS:Reactome.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IEA:GOC.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005764; C:lysosome; ISS:BHF-UCL.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0051087; F:chaperone binding; ISS:BHF-UCL.
GO; GO:0031404; F:chloride ion binding; IEA:Ensembl.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
GO; GO:0008234; F:cysteine-type peptidase activity; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0016505; F:peptidase activator activity involved in apoptotic process; IEA:Ensembl.
GO; GO:0019902; F:phosphatase binding; ISS:BHF-UCL.
GO; GO:0043621; F:protein self-association; IEA:Ensembl.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:Ensembl.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0048208; P:COPII vesicle coating; TAS:Reactome.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; TAS:Reactome.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IEA:Ensembl.
GO; GO:1903052; P:positive regulation of proteolysis involved in cellular protein catabolic process; ISS:ParkinsonsUK-UCL.
GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IBA:GO_Central.
GO; GO:0010033; P:response to organic substance; IEA:Ensembl.
GO; GO:0001913; P:T cell mediated cytotoxicity; IEA:Ensembl.
Gene3D; 2.40.128.80; -; 1.
InterPro; IPR014882; CathepsinC_exc.
InterPro; IPR036496; CathepsinC_exc_dom_sf.
InterPro; IPR025661; Pept_asp_AS.
InterPro; IPR000169; Pept_cys_AS.
InterPro; IPR025660; Pept_his_AS.
InterPro; IPR013128; Peptidase_C1A.
InterPro; IPR000668; Peptidase_C1A_C.
PANTHER; PTHR12411; PTHR12411; 1.
Pfam; PF08773; CathepsinC_exc; 1.
Pfam; PF00112; Peptidase_C1; 1.
PRINTS; PR00705; PAPAIN.
SMART; SM00645; Pept_C1; 1.
SUPFAM; SSF75001; SSF75001; 1.
PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chloride; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
Glycoprotein; Hydrolase; Lysosome; Palmoplantar keratoderma;
Polymorphism; Protease; Reference proteome; Signal; Thiol protease;
Zymogen.
SIGNAL 1 24 {ECO:0000269|PubMed:11015218,
ECO:0000269|PubMed:7665576,
ECO:0000269|PubMed:9507095}.
CHAIN 25 134 Dipeptidyl peptidase 1 exclusion domain
chain.
/FTId=PRO_0000026338.
PROPEP 135 230 {ECO:0000269|PubMed:1586157,
ECO:0000269|PubMed:7665576,
ECO:0000269|PubMed:9507095}.
/FTId=PRO_0000026339.
CHAIN 231 394 Dipeptidyl peptidase 1 heavy chain.
/FTId=PRO_0000026340.
CHAIN 395 463 Dipeptidyl peptidase 1 light chain.
/FTId=PRO_0000026341.
ACT_SITE 258 258
ACT_SITE 405 405
ACT_SITE 427 427
BINDING 302 302 Chloride.
BINDING 304 304 Chloride; via amide nitrogen.
BINDING 347 347 Chloride.
CARBOHYD 29 29 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11726493,
ECO:0000269|PubMed:19167329}.
CARBOHYD 53 53 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19167329}.
CARBOHYD 119 119 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19167329}.
CARBOHYD 276 276 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19167329}.
DISULFID 30 118
DISULFID 54 136
DISULFID 255 298
DISULFID 291 331
DISULFID 321 337
VAR_SEQ 107 141 YKEEGSKVTTYCNETMTGWVHDVLGRNWACFTGKK -> DV
TDFISHLFMQLGTVGIYDLPHLRNKLAMNRRWG (in
isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_043232.
VAR_SEQ 107 137 YKEEGSKVTTYCNETMTGWVHDVLGRNWACF -> DVTDFI
SHLFMQLGTVGIYDLPHLRNKLVIK (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_039123.
VAR_SEQ 138 463 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_039124.
VAR_SEQ 142 463 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_043233.
VARIANT 39 39 W -> S (in PLS; dbSNP:rs104894210).
{ECO:0000269|PubMed:11180012}.
/FTId=VAR_016933.
VARIANT 67 74 Missing (in PLS).
{ECO:0000269|PubMed:11106356}.
/FTId=VAR_019035.
VARIANT 127 127 H -> P (in PLS; dbSNP:rs104894216).
{ECO:0000269|PubMed:11886537}.
/FTId=VAR_016934.
VARIANT 129 129 V -> E (in PLS; dbSNP:rs760130711).
{ECO:0000269|PubMed:14974080}.
/FTId=VAR_019036.
VARIANT 139 139 G -> R (in PLS; dbSNP:rs749103588).
{ECO:0000269|PubMed:12112662,
ECO:0000269|PubMed:14974080}.
/FTId=VAR_019037.
VARIANT 153 153 I -> T (in dbSNP:rs217086).
{ECO:0000269|PubMed:11106356,
ECO:0000269|PubMed:11180601,
ECO:0000269|PubMed:11886537,
ECO:0000269|PubMed:12112662,
ECO:0000269|PubMed:12809647,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:14974080,
ECO:0000269|PubMed:1586157,
ECO:0000269|PubMed:7649281,
ECO:0000269|PubMed:9092576,
ECO:0000269|Ref.6, ECO:0000269|Ref.9}.
/FTId=VAR_016943.
VARIANT 236 236 D -> Y (in PLS; dbSNP:rs764724707).
{ECO:0000269|PubMed:11180601,
ECO:0000269|PubMed:14974080}.
/FTId=VAR_019038.
VARIANT 249 249 V -> F (in PLS).
{ECO:0000269|PubMed:10581027,
ECO:0000269|PubMed:14974080}.
/FTId=VAR_009541.
VARIANT 252 252 Q -> L (in PLS; dbSNP:rs104894207).
{ECO:0000269|PubMed:10581027,
ECO:0000269|PubMed:14974080}.
/FTId=VAR_009542.
VARIANT 272 272 R -> H (in PLS; dbSNP:rs587777534).
{ECO:0000269|PubMed:14974080}.
/FTId=VAR_019039.
VARIANT 272 272 R -> P (in PLS; dbSNP:rs587777534).
{ECO:0000269|PubMed:10581027,
ECO:0000269|PubMed:11106356,
ECO:0000269|PubMed:11158173,
ECO:0000269|PubMed:11886537,
ECO:0000269|PubMed:12112662}.
/FTId=VAR_009543.
VARIANT 286 286 Q -> R (in HMS and PLS;
dbSNP:rs104894208).
{ECO:0000269|PubMed:10662807,
ECO:0000269|PubMed:11180601}.
/FTId=VAR_016935.
VARIANT 291 291 C -> Y (in PLS; dbSNP:rs748729285).
{ECO:0000269|PubMed:11180601}.
/FTId=VAR_019040.
VARIANT 294 294 Y -> H (in PLS).
{ECO:0000269|PubMed:12809647}.
/FTId=VAR_039686.
VARIANT 300 300 G -> D (in PLS).
{ECO:0000269|PubMed:11158173,
ECO:0000269|PubMed:25799584}.
/FTId=VAR_019041.
VARIANT 300 300 G -> S (in PLS).
{ECO:0000269|PubMed:11106356}.
/FTId=VAR_019042.
VARIANT 301 301 G -> S (in PLS; dbSNP:rs104894214).
{ECO:0000269|PubMed:10581027,
ECO:0000269|PubMed:11106356,
ECO:0000269|PubMed:11180012,
ECO:0000269|PubMed:14974080}.
/FTId=VAR_009544.
VARIANT 301 301 G -> V (in PLS).
{ECO:0000269|PubMed:11106356}.
/FTId=VAR_019043.
VARIANT 304 304 Y -> N (in PLS).
{ECO:0000269|PubMed:11106356}.
/FTId=VAR_019044.
VARIANT 312 312 Q -> R (in PLS).
{ECO:0000269|PubMed:14974080}.
/FTId=VAR_019045.
VARIANT 319 319 E -> G (in PLS).
{ECO:0000269|PubMed:11106356}.
/FTId=VAR_019046.
VARIANT 339 339 R -> C (in PLS).
{ECO:0000269|PubMed:10581027,
ECO:0000269|PubMed:10662808,
ECO:0000269|PubMed:11106356,
ECO:0000269|PubMed:11886537,
ECO:0000269|PubMed:14974080}.
/FTId=VAR_009545.
VARIANT 340 340 Y -> C (in PLS).
{ECO:0000269|PubMed:10662808,
ECO:0000269|PubMed:11106356}.
/FTId=VAR_016944.
VARIANT 347 347 Y -> C (in PLS and AP1;
dbSNP:rs104894211).
{ECO:0000269|PubMed:10581027,
ECO:0000269|PubMed:10662808,
ECO:0000269|PubMed:14974080}.
/FTId=VAR_009546.
VARIANT 401 401 E -> K (in dbSNP:rs200627023).
{ECO:0000269|PubMed:11886537}.
/FTId=VAR_016945.
VARIANT 405 405 H -> N (in PLS).
{ECO:0000269|PubMed:15108292}.
/FTId=VAR_027249.
VARIANT 405 405 H -> R (in PLS; dbSNP:rs151269219).
{ECO:0000269|PubMed:15991336}.
/FTId=VAR_027250.
VARIANT 412 412 Y -> C (in AP1; dbSNP:rs28937571).
{ECO:0000269|PubMed:14974080}.
/FTId=VAR_019047.
VARIANT 429 429 W -> C (in PLS; dbSNP:rs104894215).
{ECO:0000269|PubMed:11886537}.
/FTId=VAR_016936.
VARIANT 447 447 E -> G (in PLS).
{ECO:0000269|PubMed:11106356,
ECO:0000269|PubMed:14974080}.
/FTId=VAR_019048.
VARIANT 453 453 I -> V (rare polymorphism;
dbSNP:rs3888798).
{ECO:0000269|PubMed:11180012}.
/FTId=VAR_016946.
CONFLICT 63 63 K -> I (in Ref. 6; BAD96758).
{ECO:0000305}.
CONFLICT 237 237 W -> V (in Ref. 14; AA sequence).
{ECO:0000305}.
CONFLICT 321 321 C -> S (in Ref. 14; AA sequence).
{ECO:0000305}.
CONFLICT 355 355 C -> M (in Ref. 14; AA sequence).
{ECO:0000305}.
CONFLICT 366 366 H -> R (in Ref. 14; AA sequence).
{ECO:0000305}.
CONFLICT 376 378 VYD -> YVY (in Ref. 14; AA sequence).
{ECO:0000305}.
HELIX 32 35 {ECO:0000244|PDB:4OEL}.
STRAND 37 48 {ECO:0000244|PDB:4OEL}.
TURN 49 51 {ECO:0000244|PDB:1K3B}.
HELIX 54 56 {ECO:0000244|PDB:4OEL}.
STRAND 60 69 {ECO:0000244|PDB:4OEL}.
TURN 70 72 {ECO:0000244|PDB:4OEL}.
STRAND 73 75 {ECO:0000244|PDB:4OEL}.
STRAND 81 87 {ECO:0000244|PDB:4OEL}.
TURN 88 90 {ECO:0000244|PDB:4OEL}.
STRAND 91 96 {ECO:0000244|PDB:4OEL}.
STRAND 99 110 {ECO:0000244|PDB:4OEL}.
STRAND 113 121 {ECO:0000244|PDB:4OEL}.
STRAND 123 128 {ECO:0000244|PDB:4OEL}.
STRAND 133 141 {ECO:0000244|PDB:4OEL}.
STRAND 254 256 {ECO:0000244|PDB:2DJF}.
HELIX 258 274 {ECO:0000244|PDB:4OEL}.
TURN 275 277 {ECO:0000244|PDB:4OEL}.
HELIX 285 291 {ECO:0000244|PDB:4OEL}.
HELIX 297 299 {ECO:0000244|PDB:4OEM}.
HELIX 303 306 {ECO:0000244|PDB:4OEL}.
HELIX 309 313 {ECO:0000244|PDB:4OEL}.
HELIX 319 321 {ECO:0000244|PDB:4OEL}.
STRAND 342 347 {ECO:0000244|PDB:4OEL}.
HELIX 357 367 {ECO:0000244|PDB:4OEL}.
STRAND 370 374 {ECO:0000244|PDB:4OEL}.
HELIX 378 382 {ECO:0000244|PDB:4OEL}.
STRAND 385 388 {ECO:0000244|PDB:4OEL}.
STRAND 405 414 {ECO:0000244|PDB:4OEL}.
TURN 416 418 {ECO:0000244|PDB:4OEL}.
STRAND 421 426 {ECO:0000244|PDB:4OEL}.
STRAND 431 433 {ECO:0000244|PDB:2DJG}.
STRAND 438 442 {ECO:0000244|PDB:4OEL}.
TURN 443 446 {ECO:0000244|PDB:4CDE}.
HELIX 447 449 {ECO:0000244|PDB:4OEL}.
STRAND 455 459 {ECO:0000244|PDB:4OEL}.
SEQUENCE 463 AA; 51854 MW; 4C9C7C24D900CEE6 CRC64;
MGAGPSLLLA ALLLLLSGDG AVRCDTPANC TYLDLLGTWV FQVGSSGSQR DVNCSVMGPQ
EKKVVVYLQK LDTAYDDLGN SGHFTIIYNQ GFEIVLNDYK WFAFFKYKEE GSKVTTYCNE
TMTGWVHDVL GRNWACFTGK KVGTASENVY VNIAHLKNSQ EKYSNRLYKY DHNFVKAINA
IQKSWTATTY MEYETLTLGD MIRRSGGHSR KIPRPKPAPL TAEIQQKILH LPTSWDWRNV
HGINFVSPVR NQASCGSCYS FASMGMLEAR IRILTNNSQT PILSPQEVVS CSQYAQGCEG
GFPYLIAGKY AQDFGLVEEA CFPYTGTDSP CKMKEDCFRY YSSEYHYVGG FYGGCNEALM
KLELVHHGPM AVAFEVYDDF LHYKKGIYHH TGLRDPFNPF ELTNHAVLLV GYGTDSASGM
DYWIVKNSWG TGWGENGYFR IRRGTDECAI ESIAVAATPI PKL


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EIAAB05418 Cathepsin C,Cathepsin J,CPPI,CTSC,Dipeptidyl peptidase 1,Dipeptidyl peptidase I,Dipeptidyl transferase,DPPI,DPP-I,Homo sapiens,Human
EIAAB05421 Cathepsin C,Cathepsin J,Ctsc,Dipeptidyl peptidase 1,Dipeptidyl peptidase I,Dipeptidyl transferase,DPPI,DPP-I,Mouse,Mus musculus
EIAAB05420 Bos taurus,Bovine,Cathepsin C,Cathepsin J,CTSC,Dipeptidyl peptidase 1,Dipeptidyl peptidase I,Dipeptidyl transferase,DPPI,DPP-I
EIAAB05419 Cathepsin C,Cathepsin J,Ctsc,Dipeptidyl peptidase 1,Dipeptidyl peptidase I,Dipeptidyl transferase,DPPI,DPP-I,Rat,Rattus norvegicus
EIAAB11845 Dipeptidyl aminopeptidase III,Dipeptidyl arylamidase III,Dipeptidyl peptidase 3,Dipeptidyl peptidase III,DPP III,DPP3,Homo sapiens,Human
EIAAB11846 Dipeptidyl aminopeptidase III,Dipeptidyl arylamidase III,Dipeptidyl peptidase 3,Dipeptidyl peptidase III,DPP III,Dpp3,Mouse,Mus musculus
EIAAB11847 Dipeptidyl aminopeptidase III,Dipeptidyl arylamidase III,Dipeptidyl peptidase 3,Dipeptidyl peptidase III,DPP III,Dpp3,Rat,Rattus norvegicus
EIAAB11855 Dipeptidyl peptidase 9,Dipeptidyl peptidase IX,Dipeptidyl peptidase-like protein 9,DP9,DPLP9,DPP IX,Dpp9,Mouse,Mus musculus
EIAAB11849 Dipeptidyl aminopeptidase-like protein 6,Dipeptidyl aminopeptidase-related protein,Dipeptidyl peptidase 6,Dipeptidyl peptidase IV-like protein,Dipeptidyl peptidase VI,DPP VI,DPP6,DPPX,Homo sapiens,Hum
EIAAB11848 Dipeptidyl aminopeptidase-like protein 6,Dipeptidyl aminopeptidase-related protein,Dipeptidyl peptidase 6,Dipeptidyl peptidase IV-like protein,Dipeptidyl peptidase VI,DPP VI,Dpp6,DPPX,Rat,Rattus norve
EIAAB05417 Canis familiaris,Canis lupus familiaris,Cathepsin C,Cathepsin J,CTSC,Dipeptidyl peptidase 1,Dipeptidyl peptidase I,Dipeptidyl transferase,Dog,DPPI,DPP-I
EIAAB11852 Dipeptidyl peptidase 8,Dipeptidyl peptidase IV-related protein 1,Dipeptidyl peptidase VIII,DP8,DPP VIII,DPP8,DPRP1,DPRP-1,Homo sapiens,Human,MSTP097,MSTP135,MSTP141,Prolyl dipeptidase DPP8
EIAAB11850 Bos taurus,Bovine,Dipeptidyl aminopeptidase-like protein 6,Dipeptidyl aminopeptidase-related protein,Dipeptidyl peptidase 6,Dipeptidyl peptidase IV-like protein,Dipeptidyl peptidase VI,DPP VI,DPP6,DPP
EIAAB11851 Dipeptidyl aminopeptidase-like protein 6,Dipeptidyl aminopeptidase-related protein,Dipeptidyl peptidase 6,Dipeptidyl peptidase IV-like protein,Dipeptidyl peptidase VI,DPP VI,Dpp6,Dpp-6,DPPX,Mouse,Mus
20-321-175240 DIPEPTIDYL PEPTIDASE IV (DPP IV). CD26 - MONOCLONAL ANTIBODY TO RAT DIPEPTIDYL PEPTIDASE IV (DPP IV). CD26; EC 3.4.14.5; Dipeptidyl peptidase IV; DPP IV; T-cell activation antigen CD26; TP103; Adenosi 0.1 mg
EIAAB11840 Dipeptidyl peptidase X,DPP X,Dpp10,Inactive dipeptidyl peptidase 10,Kv4 potassium channel auxiliary subunit,Rat,Rattus norvegicus
15-288-21442 Dipeptidyl peptidase 4 - EC 3.4.14.5; Dipeptidyl peptidase IV; DPP IV; T-cell activation antigen CD26; TP103; Adenosine deaminase complexing protein 2; ADABP Polyclonal 0.05 mg
15-288-21442 Dipeptidyl peptidase 4 - EC 3.4.14.5; Dipeptidyl peptidase IV; DPP IV; T-cell activation antigen CD26; TP103; Adenosine deaminase complexing protein 2; ADABP Polyclonal 0.1 mg
E0884r ELISA kit Bile canaliculus domain-specific membrane glycoprotein,Cd26,Dipeptidyl peptidase 4,Dipeptidyl peptidase IV,DPP IV,Dpp4,GP110 glycoprotein,Rat,Rattus norvegicus,T-cell activation antigen CD2 96T
EIAAB11841 Dipeptidyl peptidase X,DPP X,Dpp10,Inactive dipeptidyl peptidase 10,Mouse,Mus musculus


 

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