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P53634

- CATC_HUMAN

UniProt

P53634 - CATC_HUMAN

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Protein
Dipeptidyl peptidase 1
Gene
CTSC, CPPI
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Cofactori

Binds 1 chloride ion per heavy chain.

Enzyme regulationi

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

pH dependencei

High activity at pH 4.5-6.8.1 Publication

Sites

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

GO - Molecular functioni

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

GO - Biological processi

  1. T cell mediated cytotoxicity Source: Ensembl
  2. aging Source: Ensembl
  3. immune response Source: ProtInc
  4. positive regulation of apoptotic signaling pathway Source: Ensembl
  5. positive regulation of proteolysis involved in cellular protein catabolic process Source: ParkinsonsUK-UCL
  6. proteolysis Source: UniProtKB
  7. response to organic substance Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Ligandi

Chloride

Enzyme and pathway databases

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

Protein family/group databases

MEROPSiC01.070.

Names & Taxonomyi

Protein namesi
Recommended name:
Dipeptidyl peptidase 1 (EC:3.4.14.1)
Alternative name(s):
Cathepsin C
Cathepsin J
Dipeptidyl peptidase I
Short name:
DPP-I
Short name:
DPPI
Dipeptidyl transferase
Cleaved into the following 3 chains:
Alternative name(s):
Dipeptidyl peptidase I exclusion domain chain
Alternative name(s):
Dipeptidyl peptidase I heavy chain
Alternative name(s):
Dipeptidyl peptidase I light chain
Gene namesi
Name:CTSC
Synonyms:CPPI
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:2528. CTSC.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Involvement in diseasei

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

Keywords - Diseasei

Disease mutation, Palmoplantar keratoderma

Organism-specific databases

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 24243 Publications
Add
BLAST
Chaini25 – 134110Dipeptidyl peptidase 1 exclusion domain chain
PRO_0000026338Add
BLAST
Propeptidei135 – 23096
PRO_0000026339Add
BLAST
Chaini231 – 394164Dipeptidyl peptidase 1 heavy chain
PRO_0000026340Add
BLAST
Chaini395 – 46369Dipeptidyl peptidase 1 light chain
PRO_0000026341Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi29 – 291N-linked (GlcNAc...)2 Publications
Disulfide bondi30 ↔ 1182 Publications
Glycosylationi53 – 531N-linked (GlcNAc...)2 Publications
Disulfide bondi54 ↔ 1362 Publications
Glycosylationi119 – 1191N-linked (GlcNAc...)1 Publication
Disulfide bondi255 ↔ 2982 Publications
Glycosylationi276 – 2761N-linked (GlcNAc...)1 Publication
Disulfide bondi291 ↔ 3312 Publications
Disulfide bondi321 ↔ 3372 Publications

Post-translational modificationi

N-glycosylated. While glycosylation at Asn-53, Asn-119 and Asn-276 is mediated by STT3A-containing complexes, glycosylation at Asn-29 is mediated STT3B-containing complexes.4 Publications
In approximately 50% of the complexes the exclusion domain is cleaved at position 58 or 61. The two parts of the exclusion domain are held together by a disulfide bond.

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQBiP53634.
PaxDbiP53634.
PRIDEiP53634.

PTM databases

PhosphoSiteiP53634.

Miscellaneous databases

PMAP-CutDBP53634.

Expressioni

Tissue specificityi

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

Inductioni

Up-regulated in lymphocytes by IL2/interleukin-2.2 Publications

Gene expression databases

ArrayExpressiP53634.
BgeeiP53634.
GenevestigatoriP53634.

Organism-specific databases

HPAiCAB025364.

Interactioni

Subunit structurei

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

Binary interactionsi

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

Protein-protein interaction databases

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

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP53634.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG4870.
HOGENOMiHOG000127503.
HOVERGENiHBG005248.
InParanoidiP53634.
KOiK01275.
OMAiYDDFLHY.
OrthoDBiEOG74R1QK.
PhylomeDBiP53634.
TreeFamiTF313225.

Family and domain databases

Gene3Di2.40.128.80. 1 hit.
InterProiIPR014882. CathepsinC_exc.
IPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PfamiPF08773. CathepsinC_exc. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSiPR00705. PAPAIN.
SMARTiSM00645. Pept_C1. 1 hit.
[Graphical view]
SUPFAMiSSF75001. SSF75001. 1 hit.
PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

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

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

« Hide

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

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

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

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

Note: No experimental confirmation available.

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

Sequence cautioni

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

Natural variant

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei107 – 14135YKEEG…FTGKK → DVTDFISHLFMQLGTVGIYD LPHLRNKLAMNRRWG in isoform 3.
VSP_043232Add
BLAST
Alternative sequencei107 – 13731YKEEG…NWACF → DVTDFISHLFMQLGTVGIYD LPHLRNKLVIK in isoform 2.
VSP_039123Add
BLAST
Alternative sequencei138 – 463326Missing in isoform 2.
VSP_039124Add
BLAST
Alternative sequencei142 – 463322Missing in isoform 3.
VSP_043233Add
BLAST

Sequence conflict

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

Sequence databases

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

Genome annotation databases

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

Polymorphism databases

DMDMi317373330.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

CTSCbase

CTSC mutation db

Sequence databases

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

3D structure databases

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

Protein-protein interaction databases

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

Chemistry

BindingDBi P53634.
ChEMBLi CHEMBL2252.

Protein family/group databases

MEROPSi C01.070.

PTM databases

PhosphoSitei P53634.

Polymorphism databases

DMDMi 317373330.

Proteomic databases

MaxQBi P53634.
PaxDbi P53634.
PRIDEi P53634.

Protocols and materials databases

DNASUi 1075.
Structural Biology Knowledgebase Search...

Genome annotation databases

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

Organism-specific databases

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

Phylogenomic databases

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

Enzyme and pathway databases

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

Miscellaneous databases

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

Gene expression databases

ArrayExpressi P53634.
Bgeei P53634.
Genevestigatori P53634.

Family and domain databases

Gene3Di 2.40.128.80. 1 hit.
InterProi IPR014882. CathepsinC_exc.
IPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
[Graphical view ]
PANTHERi PTHR12411. PTHR12411. 1 hit.
Pfami PF08773. CathepsinC_exc. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view ]
PRINTSi PR00705. PAPAIN.
SMARTi SM00645. Pept_C1. 1 hit.
[Graphical view ]
SUPFAMi SSF75001. SSF75001. 1 hit.
PROSITEi PS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

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

Entry informationi

Entry nameiCATC_HUMAN
AccessioniPrimary (citable) accession number: P53634
Secondary accession number(s): A8K7V2
, B5MDD5, Q2HIY8, Q53G93, Q71E75, Q71E76, Q7M4N9, Q7Z3G7, Q7Z5U7, Q8WY99, Q8WYA7, Q8WYA8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 11, 2011
Last modified: September 3, 2014
This is version 155 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Documents

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

External Data

Dasty 3

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