Dipeptidyl peptidase 1 precursor - Mus musculus (Mouse)

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P97821 (CATC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 110. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Dipeptidyl peptidase 1
EC=3.4.14.1

Alternative name(s):
Cathepsin C
Cathepsin J
Dipeptidyl peptidase I
Short name=DPP-I
Short name=DPPI
Dipeptidyl transferase

Cleaved into the following 3 chains:

Dipeptidyl peptidase 1 exclusion domain chain
Alternative name(s):
Dipeptidyl peptidase I exclusion domain chain
Dipeptidyl peptidase 1 heavy chain
Alternative name(s):
Dipeptidyl peptidase I heavy chain
Dipeptidyl peptidase 1 light chain
Alternative name(s):
Dipeptidyl peptidase I light chain

Gene names

Name:

Ctsc

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	462 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Thiol protease. Has dipeptidylpeptidase activity. Can act as both an exopeptidase and endopeptidase. Can degrade glucagon. Plays a role in the generation of cytotoxic lymphocyte effector function.
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 By similarity.
Subunit structure	Tetramer of heterotrimers consisting of exclusion domain, heavy- and light chains By similarity.
Subcellular location	Lysosome.
Tissue specificity	Broadly distributed, but higher levels found in lung, liver, kidney and spleen. Lower levels found in testis and brain.
Sequence similarities	Belongs to the peptidase C1 family.

Ontologies

Keywords
Cellular component	Lysosome
Domain	Signal
Ligand	Chloride
Molecular function	Hydrolase Protease Thiol protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	T cell mediated cytotoxicity Inferred from genetic interaction PubMed 20435891. Source: UniProtKB aging Inferred from electronic annotation. Source: Compara proteolysis Inferred from mutant phenotype PubMed 20435891. Source: UniProtKB response to organic substance Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: Compara endoplasmic reticulum Inferred from electronic annotation. Source: Compara lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	chloride ion binding Inferred from electronic annotation. Source: Compara cysteine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW serine-type endopeptidase activity Inferred from mutant phenotype PubMed 20435891. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

Potential

Chain

25 – 134

110

Dipeptidyl peptidase 1 exclusion domain chain By similarity

PRO_0000026346

Propeptide

135 – 230

By similarity

PRO_0000026347

Chain

231 – 393

163

Dipeptidyl peptidase 1 heavy chain

PRO_0000026348

Chain

394 – 462

Dipeptidyl peptidase 1 light chain

PRO_0000026349

Sites

Active site

257

By similarity

Active site

404

By similarity

Active site

426

By similarity

Binding site

301

Chloride By similarity

Binding site

303

Chloride; via amide nitrogen By similarity

Binding site

346

Chloride By similarity

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

275

N-linked (GlcNAc...) Potential

Disulfide bond

30 ↔ 118

By similarity

Disulfide bond

54 ↔ 136

By similarity

Disulfide bond

254 ↔ 297

By similarity

Disulfide bond

290 ↔ 330

By similarity

Disulfide bond

320 ↔ 336

By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P97821 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 56574B38D7DF4710
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FASTA

462

52,376

        10         20         30         40         50         60 
MGPWTHSLRA VLLLVLLGVC TVRSDTPANC TYPDLLGTWV FQVGPRSSRS DINCSVMEAT 

        70         80         90        100        110        120 
EEKVVVHLKK LDTAYDELGN SGHFTLIYNQ GFEIVLNDYK WFAFFKYEVR GHTAISYCHE 

       130        140        150        160        170        180 
TMTGWVHDVL GRNWACFVGK KVESHIEKVN MNAAHLGGLQ ERYSERLYTH NHNFVKAINT 

       190        200        210        220        230        240 
VQKSWTATAY KEYEKMSLRD LIRRSGHSQR IPRPKPAPMT DEIQQQILNL PESWDWRNVQ 

       250        260        270        280        290        300 
GVNYVSPVRN QESCGSCYSF ASMGMLEARI RILTNNSQTP ILSPQEVVSC SPYAQGCDGG 

       310        320        330        340        350        360 
FPYLIAGKYA QDFGVVEESC FPYTAKDSPC KPRENCLRYY SSDYYYVGGF YGGCNEALMK 

       370        380        390        400        410        420 
LELVKHGPMA VAFEVHDDFL HYHSGIYHHT GLSDPFNPFE LTNHAVLLVG YGRDPVTGIE 

       430        440        450        460 
YWIIKNSWGS NWGESGYFRI RRGTDECAIE SIAVAAIPIP KL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning, chromosomal localization, and expression of murine dipeptidyl peptidase I." Pham C.T.N., Armstrong R.J., Zimonjic D.B., Popescu N.C., Payan D.G., Ley T.J. J. Biol. Chem. 272:10695-10703(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: 129/SvJ.
[2]	"Cloning and characterization of the cDNA encoding mouse dipeptidyl peptidase I (cathepsin C)." McGuire M.J., Lipsky P.E., Thiele D.L. Biochim. Biophys. Acta 1351:267-273(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c.
[3]	McGuire M.J., Lipsky P.E., Francisco N.M.C., Thiele D.L. Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[4]	"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]. Strain: C57BL/6. Tissue: Eye.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U89269 mRNA. Translation: AAB49457.1. U74683 mRNA. Translation: AAB58400.3. BC067063 mRNA. Translation: AAH67063.1.
IPI	IPI00130015.
RefSeq	NP_034112.3. NM_009982.4.
UniGene	Mm.322945.
3D structure databases
ProteinModelPortal	P97821.
SMR	P97821. Positions 25-144, 174-462.
ModBase	Search...
Protein family/group databases
MEROPS	C01.070.
PTM databases
PhosphoSite	P97821.
Proteomic databases
PaxDb	P97821.
PRIDE	P97821.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000032779; ENSMUSP00000032779; ENSMUSG00000030560.
GeneID	13032.
KEGG	mmu:13032.
Organism-specific databases
CTD	1075.
MGI	MGI:109553. Ctsc.
Phylogenomic databases
eggNOG	COG4870.
HOGENOM	HOG000068022.
HOVERGEN	HBG005248.
InParanoid	P97821.
KO	K01275.
OMA	YDDFLHY.
OrthoDB	EOG4H19VZ.
Gene expression databases
ArrayExpress	P97821.
Bgee	P97821.
CleanEx	MM_CTSC.
Genevestigator	P97821.
Family and domain databases
InterPro	IPR014882. CathepsinC_exc. IPR025661. Pept_asp_AS. IPR000169. Pept_cys_AS. IPR025660. Pept_his_AS. IPR013128. Peptidase_C1A. IPR000668. Peptidase_C1A_C. [Graphical view]
PANTHER	PTHR12411. PTHR12411. 1 hit.
Pfam	PF08773. CathepsinC_exc. 1 hit. PF00112. Peptidase_C1. 1 hit. [Graphical view]
PRINTS	PR00705. PAPAIN.
SMART	SM00645. Pept_C1. 1 hit. [Graphical view]
PROSITE	PS00640. THIOL_PROTEASE_ASN. 1 hit. PS00139. THIOL_PROTEASE_CYS. 1 hit. PS00639. THIOL_PROTEASE_HIS. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P97821.
ChEMBL	CHEMBL3454.
ChiTaRS	CTSC. mouse.
NextBio	282904.
SOURCE	Search...

Entry information

Entry name

CATC_MOUSE

Accession

Primary (citable) accession number: P97821
Secondary accession number(s): O08853

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	May 1, 1997
Last modified:	May 1, 2013
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following 3 chains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents