1JQP

dipeptidyl peptidase I (cathepsin C), a tetrameric cysteine protease of the papain family

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001913	biological_process	T cell mediated cytotoxicity
A	0004197	molecular_function	cysteine-type endopeptidase activity
A	0004252	molecular_function	serine-type endopeptidase activity
A	0005615	cellular_component	extracellular space
A	0005737	cellular_component	cytoplasm
A	0005764	cellular_component	lysosome
A	0006508	biological_process	proteolysis
A	0006915	biological_process	apoptotic process
A	0008233	molecular_function	peptidase activity
A	0008234	molecular_function	cysteine-type peptidase activity
A	0008239	molecular_function	dipeptidyl-peptidase activity
A	0016505	molecular_function	peptidase activator activity involved in apoptotic process
A	0016787	molecular_function	hydrolase activity
A	0019902	molecular_function	phosphatase binding
A	0031404	molecular_function	chloride ion binding
A	0031642	biological_process	negative regulation of myelination
A	0042802	molecular_function	identical protein binding
A	0051087	molecular_function	protein-folding chaperone binding
A	0051603	biological_process	proteolysis involved in protein catabolic process
A	1903052	biological_process	positive regulation of proteolysis involved in protein catabolic process
A	1903980	biological_process	positive regulation of microglial cell activation
A	2001235	biological_process	positive regulation of apoptotic signaling pathway

Functional Information from PROSITE/UniProt

site_id	PS00139
Number of Residues	12
Details	THIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QEsCGSCYSfAS

Chain	Residue	Details
A	GLN227-SER238

site_id	PS00639
Number of Residues	11
Details	THIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. TNHAVLLVGYG

Chain	Residue	Details
A	THR378-GLY388

site_id	PS00640
Number of Residues	20
Details	THIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YWIvKNSWgsqWGesGYFrI

Chain	Residue	Details
A	TYR397-ILE416

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10088","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10089","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	1
Details	Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10090","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P53634","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"11602245","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1pad

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1pad

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1pad