The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
Acid Proteases
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 39: Cathepsin D preproprotein

Please note: GO annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

There are 14 GO terms relating to "molecular function"

The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.
GO Term Annotations Evidence
Protein binding GO:0005515
Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).
4 P07339 (/IPI) P07339 (/IPI) P18242 (/IPI) P18242 (/IPI)
Peptidase activity GO:0008233
Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid.
4 P07339 (/IDA) P07339 (/IDA) P18242 (/IDA) P18242 (/IDA)
Endopeptidase activity GO:0004175
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain.
3 P18242 (/IDA) P18242 (/IDA) P24268 (/IDA)
Endopeptidase activity GO:0004175
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain.
2 P18242 (/ISO) P18242 (/ISO)
Aspartic-type endopeptidase activity GO:0004190
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which a water molecule bound by the side chains of aspartic residues at the active center acts as a nucleophile.
2 P18242 (/IDA) P18242 (/IDA)
Aspartic-type endopeptidase activity GO:0004190
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which a water molecule bound by the side chains of aspartic residues at the active center acts as a nucleophile.
2 P07339 (/TAS) P07339 (/TAS)
Peptidase activity GO:0008233
Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid.
2 P07339 (/IMP) P07339 (/IMP)
Peptidase activity GO:0008233
Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid.
2 P18242 (/ISO) P18242 (/ISO)
Hydrolase activity GO:0016787
Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc. Hydrolase is the systematic name for any enzyme of EC class 3.
2 P18242 (/IDA) P18242 (/IDA)
Peptide binding GO:0042277
Interacting selectively and non-covalently with peptides, any of a group of organic compounds comprising two or more amino acids linked by peptide bonds.
2 P18242 (/ISO) P18242 (/ISO)
Aspartic-type peptidase activity GO:0070001
Catalysis of the hydrolysis of peptide bonds in a polypeptide chain by a mechanism in which a water molecule bound by the side chains of aspartic residues at the active center acts as a nucleophile.
2 P18242 (/IMP) P18242 (/IMP)
Aspartic-type peptidase activity GO:0070001
Catalysis of the hydrolysis of peptide bonds in a polypeptide chain by a mechanism in which a water molecule bound by the side chains of aspartic residues at the active center acts as a nucleophile.
2 P07339 (/ISS) P07339 (/ISS)
Endopeptidase activity GO:0004175
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain.
1 P24268 (/IMP)
Peptide binding GO:0042277
Interacting selectively and non-covalently with peptides, any of a group of organic compounds comprising two or more amino acids linked by peptide bonds.
1 P24268 (/IDA)

There are 17 GO terms relating to "biological process"

The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.
GO Term Annotations Evidence
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
3 P07339 (/IDA) P07339 (/IDA) P24268 (/IDA)
Autophagosome assembly GO:0000045
The formation of a double membrane-bounded structure, the autophagosome, that occurs when a specialized membrane sac, called the isolation membrane, starts to enclose a portion of the cytoplasm.
2 P18242 (/IMP) P18242 (/IMP)
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
2 P18242 (/IC) P18242 (/IC)
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
2 P07339 (/IMP) P07339 (/IMP)
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
2 P18242 (/ISO) P18242 (/ISO)
Antigen processing and presentation of exogenous peptide antigen via MHC class II GO:0019886
The process in which an antigen-presenting cell expresses a peptide antigen of exogenous origin on its cell surface in association with an MHC class II protein complex. The peptide antigen is typically, but not always, processed from a whole protein.
2 P07339 (/TAS) P07339 (/TAS)
Collagen catabolic process GO:0030574
The proteolytic chemical reactions and pathways resulting in the breakdown of collagen in the extracellular matrix, usually carried out by proteases secreted by nearby cells.
2 P07339 (/TAS) P07339 (/TAS)
Lipoprotein catabolic process GO:0042159
The chemical reactions and pathways resulting in the breakdown of any conjugated, water-soluble protein in which the covalently attached nonprotein group consists of a lipid or lipids.
2 P07339 (/IDA) P07339 (/IDA)
Lipoprotein catabolic process GO:0042159
The chemical reactions and pathways resulting in the breakdown of any conjugated, water-soluble protein in which the covalently attached nonprotein group consists of a lipid or lipids.
2 P18242 (/ISO) P18242 (/ISO)
Positive regulation of apoptotic process GO:0043065
Any process that activates or increases the frequency, rate or extent of cell death by apoptotic process.
2 P07339 (/IDA) P07339 (/IDA)
Positive regulation of apoptotic process GO:0043065
Any process that activates or increases the frequency, rate or extent of cell death by apoptotic process.
2 P18242 (/ISO) P18242 (/ISO)
Positive regulation of cysteine-type endopeptidase activity involved in apoptotic process GO:0043280
Any process that activates or increases the activity of a cysteine-type endopeptidase involved in the apoptotic process.
2 P07339 (/IDA) P07339 (/IDA)
Positive regulation of cysteine-type endopeptidase activity involved in apoptotic process GO:0043280
Any process that activates or increases the activity of a cysteine-type endopeptidase involved in the apoptotic process.
2 P18242 (/ISO) P18242 (/ISO)
Neutrophil degranulation GO:0043312
The regulated exocytosis of secretory granules containing preformed mediators such as proteases, lipases, and inflammatory mediators by a neutrophil.
2 P07339 (/TAS) P07339 (/TAS)
Regulation of establishment of protein localization GO:0070201
Any process that modulates the frequency, rate or extent of the directed movement of a protein to a specific location.
2 P07339 (/IDA) P07339 (/IDA)
Regulation of establishment of protein localization GO:0070201
Any process that modulates the frequency, rate or extent of the directed movement of a protein to a specific location.
2 P18242 (/ISO) P18242 (/ISO)
Response to nutrient levels GO:0031667
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus reflecting the presence, absence, or concentration of nutrients.
1 P24268 (/IEP)

There are 22 GO terms relating to "cellular component"

The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.
GO Term Annotations Evidence
Lysosome GO:0005764
A small lytic vacuole that has cell cycle-independent morphology and is found in most animal cells and that contains a variety of hydrolases, most of which have their maximal activities in the pH range 5-6. The contained enzymes display latency if properly isolated. About 40 different lysosomal hydrolases are known and lysosomes have a great variety of morphologies and functions.
5 P07339 (/IDA) P07339 (/IDA) P18242 (/IDA) P18242 (/IDA) P24268 (/IDA)
Lysosome GO:0005764
A small lytic vacuole that has cell cycle-independent morphology and is found in most animal cells and that contains a variety of hydrolases, most of which have their maximal activities in the pH range 5-6. The contained enzymes display latency if properly isolated. About 40 different lysosomal hydrolases are known and lysosomes have a great variety of morphologies and functions.
4 P80209 (/ISS) Q4LAL9 (/ISS) Q4LAL9 (/ISS) Q9MZS8 (/ISS)
Collagen-containing extracellular matrix GO:0062023
An extracellular matrix consisting mainly of proteins (especially collagen) and glycosaminoglycans (mostly as proteoglycans) that provides not only essential physical scaffolding for the cellular constituents but can also initiate crucial biochemical and biomechanical cues required for tissue morphogenesis, differentiation and homeostasis. The components are secreted by cells in the vicinity and form a sheet underlying or overlying cells such as endothelial and epithelial cells.
4 P07339 (/HDA) P07339 (/HDA) P18242 (/HDA) P18242 (/HDA)
Extracellular region GO:0005576
The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.
2 P07339 (/HDA) P07339 (/HDA)
Extracellular region GO:0005576
The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.
2 P07339 (/NAS) P07339 (/NAS)
Extracellular region GO:0005576
The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.
2 P07339 (/TAS) P07339 (/TAS)
Extracellular space GO:0005615
That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid.
2 P07339 (/HDA) P07339 (/HDA)
Extracellular space GO:0005615
That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid.
2 P18242 (/IDA) P18242 (/IDA)
Extracellular space GO:0005615
That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid.
2 P07339 (/ISS) P07339 (/ISS)
Mitochondrion GO:0005739
A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
2 P18242 (/HDA) P18242 (/HDA)
Lysosome GO:0005764
A small lytic vacuole that has cell cycle-independent morphology and is found in most animal cells and that contains a variety of hydrolases, most of which have their maximal activities in the pH range 5-6. The contained enzymes display latency if properly isolated. About 40 different lysosomal hydrolases are known and lysosomes have a great variety of morphologies and functions.
2 P18242 (/ISO) P18242 (/ISO)
Lysosomal membrane GO:0005765
The lipid bilayer surrounding the lysosome and separating its contents from the cell cytoplasm.
2 P07339 (/IDA) P07339 (/IDA)
Lysosomal membrane GO:0005765
The lipid bilayer surrounding the lysosome and separating its contents from the cell cytoplasm.
2 P18242 (/ISO) P18242 (/ISO)
Endosome membrane GO:0010008
The lipid bilayer surrounding an endosome.
2 P07339 (/IDA) P07339 (/IDA)
Endosome membrane GO:0010008
The lipid bilayer surrounding an endosome.
2 P18242 (/ISO) P18242 (/ISO)
Specific granule lumen GO:0035580
The volume enclosed by the membrane of a specific granule, a granule with a membranous, tubular internal structure, found primarily in mature neutrophil cells. Most are released into the extracellular fluid. Specific granules contain lactoferrin, lysozyme, vitamin B12 binding protein and elastase.
2 P07339 (/TAS) P07339 (/TAS)
Lysosomal lumen GO:0043202
The volume enclosed within the lysosomal membrane.
2 P07339 (/TAS) P07339 (/TAS)
Membrane raft GO:0045121
Any of the small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes. Small rafts can sometimes be stabilized to form larger platforms through protein-protein and protein-lipid interactions.
2 P07339 (/IDA) P07339 (/IDA)
Membrane raft GO:0045121
Any of the small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes. Small rafts can sometimes be stabilized to form larger platforms through protein-protein and protein-lipid interactions.
2 P18242 (/ISO) P18242 (/ISO)
Extracellular exosome GO:0070062
A vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm.
2 P07339 (/HDA) P07339 (/HDA)
Tertiary granule lumen GO:1904724
Any membrane-enclosed lumen that is part of a tertiary granule.
2 P07339 (/TAS) P07339 (/TAS)
Ficolin-1-rich granule lumen GO:1904813
Any membrane-enclosed lumen that is part of a ficolin-1-rich granule.
2 P07339 (/TAS) P07339 (/TAS)
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