CATH Superfamily 2.60.40.1910
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: waiting to be named.
FunFam 1: Leucyl-cystinyl aminopeptidase
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 23 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 |
---|---|---|
Aminopeptidase activity GO:0004177
Catalysis of the hydrolysis of N-terminal amino acid residues from in a polypeptide chain.
|
4 | P97629 (/IDA) Q6P179 (/IDA) Q9EQH2 (/IDA) Q9NZ08 (/IDA) |
Aminopeptidase activity GO:0004177
Catalysis of the hydrolysis of N-terminal amino acid residues from in a polypeptide chain.
|
3 | P97629 (/IMP) Q8C129 (/IMP) Q9JJ22 (/IMP) |
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).
|
3 | Q8C129 (/IPI) Q9NZ08 (/IPI) Q9UIQ6 (/IPI) |
Aminopeptidase activity GO:0004177
Catalysis of the hydrolysis of N-terminal amino acid residues from in a polypeptide chain.
|
2 | Q8C129 (/ISO) Q9EQH2 (/ISO) |
Aminopeptidase activity GO:0004177
Catalysis of the hydrolysis of N-terminal amino acid residues from in a polypeptide chain.
|
2 | Q9EQH2 (/ISS) Q9JJ22 (/ISS) |
Interleukin-6 receptor binding GO:0005138
Interacting selectively and non-covalently with the interleukin-6 receptor.
|
2 | Q9EQH2 (/ISS) Q9JJ22 (/ISS) |
Metalloexopeptidase activity GO:0008235
Catalysis of the hydrolysis of a peptide bond not more than three residues from the N- or C-terminus of a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.
|
2 | Q9EQH2 (/ISS) Q9JJ22 (/ISS) |
Zinc ion binding GO:0008270
Interacting selectively and non-covalently with zinc (Zn) ions.
|
2 | Q6P179 (/TAS) Q9UIQ6 (/TAS) |
Aminopeptidase activity GO:0004177
Catalysis of the hydrolysis of N-terminal amino acid residues from in a polypeptide chain.
|
1 | Q9UIQ6 (/EXP) |
Aminopeptidase activity GO:0004177
Catalysis of the hydrolysis of N-terminal amino acid residues from in a polypeptide chain.
|
1 | Q9UIQ6 (/TAS) |
Interleukin-6 receptor binding GO:0005138
Interacting selectively and non-covalently with the interleukin-6 receptor.
|
1 | Q9NZ08 (/IPI) |
Interleukin-6 receptor binding GO:0005138
Interacting selectively and non-covalently with the interleukin-6 receptor.
|
1 | Q9EQH2 (/ISO) |
Interleukin-1, type II receptor binding GO:0005151
Interacting selectively and non-covalently with a Type II interleukin-1 receptor.
|
1 | Q9NZ08 (/TAS) |
Tumor necrosis factor receptor binding GO:0005164
Interacting selectively and non-covalently with the tumor necrosis factor receptor.
|
1 | Q9JJ22 (/IPI) |
Tumor necrosis factor receptor binding GO:0005164
Interacting selectively and non-covalently with the tumor necrosis factor receptor.
|
1 | Q9EQH2 (/ISO) |
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.
|
1 | Q9EQH2 (/IMP) |
Metalloexopeptidase activity GO:0008235
Catalysis of the hydrolysis of a peptide bond not more than three residues from the N- or C-terminus of a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.
|
1 | Q9NZ08 (/IDA) |
Metalloexopeptidase activity GO:0008235
Catalysis of the hydrolysis of a peptide bond not more than three residues from the N- or C-terminus of a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.
|
1 | Q9EQH2 (/ISO) |
Metallopeptidase activity GO:0008237
Catalysis of the hydrolysis of peptide bonds by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.
|
1 | Q6P179 (/IDA) |
Metallopeptidase activity GO:0008237
Catalysis of the hydrolysis of peptide bonds by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.
|
1 | Q9UIQ6 (/TAS) |
Zinc ion binding GO:0008270
Interacting selectively and non-covalently with zinc (Zn) ions.
|
1 | Q9JJ22 (/IMP) |
Zinc ion binding GO:0008270
Interacting selectively and non-covalently with zinc (Zn) ions.
|
1 | Q9EQH2 (/ISO) |
Zinc ion binding GO:0008270
Interacting selectively and non-covalently with zinc (Zn) ions.
|
1 | Q9NZ08 (/NAS) |
There are 32 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 |
---|---|---|
Negative regulation of cold-induced thermogenesis GO:0120163
Any process that stops, prevents, or reduces the rate of cold-induced thermogenesis.
|
4 | A0A0G2JYN3 (/ISS) A0A0H2UHK5 (/ISS) P97629 (/ISS) Q9UIQ6 (/ISS) |
Antigen processing and presentation of peptide antigen via MHC class I GO:0002474
The process in which an antigen-presenting cell expresses a peptide antigen on its cell surface in association with an MHC class I protein complex. Class I here refers to classical class I molecules.
|
2 | Q6P179 (/TAS) Q9NZ08 (/TAS) |
Membrane protein ectodomain proteolysis GO:0006509
The proteolytic cleavage of transmembrane proteins and release of their ectodomain (extracellular domain).
|
2 | Q9EQH2 (/ISS) Q9JJ22 (/ISS) |
Regulation of blood pressure GO:0008217
Any process that modulates the force with which blood travels through the circulatory system. The process is controlled by a balance of processes that increase pressure and decrease pressure.
|
2 | Q6P179 (/TAS) Q9NZ08 (/TAS) |
Antigen processing and presentation of endogenous peptide antigen via MHC class I GO:0019885
The process in which an antigen-presenting cell expresses a peptide antigen of endogenous origin on its cell surface in association with an MHC class I protein complex. The peptide antigen is typically, but not always, processed from a whole protein. Class I here refers to classical class I molecules.
|
2 | Q6P179 (/TAS) Q9NZ08 (/TAS) |
Protein polyubiquitination GO:0000209
Addition of multiple ubiquitin groups to a protein, forming a ubiquitin chain.
|
1 | Q9UIQ6 (/TAS) |
Angiogenesis GO:0001525
Blood vessel formation when new vessels emerge from the proliferation of pre-existing blood vessels.
|
1 | Q9NZ08 (/TAS) |
Antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent GO:0002480
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 I protein complex following intracellular transport via a pathway not requiring TAP (transporter associated with antigen processing). The peptide is typically a fragment of a larger exogenous protein which has been degraded within the cell. Class I here refers to classical class I molecules.
|
1 | Q9UIQ6 (/TAS) |
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
1 | Q9EQH2 (/IDA) |
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
1 | Q9JJ22 (/IMP) |
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
1 | Q9EQH2 (/ISO) |
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
1 | Q9UIQ6 (/TAS) |
Membrane protein ectodomain proteolysis GO:0006509
The proteolytic cleavage of transmembrane proteins and release of their ectodomain (extracellular domain).
|
1 | Q9NZ08 (/IDA) |
Membrane protein ectodomain proteolysis GO:0006509
The proteolytic cleavage of transmembrane proteins and release of their ectodomain (extracellular domain).
|
1 | Q9EQH2 (/ISO) |
Cell-cell signaling GO:0007267
Any process that mediates the transfer of information from one cell to another. This process includes signal transduction in the receiving cell and, where applicable, release of a ligand and any processes that actively facilitate its transport and presentation to the receiving cell. Examples include signaling via soluble ligands, via cell adhesion molecules and via gap junctions.
|
1 | Q9UIQ6 (/TAS) |
Female pregnancy GO:0007565
The set of physiological processes that allow an embryo or foetus to develop within the body of a female animal. It covers the time from fertilization of a female ovum by a male spermatozoon until birth.
|
1 | Q9UIQ6 (/TAS) |
Regulation of blood pressure GO:0008217
Any process that modulates the force with which blood travels through the circulatory system. The process is controlled by a balance of processes that increase pressure and decrease pressure.
|
1 | Q9NZ08 (/NAS) |
Response to bacterium GO:0009617
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 from a bacterium.
|
1 | Q9NZ08 (/NAS) |
Response to hormone GO:0009725
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 hormone stimulus.
|
1 | P97629 (/IDA) |
Neuropeptide catabolic process GO:0010813
The chemical reactions and pathways resulting in the breakdown of neuropeptides. Neuropeptides are signaling peptides that travel across a synaptic junction.
|
1 | P97629 (/IMP) |
Antigen processing and presentation GO:0019882
The process in which an antigen-presenting cell expresses antigen (peptide or lipid) on its cell surface in association with an MHC protein complex.
|
1 | Q9JJ22 (/TAS) |
Antigen processing and presentation of endogenous peptide antigen via MHC class I GO:0019885
The process in which an antigen-presenting cell expresses a peptide antigen of endogenous origin on its cell surface in association with an MHC class I protein complex. The peptide antigen is typically, but not always, processed from a whole protein. Class I here refers to classical class I molecules.
|
1 | Q9NZ08 (/NAS) |
Protein catabolic process GO:0030163
The chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds.
|
1 | Q8C129 (/IMP) |
Peptide catabolic process GO:0043171
The chemical reactions and pathways resulting in the breakdown of peptides, compounds of 2 or more (but usually less than 100) amino acids where the alpha carboxyl group of one is bound to the alpha amino group of another.
|
1 | P97629 (/IDA) |
Peptide catabolic process GO:0043171
The chemical reactions and pathways resulting in the breakdown of peptides, compounds of 2 or more (but usually less than 100) amino acids where the alpha carboxyl group of one is bound to the alpha amino group of another.
|
1 | P97629 (/IMP) |
Regulation of innate immune response GO:0045088
Any process that modulates the frequency, rate or extent of the innate immune response, the organism's first line of defense against infection.
|
1 | Q9NZ08 (/NAS) |
Fat cell differentiation GO:0045444
The process in which a relatively unspecialized cell acquires specialized features of an adipocyte, an animal connective tissue cell specialized for the synthesis and storage of fat.
|
1 | Q9NZ08 (/NAS) |
Positive regulation of angiogenesis GO:0045766
Any process that activates or increases angiogenesis.
|
1 | Q9EQH2 (/IMP) |
Positive regulation of blood pressure GO:0045777
Any process in which the force of blood traveling through the circulatory system is increased.
|
1 | P97629 (/IMP) |
Regulation of long-term neuronal synaptic plasticity GO:0048169
A process that modulates long-term neuronal synaptic plasticity, the ability of neuronal synapses to change long-term as circumstances require. Long-term neuronal synaptic plasticity generally involves increase or decrease in actual synapse numbers.
|
1 | P97629 (/IMP) |
SMAD protein signal transduction GO:0060395
The cascade of processes by which a signal interacts with a receptor, causing a change in the activity of a SMAD protein, and ultimately effecting a change in the functioning of the cell.
|
1 | Q8C129 (/IDA) |
Negative regulation of cold-induced thermogenesis GO:0120163
Any process that stops, prevents, or reduces the rate of cold-induced thermogenesis.
|
1 | Q8C129 (/IMP) |
There are 30 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 |
---|---|---|
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 | Q9EQH2 (/ISS) Q9JJ22 (/ISS) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
2 | P97629 (/IDA) Q9EQH2 (/IDA) |
Endoplasmic reticulum lumen GO:0005788
The volume enclosed by the membranes of the endoplasmic reticulum.
|
2 | Q6P179 (/IDA) Q9JJ22 (/IDA) |
Endoplasmic reticulum lumen GO:0005788
The volume enclosed by the membranes of the endoplasmic reticulum.
|
2 | Q6P179 (/TAS) Q9NZ08 (/TAS) |
Plasma membrane GO:0005886
The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
|
2 | P97629 (/IDA) Q8C129 (/IDA) |
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
|
2 | Q9NZ08 (/HDA) Q9UIQ6 (/HDA) |
Intracellular membrane-bounded organelle GO:0043231
Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane.
|
2 | P97629 (/IDA) Q9JJ22 (/IDA) |
Perinuclear region of cytoplasm GO:0048471
Cytoplasm situated near, or occurring around, the nucleus.
|
2 | P97629 (/IDA) Q8C129 (/IDA) |
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.
|
1 | Q9NZ08 (/IDA) |
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.
|
1 | Q9EQH2 (/ISO) |
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.
|
1 | Q9NZ08 (/HDA) |
Lysosomal membrane GO:0005765
The lipid bilayer surrounding the lysosome and separating its contents from the cell cytoplasm.
|
1 | Q9UIQ6 (/HDA) |
Endoplasmic reticulum GO:0005783
The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
|
1 | Q9NZ08 (/NAS) |
Endoplasmic reticulum lumen GO:0005788
The volume enclosed by the membranes of the endoplasmic reticulum.
|
1 | Q9EQH2 (/ISO) |
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
|
1 | Q9NZ08 (/NAS) |
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
|
1 | Q9UIQ6 (/TAS) |
Integral component of plasma membrane GO:0005887
The component of the plasma membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
|
1 | Q9UIQ6 (/IDA) |
Integral component of plasma membrane GO:0005887
The component of the plasma membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
|
1 | Q8C129 (/ISO) |
Cell surface GO:0009986
The external part of the cell wall and/or plasma membrane.
|
1 | P97629 (/IDA) |
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
|
1 | Q8C129 (/IMP) |
Integral component of membrane GO:0016021
The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
|
1 | Q9NZ08 (/NAS) |
Cytoplasmic vesicle membrane GO:0030659
The lipid bilayer surrounding a cytoplasmic vesicle.
|
1 | Q8C129 (/IDA) |
Cytoplasmic vesicle membrane GO:0030659
The lipid bilayer surrounding a cytoplasmic vesicle.
|
1 | Q8C129 (/TAS) |
Early endosome lumen GO:0031905
The volume enclosed by the membrane of an early endosome.
|
1 | Q9UIQ6 (/TAS) |
Vesicle GO:0031982
Any small, fluid-filled, spherical organelle enclosed by membrane.
|
1 | P97629 (/IDA) |
Insulin-responsive compartment GO:0032593
A small membrane-bounded vesicle that releases its contents by exocytosis in response to insulin stimulation; the contents are enriched in GLUT4, IRAP and VAMP2.
|
1 | P97629 (/IDA) |
Neuronal cell body GO:0043025
The portion of a neuron that includes the nucleus, but excludes cell projections such as axons and dendrites.
|
1 | P97629 (/IDA) |
Intracellular organelle GO:0043229
Organized structure of distinctive morphology and function, occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, vesicles, ribosomes and the cytoskeleton. Excludes the plasma membrane.
|
1 | P97629 (/IDA) |
Intracellular membrane-bounded organelle GO:0043231
Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane.
|
1 | Q9EQH2 (/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.
|
1 | Q9NZ08 (/HDA) |