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:
"Neutral Protease Domain 2
".
FunFam 10: 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 8 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.
|
2 | P97629 (/IMP) Q8C129 (/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).
|
2 | Q8C129 (/IPI) Q9UIQ6 (/IPI) |
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 | P97629 (/IDA) |
Aminopeptidase activity GO:0004177
Catalysis of the hydrolysis of N-terminal amino acid residues from in a polypeptide chain.
|
1 | Q8C129 (/ISO) |
Aminopeptidase activity GO:0004177
Catalysis of the hydrolysis of N-terminal amino acid residues from in a polypeptide chain.
|
1 | Q9UIQ6 (/TAS) |
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 | Q9UIQ6 (/TAS) |
There are 15 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) |
Protein polyubiquitination GO:0000209
Addition of multiple ubiquitin groups to a protein, forming a ubiquitin chain.
|
1 | Q9UIQ6 (/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 | Q9UIQ6 (/TAS) |
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) |
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) |
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) |
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 18 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 |
---|---|---|
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) |
Perinuclear region of cytoplasm GO:0048471
Cytoplasm situated near, or occurring around, the nucleus.
|
2 | P97629 (/IDA) Q8C129 (/IDA) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
1 | P97629 (/IDA) |
Lysosomal membrane GO:0005765
The lipid bilayer surrounding the lysosome and separating its contents from the cell cytoplasm.
|
1 | Q9UIQ6 (/HDA) |
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 | Q9UIQ6 (/HDA) |
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
|
1 | Q8C129 (/IMP) |
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 | P97629 (/IDA) |