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.

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 1: ATP synthase subunit alpha

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
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).
203 P0ABB0 (/IPI) P0ABB0 (/IPI) P0ABB0 (/IPI) P0ABB0 (/IPI) P0ABB0 (/IPI) P0ABB0 (/IPI) P0ABB0 (/IPI) P0ABB0 (/IPI) P0ABB0 (/IPI) P0ABB0 (/IPI)
(193 more)
Proton-transporting ATP synthase activity, rotational mechanism GO:0046933
Enables the transfer of protons from one side of a membrane to the other according to the reaction: ADP + H2O + phosphate + H+(in) = ATP + H+(out), by a rotational mechanism.
9 P25705 (/ISS) P25705 (/ISS) P25705 (/ISS) P25705 (/ISS) P35381 (/ISS) Q9KNH3 (/ISS) Q9KNH3 (/ISS) Q9KNH3 (/ISS) Q9KNH3 (/ISS)
Chaperone binding GO:0051087
Interacting selectively and non-covalently with a chaperone protein, a class of proteins that bind to nascent or unfolded polypeptides and ensure correct folding or transport.
6 P05494 (/IPI) P05494 (/IPI) P05494 (/IPI) P05494 (/IPI) P05494 (/IPI) P05494 (/IPI)
Proton-transporting ATP synthase activity, rotational mechanism GO:0046933
Enables the transfer of protons from one side of a membrane to the other according to the reaction: ADP + H2O + phosphate + H+(in) = ATP + H+(out), by a rotational mechanism.
5 P25705 (/IMP) P25705 (/IMP) P25705 (/IMP) P25705 (/IMP) Q03265 (/IMP)
RNA binding GO:0003723
Interacting selectively and non-covalently with an RNA molecule or a portion thereof.
4 P25705 (/HDA) P25705 (/HDA) P25705 (/HDA) P25705 (/HDA)
ATP binding GO:0005524
Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
4 P25705 (/ISS) P25705 (/ISS) P25705 (/ISS) P25705 (/ISS)
Zinc ion binding GO:0008270
Interacting selectively and non-covalently with zinc (Zn) ions.
4 F4IMB5 (/IDA) P56757 (/IDA) P56757 (/IDA) P56757 (/IDA)
Transmembrane transporter activity GO:0022857
Enables the transfer of a substance, usually a specific substance or a group of related substances, from one side of a membrane to the other.
4 P25705 (/IC) P25705 (/IC) P25705 (/IC) P25705 (/IC)
MHC class I protein binding GO:0042288
Interacting selectively and non-covalently with major histocompatibility complex class I molecules; a set of molecules displayed on cell surfaces that are responsible for lymphocyte recognition and antigen presentation.
4 P25705 (/IDA) P25705 (/IDA) P25705 (/IDA) P25705 (/IDA)
Angiostatin binding GO:0043532
Interacting selectively and non-covalently with angiostatin, a proteolytic product of plasminogen or plasmin containing at least one intact kringle domain, and which is an inhibitor of angiogenesis.
4 P25705 (/IPI) P25705 (/IPI) P25705 (/IPI) P25705 (/IPI)
Protease binding GO:0002020
Interacting selectively and non-covalently with any protease or peptidase.
1 P15999 (/IPI)
Protease binding GO:0002020
Interacting selectively and non-covalently with any protease or peptidase.
1 Q03265 (/ISO)
ATP binding GO:0005524
Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
1 P15999 (/IDA)
ATP binding GO:0005524
Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
1 Q03265 (/IMP)
ATP binding GO:0005524
Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
1 P24487 (/ISM)
ATP binding GO:0005524
Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
1 Q03265 (/ISO)
Poly(U) RNA binding GO:0008266
Interacting selectively and non-covalently with a sequence of uracil residues in an RNA molecule.
1 F4IMB5 (/IDA)
MHC class I protein binding GO:0042288
Interacting selectively and non-covalently with major histocompatibility complex class I molecules; a set of molecules displayed on cell surfaces that are responsible for lymphocyte recognition and antigen presentation.
1 Q03265 (/ISO)
ADP binding GO:0043531
Interacting selectively and non-covalently with ADP, adenosine 5'-diphosphate.
1 P15999 (/IDA)
ADP binding GO:0043531
Interacting selectively and non-covalently with ADP, adenosine 5'-diphosphate.
1 Q03265 (/ISO)
Angiostatin binding GO:0043532
Interacting selectively and non-covalently with angiostatin, a proteolytic product of plasminogen or plasmin containing at least one intact kringle domain, and which is an inhibitor of angiogenesis.
1 Q03265 (/ISO)
Proton-transporting ATP synthase activity, rotational mechanism GO:0046933
Enables the transfer of protons from one side of a membrane to the other according to the reaction: ADP + H2O + phosphate + H+(in) = ATP + H+(out), by a rotational mechanism.
1 Q03265 (/ISO)
Enterobactin binding GO:1903981
Interacting selectively and non-covalently with enterobactin.
1 Q9XXK1 (/IDA)

There are 34 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
ATP synthesis coupled proton transport GO:0015986
The transport of protons across a membrane to generate an electrochemical gradient (proton-motive force) that powers ATP synthesis.
201 P07251 (/IMP) P07251 (/IMP) P07251 (/IMP) P07251 (/IMP) P07251 (/IMP) P07251 (/IMP) P07251 (/IMP) P07251 (/IMP) P0ABB0 (/IMP) P0ABB0 (/IMP)
(191 more)
ATP synthesis coupled proton transport GO:0015986
The transport of protons across a membrane to generate an electrochemical gradient (proton-motive force) that powers ATP synthesis.
8 P07251 (/IDA) P07251 (/IDA) P07251 (/IDA) P07251 (/IDA) P07251 (/IDA) P07251 (/IDA) P07251 (/IDA) P07251 (/IDA)
ATP biosynthetic process GO:0006754
The chemical reactions and pathways resulting in the formation of ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
7 A0A1D8PDC4 (/NAS) P25705 (/NAS) P25705 (/NAS) P25705 (/NAS) P25705 (/NAS) Q06735 (/NAS) Q06735 (/NAS)
ATP synthesis coupled proton transport GO:0015986
The transport of protons across a membrane to generate an electrochemical gradient (proton-motive force) that powers ATP synthesis.
5 P35381 (/ISS) Q9KNH3 (/ISS) Q9KNH3 (/ISS) Q9KNH3 (/ISS) Q9KNH3 (/ISS)
Mitochondrial ATP synthesis coupled proton transport GO:0042776
The transport of protons across a mitochondrial membrane to generate an electrochemical gradient (proton-motive force) that powers ATP synthesis.
5 P24487 (/TAS) P25705 (/TAS) P25705 (/TAS) P25705 (/TAS) P25705 (/TAS)
Negative regulation of endothelial cell proliferation GO:0001937
Any process that stops, prevents, or reduces the rate or extent of endothelial cell proliferation.
4 P25705 (/IMP) P25705 (/IMP) P25705 (/IMP) P25705 (/IMP)
Lipid metabolic process GO:0006629
The chemical reactions and pathways involving lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent. Includes fatty acids; neutral fats, other fatty-acid esters, and soaps; long-chain (fatty) alcohols and waxes; sphingoids and other long-chain bases; glycolipids, phospholipids and sphingolipids; and carotenes, polyprenols, sterols, terpenes and other isoprenoids.
4 P25705 (/ISS) P25705 (/ISS) P25705 (/ISS) P25705 (/ISS)
ATP biosynthetic process GO:0006754
The chemical reactions and pathways resulting in the formation of ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
4 P25705 (/IC) P25705 (/IC) P25705 (/IC) P25705 (/IC)
ATP biosynthetic process GO:0006754
The chemical reactions and pathways resulting in the formation of ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
4 P25705 (/IMP) P25705 (/IMP) P25705 (/IMP) P25705 (/IMP)
ATP biosynthetic process GO:0006754
The chemical reactions and pathways resulting in the formation of ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
4 P25705 (/TAS) P25705 (/TAS) P25705 (/TAS) P25705 (/TAS)
Cristae formation GO:0042407
The assembly of cristae, the inwards folds of the inner mitochondrial membrane.
4 P25705 (/TAS) P25705 (/TAS) P25705 (/TAS) P25705 (/TAS)
Mitochondrial ATP synthesis coupled proton transport GO:0042776
The transport of protons across a mitochondrial membrane to generate an electrochemical gradient (proton-motive force) that powers ATP synthesis.
4 P25705 (/IC) P25705 (/IC) P25705 (/IC) P25705 (/IC)
Positive regulation of blood vessel endothelial cell migration GO:0043536
Any process that activates or increases the frequency, rate or extent of the migration of the endothelial cells of blood vessels.
4 P25705 (/IGI) P25705 (/IGI) P25705 (/IGI) P25705 (/IGI)
Response to cold GO:0009409
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 cold stimulus, a temperature stimulus below the optimal temperature for that organism.
3 P56757 (/IEP) P56757 (/IEP) P56757 (/IEP)
Defense response to bacterium GO:0042742
Reactions triggered in response to the presence of a bacterium that act to protect the cell or organism.
3 P56757 (/IEP) P56757 (/IEP) P56757 (/IEP)
ATP biosynthetic process GO:0006754
The chemical reactions and pathways resulting in the formation of ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
2 P05036 (/IDA) P05036 (/IDA)
Negative regulation of endothelial cell proliferation GO:0001937
Any process that stops, prevents, or reduces the rate or extent of endothelial cell proliferation.
1 Q03265 (/ISO)
Generation of precursor metabolites and energy GO:0006091
The chemical reactions and pathways resulting in the formation of precursor metabolites, substances from which energy is derived, and any process involved in the liberation of energy from these substances.
1 C8VMQ7 (/RCA)
Lipid metabolic process GO:0006629
The chemical reactions and pathways involving lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent. Includes fatty acids; neutral fats, other fatty-acid esters, and soaps; long-chain (fatty) alcohols and waxes; sphingoids and other long-chain bases; glycolipids, phospholipids and sphingolipids; and carotenes, polyprenols, sterols, terpenes and other isoprenoids.
1 Q03265 (/IMP)
ATP biosynthetic process GO:0006754
The chemical reactions and pathways resulting in the formation of ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
1 Q03265 (/ISO)
Apoptotic process GO:0006915
A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died.
1 P15999 (/IEP)
Aging GO:0007568
A developmental process that is a deterioration and loss of function over time. Aging includes loss of functions such as resistance to disease, homeostasis, and fertility, as well as wear and tear. Aging includes cellular senescence, but is more inclusive. May precede death and may succeed developmental maturation (GO:0021700).
1 P15999 (/IEP)
Response to muscle activity GO:0014850
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 muscle activity stimulus.
1 P15999 (/IEP)
Lipid storage GO:0019915
The accumulation and maintenance in cells or tissues of lipids, compounds soluble in organic solvents but insoluble or sparingly soluble in aqueous solvents. Lipid reserves can be accumulated during early developmental stages for mobilization and utilization at later stages of development.
1 P35381 (/IMP)
Electron transport chain GO:0022900
A process in which a series of electron carriers operate together to transfer electrons from donors to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient.
1 P35381 (/IDA)
Iron import into cell GO:0033212
The directed movement of iron ions from outside of a cell into the cytoplasmic compartment. This may occur via transport across the plasma membrane or via endocytosis.
1 Q9XXK1 (/IMP)
Positive regulation of blood vessel endothelial cell migration GO:0043536
Any process that activates or increases the frequency, rate or extent of the migration of the endothelial cells of blood vessels.
1 Q03265 (/ISO)
Response to ethanol GO:0045471
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 an ethanol stimulus.
1 P15999 (/IEP)
ATP metabolic process GO:0046034
The chemical reactions and pathways involving ATP, adenosine triphosphate, a universally important coenzyme and enzyme regulator.
1 P15999 (/IDA)
ATP metabolic process GO:0046034
The chemical reactions and pathways involving ATP, adenosine triphosphate, a universally important coenzyme and enzyme regulator.
1 Q03265 (/ISO)
Iron ion homeostasis GO:0055072
Any process involved in the maintenance of an internal steady state of iron ions within an organism or cell.
1 Q9XXK1 (/IDA)
Cellular response to dexamethasone stimulus GO:0071549
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a dexamethasone stimulus.
1 P15999 (/IEP)
Cellular response to nitric oxide GO:0071732
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a nitric oxide stimulus.
1 P15999 (/IEP)
Regulation of choline O-acetyltransferase activity GO:1902769
Any process that modulates the frequency, rate or extent of choline O-acetyltransferase activity.
1 P35381 (/IDA)

There are 58 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
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
197 P0ABB0 (/HDA) P0ABB0 (/HDA) P0ABB0 (/HDA) P0ABB0 (/HDA) P0ABB0 (/HDA) P0ABB0 (/HDA) P0ABB0 (/HDA) P0ABB0 (/HDA) P0ABB0 (/HDA) P0ABB0 (/HDA)
(187 more)
Proton-transporting ATP synthase complex, catalytic core F(1) GO:0045261
The sector of a hydrogen-transporting ATP synthase complex in which the catalytic activity resides; it comprises the catalytic core and central stalk, and is peripherally associated with a membrane, such as the plasma membrane or the mitochondrial inner membrane, when the entire ATP synthase is assembled.
193 P0ABB0 (/IMP) P0ABB0 (/IMP) P0ABB0 (/IMP) P0ABB0 (/IMP) P0ABB0 (/IMP) P0ABB0 (/IMP) P0ABB0 (/IMP) P0ABB0 (/IMP) P0ABB0 (/IMP) P0ABB0 (/IMP)
(183 more)
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.
15 P07251 (/HDA) P07251 (/HDA) P07251 (/HDA) P07251 (/HDA) P07251 (/HDA) P07251 (/HDA) P07251 (/HDA) P07251 (/HDA) P25705 (/HDA) P25705 (/HDA)
(5 more)
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.
15 F4IMB5 (/IDA) P07251 (/IDA) P07251 (/IDA) P07251 (/IDA) P07251 (/IDA) P07251 (/IDA) P07251 (/IDA) P07251 (/IDA) P07251 (/IDA) P15999 (/IDA)
(5 more)
Cell wall GO:0005618
The rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal, most prokaryotic cells and some protozoan parasites, maintaining their shape and protecting them from osmotic lysis. In plants it is made of cellulose and, often, lignin; in fungi it is composed largely of polysaccharides; in bacteria it is composed of peptidoglycan; in protozoan parasites such as Giardia species, it's made of carbohydrates and proteins.
12 P9WPU7 (/HDA) P9WPU7 (/HDA) P9WPU7 (/HDA) P9WPU7 (/HDA) P9WPU7 (/HDA) P9WPU7 (/HDA) P9WPU7 (/HDA) P9WPU7 (/HDA) P9WPU7 (/HDA) P9WPU7 (/HDA)
(2 more)
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.
12 P9WPU7 (/HDA) P9WPU7 (/HDA) P9WPU7 (/HDA) P9WPU7 (/HDA) P9WPU7 (/HDA) P9WPU7 (/HDA) P9WPU7 (/HDA) P9WPU7 (/HDA) P9WPU7 (/HDA) P9WPU7 (/HDA)
(2 more)
Mitochondrial proton-transporting ATP synthase, catalytic core GO:0005754
The hexamer, comprising three alpha and three beta subunits, that possesses the catalytic activity of the mitochondrial hydrogen-transporting ATP synthase.
8 P07251 (/IDA) P07251 (/IDA) P07251 (/IDA) P07251 (/IDA) P07251 (/IDA) P07251 (/IDA) P07251 (/IDA) P07251 (/IDA)
Mitochondrial proton-transporting ATP synthase, catalytic core GO:0005754
The hexamer, comprising three alpha and three beta subunits, that possesses the catalytic activity of the mitochondrial hydrogen-transporting ATP synthase.
8 P07251 (/IMP) P07251 (/IMP) P07251 (/IMP) P07251 (/IMP) P07251 (/IMP) P07251 (/IMP) P07251 (/IMP) P07251 (/IMP)
Mitochondrial intermembrane space GO:0005758
The region between the inner and outer lipid bilayers of the mitochondrial envelope.
8 P07251 (/TAS) P07251 (/TAS) P07251 (/TAS) P07251 (/TAS) P07251 (/TAS) P07251 (/TAS) P07251 (/TAS) P07251 (/TAS)
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
8 P07251 (/TAS) P07251 (/TAS) P07251 (/TAS) P07251 (/TAS) P07251 (/TAS) P07251 (/TAS) P07251 (/TAS) P07251 (/TAS)
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
8 F4IMB5 (/IDA) P25705 (/IDA) P25705 (/IDA) P25705 (/IDA) P25705 (/IDA) P56757 (/IDA) P56757 (/IDA) P56757 (/IDA)
Mitochondrial nucleoid GO:0042645
The region of a mitochondrion to which the DNA is confined.
8 P07251 (/IDA) P07251 (/IDA) P07251 (/IDA) P07251 (/IDA) P07251 (/IDA) P07251 (/IDA) P07251 (/IDA) P07251 (/IDA)
Mitochondrial proton-transporting ATP synthase complex GO:0005753
A proton-transporting ATP synthase complex found in the mitochondrial membrane.
7 A5A6H5 (/ISS) A5A6H5 (/ISS) A5A6H5 (/ISS) A5A6H5 (/ISS) Q03265 (/ISS) Q5R546 (/ISS) Q5R546 (/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.
6 P25705 (/NAS) P25705 (/NAS) P25705 (/NAS) P25705 (/NAS) Q06735 (/NAS) Q06735 (/NAS)
Mitochondrial proton-transporting ATP synthase complex GO:0005753
A proton-transporting ATP synthase complex found in the mitochondrial membrane.
6 P15999 (/IDA) P19483 (/IDA) P25705 (/IDA) P25705 (/IDA) P25705 (/IDA) P25705 (/IDA)
Mitochondrial membrane GO:0031966
Either of the lipid bilayers that surround the mitochondrion and form the mitochondrial envelope.
6 P05494 (/IDA) P05494 (/IDA) P05494 (/IDA) P05494 (/IDA) P05494 (/IDA) P05494 (/IDA)
Mitochondrial inner membrane GO:0005743
The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae.
5 P15999 (/IDA) P25705 (/IDA) P25705 (/IDA) P25705 (/IDA) P25705 (/IDA)
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.
5 A0A1D8PDC4 (/IDA) P25705 (/IDA) P25705 (/IDA) P25705 (/IDA) P25705 (/IDA)
Mitochondrial matrix GO:0005759
The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.
4 P25705 (/TAS) P25705 (/TAS) P25705 (/TAS) P25705 (/TAS)
Chloroplast GO:0009507
A chlorophyll-containing plastid with thylakoids organized into grana and frets, or stroma thylakoids, and embedded in a stroma.
4 F4IMB5 (/IDA) P56757 (/IDA) P56757 (/IDA) P56757 (/IDA)
Proton-transporting ATP synthase complex GO:0045259
A proton-transporting two-sector ATPase complex that catalyzes the phosphorylation of ADP to ATP during oxidative phosphorylation. The complex comprises a membrane sector (F0) that carries out proton transport and a cytoplasmic compartment sector (F1) that catalyzes ATP synthesis by a rotational mechanism; the extramembrane sector (containing 3 a and 3 b subunits) is connected via the d-subunit to the membrane sector by several smaller subunits. Within this complex, the g and e subunits and the 9-12 c subunits rotate by consecutive 120 degree angles and perform parts of ATP synthesis. This movement is driven by the hydrogen ion electrochemical potential gradient.
4 P25705 (/IDA) P25705 (/IDA) P25705 (/IDA) P25705 (/IDA)
Plasma membrane proton-transporting ATP synthase complex, catalytic core F(1) GO:0045262
The catalytic sector of the plasma membrane hydrogen-transporting ATP synthase; it comprises the catalytic core and central stalk, and is peripherally associated with the plasma membrane when the entire ATP synthase is assembled. Examples of this component are found in Bacterial species.
4 Q9KNH3 (/ISS) Q9KNH3 (/ISS) Q9KNH3 (/ISS) Q9KNH3 (/ISS)
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.
4 P25705 (/HDA) P25705 (/HDA) P25705 (/HDA) P25705 (/HDA)
Chloroplast thylakoid GO:0009534
Sac-like membranous structures (cisternae) in a chloroplast combined into stacks (grana) and present singly in the stroma (stroma thylakoids or frets) as interconnections between grana. An example of this component is found in Arabidopsis thaliana.
3 P56757 (/IDA) P56757 (/IDA) P56757 (/IDA)
Chloroplast thylakoid membrane GO:0009535
The pigmented membrane of a chloroplast thylakoid. An example of this component is found in Arabidopsis thaliana.
3 P56757 (/IDA) P56757 (/IDA) P56757 (/IDA)
Thylakoid GO:0009579
A membranous cellular structure that bears the photosynthetic pigments in plants, algae, and cyanobacteria. In cyanobacteria thylakoids are of various shapes and are attached to, or continuous with, the plasma membrane. In eukaryotes they are flattened, membrane-bounded disk-like structures located in the chloroplasts; in the chloroplasts of higher plants the thylakoids form dense stacks called grana. Isolated thylakoid preparations can carry out photosynthetic electron transport and the associated phosphorylation.
3 P56757 (/IDA) P56757 (/IDA) P56757 (/IDA)
Cell surface GO:0009986
The external part of the cell wall and/or plasma membrane.
3 A0A1D8PDC4 (/IDA) G8B7R3 (/IDA) P15999 (/IDA)
Plastoglobule GO:0010287
A lipoprotein particle present in chloroplasts. They are rich in non-polar lipids (triglycerides, esters) as well as in prenylquinones, plastoquinone and tocopherols. Plastoglobules are often associated with thylakoid membranes, suggesting an exchange of lipids with thylakoids.
3 P56757 (/IDA) P56757 (/IDA) P56757 (/IDA)
Stromule GO:0010319
Thin filamentous structure extending from the surface of all plastid types examined so far, including chloroplast, proplastid, etioplast, leucoplast, amyloplast, and chromoplast. In general, stromules are more abundant in tissues containing non-green plastids, and in cells containing smaller plastids. The primary function of stromules is still unresolved, although the presence of stromules markedly increases the plastid surface area, potentially increasing transport to and from the cytosol. Other functions of stromules, such as transfer of macromolecules between plastids and starch granule formation in cereal endosperm, may be restricted to particular tissues and cell types.
3 P56757 (/IDA) P56757 (/IDA) P56757 (/IDA)
Thylakoid lumen GO:0031977
The volume enclosed by a thylakoid membrane.
3 P56757 (/IDA) P56757 (/IDA) P56757 (/IDA)
Proton-transporting ATP synthase complex, catalytic core F(1) GO:0045261
The sector of a hydrogen-transporting ATP synthase complex in which the catalytic activity resides; it comprises the catalytic core and central stalk, and is peripherally associated with a membrane, such as the plasma membrane or the mitochondrial inner membrane, when the entire ATP synthase is assembled.
3 P05036 (/IDA) P05036 (/IDA) P15999 (/IDA)
Mitochondrial proton-transporting ATP synthase complex, catalytic core F(1) GO:0000275
The catalytic sector of the mitochondrial hydrogen-transporting ATP synthase; it comprises the catalytic core and central stalk, and is peripherally associated with the mitochondrial inner membrane when the entire ATP synthase is assembled.
2 Q06735 (/NAS) Q06735 (/NAS)
Plasma membrane proton-transporting ATP synthase complex GO:0045260
A proton-transporting ATP synthase complex found in the plasma membrane. Examples of this component are found in Bacterial species.
2 P27179 (/IDA) P27179 (/IDA)
Mitochondrial proton-transporting ATP synthase complex, catalytic core F(1) GO:0000275
The catalytic sector of the mitochondrial hydrogen-transporting ATP synthase; it comprises the catalytic core and central stalk, and is peripherally associated with the mitochondrial inner membrane when the entire ATP synthase is assembled.
1 P15999 (/IDA)
Mitochondrial proton-transporting ATP synthase complex, catalytic core F(1) GO:0000275
The catalytic sector of the mitochondrial hydrogen-transporting ATP synthase; it comprises the catalytic core and central stalk, and is peripherally associated with the mitochondrial inner membrane when the entire ATP synthase is assembled.
1 Q03265 (/ISO)
Mitochondrial proton-transporting ATP synthase complex, catalytic core F(1) GO:0000275
The catalytic sector of the mitochondrial hydrogen-transporting ATP synthase; it comprises the catalytic core and central stalk, and is peripherally associated with the mitochondrial inner membrane when the entire ATP synthase is assembled.
1 P35381 (/ISS)
Nucleus GO:0005634
A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
1 P15999 (/IDA)
Nucleus GO:0005634
A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
1 Q03265 (/ISO)
Nucleolus GO:0005730
A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome.
1 F4IMB5 (/IDA)
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.
1 Q03265 (/ISO)
Mitochondrial inner membrane GO:0005743
The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae.
1 Q03265 (/HDA)
Mitochondrial inner membrane GO:0005743
The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae.
1 Q03265 (/ISO)
Mitochondrial proton-transporting ATP synthase complex GO:0005753
A proton-transporting ATP synthase complex found in the mitochondrial membrane.
1 Q03265 (/ISO)
Mitochondrial proton-transporting ATP synthase, catalytic core GO:0005754
The hexamer, comprising three alpha and three beta subunits, that possesses the catalytic activity of the mitochondrial hydrogen-transporting ATP synthase.
1 P24487 (/TAS)
Vacuole GO:0005773
A closed structure, found only in eukaryotic cells, that is completely surrounded by unit membrane and contains liquid material. Cells contain one or several vacuoles, that may have different functions from each other. Vacuoles have a diverse array of functions. They can act as a storage organelle for nutrients or waste products, as a degradative compartment, as a cost-effective way of increasing cell size, and as a homeostatic regulator controlling both turgor pressure and pH of the cytosol.
1 F4IMB5 (/IDA)
Vacuolar membrane GO:0005774
The lipid bilayer surrounding the vacuole and separating its contents from the cytoplasm of the cell.
1 F4IMB5 (/IDA)
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.
1 Q03265 (/ISO)
Chloroplast envelope GO:0009941
The double lipid bilayer enclosing the chloroplast and separating its contents from the rest of the cytoplasm; includes the intermembrane space.
1 F4IMB5 (/IDA)
Cell surface GO:0009986
The external part of the cell wall and/or plasma membrane.
1 Q03265 (/ISO)
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
1 Q03265 (/IMP)
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
1 Q03265 (/ISO)
Proton-transporting two-sector ATPase complex GO:0016469
A large protein complex that catalyzes the synthesis or hydrolysis of ATP by a rotational mechanism, coupled to the transport of protons across a membrane. The complex comprises a membrane sector (F0, V0, or A0) that carries out proton transport and a cytoplasmic compartment sector (F1, V1, or A1) that catalyzes ATP synthesis or hydrolysis. Two major types have been characterized: V-type ATPases couple ATP hydrolysis to the transport of protons across a concentration gradient, whereas F-type ATPases, also known as ATP synthases, normally run in the reverse direction to utilize energy from a proton concentration or electrochemical gradient to synthesize ATP. A third type, A-type ATPases have been found in archaea, and are closely related to eukaryotic V-type ATPases but are reversible.
1 Q1Q3H2 (/ISM)
Hyphal cell wall GO:0030446
The cell wall surrounding a fungal hypha.
1 A0A1D8PDC4 (/IDA)
Myelin sheath GO:0043209
An electrically insulating fatty layer that surrounds the axons of many neurons. It is an outgrowth of glial cells: Schwann cells supply the myelin for peripheral neurons while oligodendrocytes supply it to those of the central nervous system.
1 Q03265 (/HDA)
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.
1 P15999 (/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.
1 Q03265 (/ISO)
Proton-transporting ATP synthase complex GO:0045259
A proton-transporting two-sector ATPase complex that catalyzes the phosphorylation of ADP to ATP during oxidative phosphorylation. The complex comprises a membrane sector (F0) that carries out proton transport and a cytoplasmic compartment sector (F1) that catalyzes ATP synthesis by a rotational mechanism; the extramembrane sector (containing 3 a and 3 b subunits) is connected via the d-subunit to the membrane sector by several smaller subunits. Within this complex, the g and e subunits and the 9-12 c subunits rotate by consecutive 120 degree angles and perform parts of ATP synthesis. This movement is driven by the hydrogen ion electrochemical potential gradient.
1 Q03265 (/ISO)
Proton-transporting ATP synthase complex, catalytic core F(1) GO:0045261
The sector of a hydrogen-transporting ATP synthase complex in which the catalytic activity resides; it comprises the catalytic core and central stalk, and is peripherally associated with a membrane, such as the plasma membrane or the mitochondrial inner membrane, when the entire ATP synthase is assembled.
1 Q03265 (/ISO)
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