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:
"Laminin
".
FunFam 162: Coagulation factor X (Predicted)
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 18 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 |
---|---|---|
Serine-type endopeptidase activity GO:0004252
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
|
10 | P00742 (/IDA) P00742 (/IDA) P00742 (/IDA) P00742 (/IDA) P81428 (/IDA) P82807 (/IDA) P83370 (/IDA) Q56VR3 (/IDA) Q58L94 (/IDA) Q58L96 (/IDA) |
Endopeptidase activity GO:0004175
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain.
|
9 | P00741 (/ISS) P16293 (/ISS) P16294 (/ISS) P16296 (/ISS) P19540 (/ISS) Q6SA95 (/ISS) Q804X6 (/ISS) Q95ND7 (/ISS) Q95ND7 (/ISS) |
Calcium ion binding GO:0005509
Interacting selectively and non-covalently with calcium ions (Ca2+).
|
9 | P00741 (/ISS) P16293 (/ISS) P16294 (/ISS) P16296 (/ISS) P19540 (/ISS) Q6SA95 (/ISS) Q804X6 (/ISS) Q95ND7 (/ISS) Q95ND7 (/ISS) |
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).
|
8 | P00740 (/IPI) P00742 (/IPI) P00742 (/IPI) P00742 (/IPI) P00742 (/IPI) Q56VR3 (/IPI) Q58L95 (/IPI) Q58L96 (/IPI) |
Serine-type endopeptidase activity GO:0004252
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
|
5 | A6MFK7 (/ISS) A6MFK8 (/ISS) B5G6G5 (/ISS) Q58L93 (/ISS) Q58L95 (/ISS) |
Serine-type endopeptidase activity GO:0004252
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
|
4 | P00742 (/IMP) P00742 (/IMP) P00742 (/IMP) P00742 (/IMP) |
Serine-type endopeptidase activity GO:0004252
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
|
4 | P00742 (/TAS) P00742 (/TAS) P00742 (/TAS) P00742 (/TAS) |
Phospholipid binding GO:0005543
Interacting selectively and non-covalently with phospholipids, a class of lipids containing phosphoric acid as a mono- or diester.
|
4 | P00742 (/IDA) P00742 (/IDA) P00742 (/IDA) P00742 (/IDA) |
Endopeptidase activity GO:0004175
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain.
|
2 | P00740 (/IDA) P00741 (/IDA) |
Serine-type endopeptidase activity GO:0004252
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
|
2 | O88947 (/ISO) O88947 (/ISO) |
Calcium ion binding GO:0005509
Interacting selectively and non-covalently with calcium ions (Ca2+).
|
2 | P00740 (/IDA) P00741 (/IDA) |
Phospholipid binding GO:0005543
Interacting selectively and non-covalently with phospholipids, a class of lipids containing phosphoric acid as a mono- or diester.
|
2 | O88947 (/ISO) O88947 (/ISO) |
Magnesium ion binding GO:0000287
Interacting selectively and non-covalently with magnesium (Mg) ions.
|
1 | P00741 (/IDA) |
Endopeptidase activity GO:0004175
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain.
|
1 | P16294 (/ISO) |
Serine-type endopeptidase activity GO:0004252
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
|
1 | P00740 (/NAS) |
Calcium ion binding GO:0005509
Interacting selectively and non-covalently with calcium ions (Ca2+).
|
1 | P16294 (/ISO) |
Calcium ion binding GO:0005509
Interacting selectively and non-covalently with calcium ions (Ca2+).
|
1 | Q9CQW3 (/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.
|
1 | P16294 (/IDA) |
There are 23 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.
|
8 | P00741 (/ISS) P16293 (/ISS) P16296 (/ISS) P19540 (/ISS) Q6SA95 (/ISS) Q804X6 (/ISS) Q95ND7 (/ISS) Q95ND7 (/ISS) |
Blood coagulation GO:0007596
The sequential process in which the multiple coagulation factors of the blood interact, ultimately resulting in the formation of an insoluble fibrin clot; it may be divided into three stages: stage 1, the formation of intrinsic and extrinsic prothrombin converting principle; stage 2, the formation of thrombin; stage 3, the formation of stable fibrin polymers.
|
8 | P00741 (/ISS) P16293 (/ISS) P16294 (/ISS) P19540 (/ISS) Q6SA95 (/ISS) Q804X6 (/ISS) Q95ND7 (/ISS) Q95ND7 (/ISS) |
Zymogen activation GO:0031638
The proteolytic processing of an inactive enzyme to an active form.
|
8 | P16293 (/ISS) P16294 (/ISS) P16296 (/ISS) P19540 (/ISS) Q6SA95 (/ISS) Q804X6 (/ISS) Q95ND7 (/ISS) Q95ND7 (/ISS) |
Endoplasmic reticulum to Golgi vesicle-mediated transport GO:0006888
The directed movement of substances from the endoplasmic reticulum (ER) to the Golgi, mediated by COP II vesicles. Small COP II coated vesicles form from the ER and then fuse directly with the cis-Golgi. Larger structures are transported along microtubules to the cis-Golgi.
|
6 | P00740 (/TAS) P00742 (/TAS) P00742 (/TAS) P00742 (/TAS) P00742 (/TAS) P22891 (/TAS) |
Positive regulation of blood coagulation in other organism GO:0035807
Any process in which an organism activates, maintains or increases the frequency, rate or extent of blood coagulation in another organism. Blood coagulation is the sequential process in which the multiple coagulation factors of the blood interact, ultimately resulting in the formation of an insoluble fibrin clot.
|
6 | P81428 (/IDA) P82807 (/IDA) P83370 (/IDA) Q56VR3 (/IDA) Q58L94 (/IDA) Q58L96 (/IDA) |
Envenomation resulting in positive regulation of blood coagulation in other organism GO:0044469
A process that begins with venom being forced into an organism by the bite or sting of another organism, and ends with the resultant activation, maintenance or an increase in the frequency, rate or extent of blood coagulation in the bitten organism.
|
6 | P81428 (/IDA) P82807 (/IDA) P83370 (/IDA) Q56VR3 (/IDA) Q58L94 (/IDA) Q58L96 (/IDA) |
Positive regulation of blood coagulation in other organism GO:0035807
Any process in which an organism activates, maintains or increases the frequency, rate or extent of blood coagulation in another organism. Blood coagulation is the sequential process in which the multiple coagulation factors of the blood interact, ultimately resulting in the formation of an insoluble fibrin clot.
|
5 | A6MFK7 (/ISS) A6MFK8 (/ISS) B5G6G5 (/ISS) Q58L93 (/ISS) Q58L95 (/ISS) |
Envenomation resulting in positive regulation of blood coagulation in other organism GO:0044469
A process that begins with venom being forced into an organism by the bite or sting of another organism, and ends with the resultant activation, maintenance or an increase in the frequency, rate or extent of blood coagulation in the bitten organism.
|
5 | A6MFK7 (/ISS) A6MFK8 (/ISS) B5G6G5 (/ISS) Q58L93 (/ISS) Q58L95 (/ISS) |
Blood coagulation GO:0007596
The sequential process in which the multiple coagulation factors of the blood interact, ultimately resulting in the formation of an insoluble fibrin clot; it may be divided into three stages: stage 1, the formation of intrinsic and extrinsic prothrombin converting principle; stage 2, the formation of thrombin; stage 3, the formation of stable fibrin polymers.
|
4 | P00742 (/IC) P00742 (/IC) P00742 (/IC) P00742 (/IC) |
Blood coagulation GO:0007596
The sequential process in which the multiple coagulation factors of the blood interact, ultimately resulting in the formation of an insoluble fibrin clot; it may be divided into three stages: stage 1, the formation of intrinsic and extrinsic prothrombin converting principle; stage 2, the formation of thrombin; stage 3, the formation of stable fibrin polymers.
|
4 | P00740 (/IDA) P16296 (/IDA) Q63207 (/IDA) Q9CQW3 (/IDA) |
Blood coagulation GO:0007596
The sequential process in which the multiple coagulation factors of the blood interact, ultimately resulting in the formation of an insoluble fibrin clot; it may be divided into three stages: stage 1, the formation of intrinsic and extrinsic prothrombin converting principle; stage 2, the formation of thrombin; stage 3, the formation of stable fibrin polymers.
|
4 | P00742 (/TAS) P00742 (/TAS) P00742 (/TAS) P00742 (/TAS) |
Blood coagulation, extrinsic pathway GO:0007598
A protein activation cascade that contributes to blood coagulation and consists of the self-limited process linking exposure and activation of tissue factor to the activation of clotting factor X.
|
4 | P00742 (/TAS) P00742 (/TAS) P00742 (/TAS) P00742 (/TAS) |
Hemostasis GO:0007599
The stopping of bleeding (loss of body fluid) or the arrest of the circulation to an organ or part.
|
4 | F1QLC3 (/IMP) Q4V971 (/IMP) Q6PGW7 (/IMP) Q8JHC8 (/IMP) |
Positive regulation of cell migration GO:0030335
Any process that activates or increases the frequency, rate or extent of cell migration.
|
4 | P00742 (/TAS) P00742 (/TAS) P00742 (/TAS) P00742 (/TAS) |
Positive regulation of protein kinase B signaling GO:0051897
Any process that activates or increases the frequency, rate or extent of protein kinase B signaling, a series of reactions mediated by the intracellular serine/threonine kinase protein kinase B.
|
4 | P00742 (/IDA) P00742 (/IDA) P00742 (/IDA) P00742 (/IDA) |
Blood coagulation GO:0007596
The sequential process in which the multiple coagulation factors of the blood interact, ultimately resulting in the formation of an insoluble fibrin clot; it may be divided into three stages: stage 1, the formation of intrinsic and extrinsic prothrombin converting principle; stage 2, the formation of thrombin; stage 3, the formation of stable fibrin polymers.
|
3 | P00740 (/IMP) P16294 (/IMP) Q9CQW3 (/IMP) |
Blood coagulation GO:0007596
The sequential process in which the multiple coagulation factors of the blood interact, ultimately resulting in the formation of an insoluble fibrin clot; it may be divided into three stages: stage 1, the formation of intrinsic and extrinsic prothrombin converting principle; stage 2, the formation of thrombin; stage 3, the formation of stable fibrin polymers.
|
3 | O88947 (/ISO) O88947 (/ISO) P16294 (/ISO) |
Zymogen activation GO:0031638
The proteolytic processing of an inactive enzyme to an active form.
|
2 | P00740 (/IDA) P00741 (/IDA) |
Positive regulation of protein kinase B signaling GO:0051897
Any process that activates or increases the frequency, rate or extent of protein kinase B signaling, a series of reactions mediated by the intracellular serine/threonine kinase protein kinase B.
|
2 | O88947 (/ISO) O88947 (/ISO) |
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
1 | P00740 (/IDA) |
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
1 | P16294 (/ISO) |
Blood coagulation, intrinsic pathway GO:0007597
A protein activation cascade that contributes to blood coagulation and consists of the interactions among high molecular weight kininogen, prekallikrein, and factor XII that lead to the activation of clotting factor X.
|
1 | P00740 (/TAS) |
Zymogen activation GO:0031638
The proteolytic processing of an inactive enzyme to an active form.
|
1 | P16294 (/ISO) |
There are 20 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 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.
|
9 | P00741 (/ISS) P16293 (/ISS) P16294 (/ISS) P16296 (/ISS) P19540 (/ISS) Q6SA95 (/ISS) Q804X6 (/ISS) Q95ND7 (/ISS) Q95ND7 (/ISS) |
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.
|
7 | P81428 (/IDA) P82807 (/IDA) P83370 (/IDA) Q56VR3 (/IDA) Q58L94 (/IDA) Q58L96 (/IDA) Q9CQW3 (/IDA) |
Endoplasmic reticulum lumen GO:0005788
The volume enclosed by the membranes of the endoplasmic reticulum.
|
6 | P00740 (/TAS) P00742 (/TAS) P00742 (/TAS) P00742 (/TAS) P00742 (/TAS) P22891 (/TAS) |
Golgi lumen GO:0005796
The volume enclosed by the membranes of any cisterna or subcompartment of the Golgi apparatus, including the cis- and trans-Golgi networks.
|
6 | P00740 (/TAS) P00742 (/TAS) P00742 (/TAS) P00742 (/TAS) P00742 (/TAS) P22891 (/TAS) |
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.
|
5 | A6MFK7 (/ISS) A6MFK8 (/ISS) B5G6G5 (/ISS) Q58L93 (/ISS) Q58L95 (/ISS) |
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.
|
5 | P00740 (/NAS) P00742 (/NAS) P00742 (/NAS) P00742 (/NAS) P00742 (/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.
|
5 | P00740 (/TAS) P00742 (/TAS) P00742 (/TAS) P00742 (/TAS) P00742 (/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.
|
5 | P00740 (/TAS) P00742 (/TAS) P00742 (/TAS) P00742 (/TAS) P00742 (/TAS) |
Intrinsic component of external side of plasma membrane GO:0031233
The component of a plasma membrane consisting of gene products and protein complexes that penetrate the external side of the plasma membrane only, either directly or via some covalently attached hydrophobic anchor.
|
4 | P00742 (/IC) P00742 (/IC) P00742 (/IC) P00742 (/IC) |
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).
|
2 | O88947 (/ISO) O88947 (/ISO) |
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
|
2 | O88947 (/ISO) O88947 (/ISO) |
Protein-containing complex GO:0032991
A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.
|
2 | Q56VR3 (/IDA) Q58L96 (/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.
|
2 | O88947 (/ISO) O88947 (/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 | P00740 (/HDA) P22891 (/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.
|
1 | P00740 (/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.
|
1 | P16294 (/ISO) |
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 | Q63207 (/IDA) |
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
|
1 | Q63207 (/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 | Q63207 (/IDA) |
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.
|
1 | P00740 (/HDA) |