The name of this superfamily has been modified since the most recent official CATH+ release (v4_4_0). At the point of the last release, this superfamily was named:

"
Laminin
".

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 483: Tissue-type plasminogen activator

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 10 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).
3 P00750 (/IDA) P11214 (/IDA) Q28198 (/IDA)
Phosphoprotein binding GO:0051219
Interacting selectively and non-covalently with a phosphorylated protein.
2 P00750 (/IPI) Q28198 (/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).
1 P11214 (/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 P00750 (/TAS)
Signaling receptor binding GO:0005102
Interacting selectively and non-covalently with one or more specific sites on a receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function.
1 P00750 (/IPI)
Signaling receptor binding GO:0005102
Interacting selectively and non-covalently with one or more specific sites on a receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function.
1 P11214 (/ISO)
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).
1 P00750 (/IPI)
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).
1 P00750 (/TAS)
Phosphoprotein binding GO:0051219
Interacting selectively and non-covalently with a phosphorylated protein.
1 P11214 (/ISO)
Serpin family protein binding GO:0097655
Interacting selectively and non-covalently with any member of the serpin protein family (serine protease inhibitors or classified inhibitor family I4). Serpins are a broadly distributed family of protease inhibitors that use a conformational change to inhibit target enzymes. They are central in controlling many important proteolytic cascades. The majority of serpins inhibit serine proteases, but serpins that inhibit caspases and papain-like cysteine proteases have also been identified. Rarely, serpins perform a non-inhibitory function; for example, several human serpins function as hormone transporters and certain serpins function as molecular chaperones or tumor suppressors.
1 Q28198 (/IPI)

There are 25 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
Plasminogen activation GO:0031639
The process in which inactive plasminogen is processed to active plasmin. This process includes cleavage at an internal Arg-Val site to form an N-terminal A-chain and C-terminal B-chain held together by a disulfide bond, and can include further proteolytic cleavage events to remove the preactivation peptide.
3 P00750 (/IDA) P19637 (/IDA) Q28198 (/IDA)
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
2 P11214 (/IDA) Q28198 (/IDA)
Response to hypoxia GO:0001666
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 indicating lowered oxygen tension. Hypoxia, defined as a decline in O2 levels below normoxic levels of 20.8 - 20.95%, results in metabolic adaptation at both the cellular and organismal level.
1 P11214 (/IMP)
Cellular protein modification process GO:0006464
The covalent alteration of one or more amino acids occurring in proteins, peptides and nascent polypeptides (co-translational, post-translational modifications) occurring at the level of an individual cell. Includes the modification of charged tRNAs that are destined to occur in a protein (pre-translation modification).
1 P00750 (/TAS)
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
1 P00750 (/TAS)
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.
1 P00750 (/TAS)
Smooth muscle cell migration GO:0014909
The orderly movement of a smooth muscle cell from one site to another, often during the development of a multicellular organism.
1 P11214 (/IMP)
Plasminogen activation GO:0031639
The process in which inactive plasminogen is processed to active plasmin. This process includes cleavage at an internal Arg-Val site to form an N-terminal A-chain and C-terminal B-chain held together by a disulfide bond, and can include further proteolytic cleavage events to remove the preactivation peptide.
1 P11214 (/ISO)
Synaptic transmission, glutamatergic GO:0035249
The vesicular release of glutamate from a presynapse, across a chemical synapse, the subsequent activation of glutamate receptors at the postsynapse of a target cell (neuron, muscle, or secretory cell) and the effects of this activation on the postsynaptic membrane potential and ionic composition of the postsynaptic cytosol. This process encompasses both spontaneous and evoked release of neurotransmitter and all parts of synaptic vesicle exocytosis. Evoked transmission starts with the arrival of an action potential at the presynapse.
1 P19637 (/IMP)
Synaptic transmission, glutamatergic GO:0035249
The vesicular release of glutamate from a presynapse, across a chemical synapse, the subsequent activation of glutamate receptors at the postsynapse of a target cell (neuron, muscle, or secretory cell) and the effects of this activation on the postsynaptic membrane potential and ionic composition of the postsynaptic cytosol. This process encompasses both spontaneous and evoked release of neurotransmitter and all parts of synaptic vesicle exocytosis. Evoked transmission starts with the arrival of an action potential at the presynapse.
1 P11214 (/ISO)
Wound healing GO:0042060
The series of events that restore integrity to a damaged tissue, following an injury.
1 P19637 (/IEP)
Fibrinolysis GO:0042730
A process that solubilizes fibrin in the bloodstream of a multicellular organism, chiefly by the proteolytic action of plasmin.
1 P00750 (/TAS)
Negative regulation of proteolysis GO:0045861
Any process that stops, prevents, or reduces the frequency, rate or extent of the hydrolysis of a peptide bond or bonds within a protein.
1 P00750 (/IDA)
Negative regulation of proteolysis GO:0045861
Any process that stops, prevents, or reduces the frequency, rate or extent of the hydrolysis of a peptide bond or bonds within a protein.
1 P11214 (/ISO)
Platelet-derived growth factor receptor signaling pathway GO:0048008
The series of molecular signals generated as a consequence of a platelet-derived growth factor receptor binding to one of its physiological ligands.
1 P11214 (/IDA)
Platelet-derived growth factor receptor signaling pathway GO:0048008
The series of molecular signals generated as a consequence of a platelet-derived growth factor receptor binding to one of its physiological ligands.
1 P11214 (/IMP)
Regulation of synaptic plasticity GO:0048167
A process that modulates synaptic plasticity, the ability of synapses to change as circumstances require. They may alter function, such as increasing or decreasing their sensitivity, or they may increase or decrease in actual numbers.
1 P19637 (/IEP)
Response to cAMP GO:0051591
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 cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate) stimulus.
1 P19637 (/IEP)
Positive regulation of ovulation GO:0060279
Any process that activates or increases the frequency, rate or extent of ovulation, the release of a mature ovum/oocyte from an ovary.
1 P19637 (/IMP)
Positive regulation of ovulation GO:0060279
Any process that activates or increases the frequency, rate or extent of ovulation, the release of a mature ovum/oocyte from an ovary.
1 P11214 (/ISO)
Response to fatty acid GO:0070542
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 fatty acid stimulus.
1 P19637 (/IEP)
Cellular response to follicle-stimulating hormone stimulus GO:0071372
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 follicle-stimulating hormone stimulus.
1 P19637 (/IEP)
Cellular response to luteinizing hormone stimulus GO:0071373
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 luteinizing hormone stimulus.
1 P19637 (/IEP)
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 P19637 (/IEP)
Trans-synaptic signaling by BDNF, modulating synaptic transmission GO:0099183
Cell-cell signaling between presynapse and postsynapse, via the vesicular release and reception of brain derived neurotrophic factor (BDNF), that modulates the synaptic transmission properties of the synapse.
1 P11214 (/IMP)

There are 25 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.
3 P11214 (/IDA) P19637 (/IDA) Q28198 (/IDA)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
3 P00750 (/IDA) P11214 (/IDA) P19637 (/IDA)
Glutamatergic synapse GO:0098978
A synapse that uses glutamate as a neurotransmitter.
2 P11214 (/IMP) P19637 (/IMP)
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 P00750 (/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.
1 P11214 (/ISO)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
1 P11214 (/ISO)
Cell surface GO:0009986
The external part of the cell wall and/or plasma membrane.
1 P00750 (/IDA)
Cell surface GO:0009986
The external part of the cell wall and/or plasma membrane.
1 P11214 (/ISO)
Secretory granule GO:0030141
A small subcellular vesicle, surrounded by a membrane, that is formed from the Golgi apparatus and contains a highly concentrated protein destined for secretion. Secretory granules move towards the periphery of the cell and upon stimulation, their membranes fuse with the cell membrane, and their protein load is exteriorized. Processing of the contained protein may take place in secretory granules.
1 P11214 (/IDA)
Apical part of cell GO:0045177
The region of a polarized cell that forms a tip or is distal to a base. For example, in a polarized epithelial cell, the apical region has an exposed surface and lies opposite to the basal lamina that separates the epithelium from other tissue.
1 P11214 (/IDA)
Synapse GO:0045202
The junction between a nerve fiber of one neuron and another neuron, muscle fiber or glial cell. As the nerve fiber approaches the synapse it enlarges into a specialized structure, the presynaptic nerve ending, which contains mitochondria and synaptic vesicles. At the tip of the nerve ending is the presynaptic membrane; facing it, and separated from it by a minute cleft (the synaptic cleft) is a specialized area of membrane on the receiving cell, known as the postsynaptic membrane. In response to the arrival of nerve impulses, the presynaptic nerve ending secretes molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane.
1 P19637 (/IDA)
Synapse GO:0045202
The junction between a nerve fiber of one neuron and another neuron, muscle fiber or glial cell. As the nerve fiber approaches the synapse it enlarges into a specialized structure, the presynaptic nerve ending, which contains mitochondria and synaptic vesicles. At the tip of the nerve ending is the presynaptic membrane; facing it, and separated from it by a minute cleft (the synaptic cleft) is a specialized area of membrane on the receiving cell, known as the postsynaptic membrane. In response to the arrival of nerve impulses, the presynaptic nerve ending secretes molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane.
1 P11214 (/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 P00750 (/HDA)
Schaffer collateral - CA1 synapse GO:0098685
A synapse between the Schaffer collateral axon of a CA3 pyramidal cell and a CA1 pyramidal cell.
1 P11214 (/IMP)
Postsynapse GO:0098794
The part of a synapse that is part of the post-synaptic cell.
1 P19637 (/IDA)
Postsynapse GO:0098794
The part of a synapse that is part of the post-synaptic cell.
1 P19637 (/IMP)
Postsynapse GO:0098794
The part of a synapse that is part of the post-synaptic cell.
1 P11214 (/ISO)
Glutamatergic synapse GO:0098978
A synapse that uses glutamate as a neurotransmitter.
1 P19637 (/IDA)
Glutamatergic synapse GO:0098978
A synapse that uses glutamate as a neurotransmitter.
1 P11214 (/ISO)
Neuronal dense core vesicle GO:0098992
A dense core vesicle (granule) that is part of a neuron. These vesicles typically contain neuropeptides. They can be found in all parts of neurons, including the soma, dendrites, axonal swellings (varicosities) and synaptic terminals.
1 P19637 (/IDA)
Neuronal dense core vesicle GO:0098992
A dense core vesicle (granule) that is part of a neuron. These vesicles typically contain neuropeptides. They can be found in all parts of neurons, including the soma, dendrites, axonal swellings (varicosities) and synaptic terminals.
1 P19637 (/IMP)
Neuronal dense core vesicle GO:0098992
A dense core vesicle (granule) that is part of a neuron. These vesicles typically contain neuropeptides. They can be found in all parts of neurons, including the soma, dendrites, axonal swellings (varicosities) and synaptic terminals.
1 P11214 (/ISO)
Perisynaptic space GO:0099544
The extracellular region immediately adjacent to to a synapse.
1 P19637 (/IDA)
Perisynaptic space GO:0099544
The extracellular region immediately adjacent to to a synapse.
1 P19637 (/IMP)
Perisynaptic space GO:0099544
The extracellular region immediately adjacent to to a synapse.
1 P11214 (/ISO)
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