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:

"
Hepatocyte Growth Factor
".

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: Coagulation factor XI

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 7 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).
8 P03951 (/TAS) P03951 (/TAS) P03951 (/TAS) P03951 (/TAS) P03952 (/TAS) P03952 (/TAS) P03952 (/TAS) P03952 (/TAS)
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 P03951 (/IPI) P03951 (/IPI) P03951 (/IPI) P03951 (/IPI) P03952 (/IPI) P03952 (/IPI) P03952 (/IPI) P03952 (/IPI)
Serine-type aminopeptidase activity GO:0070009
Catalysis of the hydrolysis of a peptide bond not more than three residues from the N-terminus of 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 A0A0G2K4I9 (/IDA) A0A0G2K4I9 (/IDA) A0A0G2K4I9 (/IDA) A0A0G2K4I9 (/IDA) Q6TUF8 (/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).
4 P03951 (/NAS) P03951 (/NAS) P03951 (/NAS) P03951 (/NAS)
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
4 Q91Y47 (/ISO) Q91Y47 (/ISO) Q91Y47 (/ISO) Q91Y47 (/ISO)
Protein homodimerization activity GO:0042803
Interacting selectively and non-covalently with an identical protein to form a homodimer.
4 Q2KJ63 (/IDA) Q2KJ63 (/IDA) Q2KJ63 (/IDA) Q2KJ63 (/IDA)
Serine-type aminopeptidase activity GO:0070009
Catalysis of the hydrolysis of a peptide bond not more than three residues from the N-terminus of 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 Q91Y47 (/ISO) Q91Y47 (/ISO) Q91Y47 (/ISO) Q91Y47 (/ISO)

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
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.
12 P26262 (/ISO) P26262 (/ISO) P26262 (/ISO) P26262 (/ISO) P26262 (/ISO) P26262 (/ISO) P26262 (/ISO) P26262 (/ISO) Q91Y47 (/ISO) Q91Y47 (/ISO)
(2 more)
Positive regulation of fibrinolysis GO:0051919
Any process that activates, maintains or increases the frequency, rate or extent of fibrinolysis, an ongoing process that solubilizes fibrin, resulting in the removal of small blood clots.
12 P26262 (/ISO) P26262 (/ISO) P26262 (/ISO) P26262 (/ISO) P26262 (/ISO) P26262 (/ISO) P26262 (/ISO) P26262 (/ISO) Q91Y47 (/ISO) Q91Y47 (/ISO)
(2 more)
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.
9 A0A0G2K4I9 (/IDA) A0A0G2K4I9 (/IDA) A0A0G2K4I9 (/IDA) A0A0G2K4I9 (/IDA) P03951 (/IDA) P03951 (/IDA) P03951 (/IDA) P03951 (/IDA) Q6TUF8 (/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.
9 A0A0G2K4I9 (/TAS) A0A0G2K4I9 (/TAS) A0A0G2K4I9 (/TAS) A0A0G2K4I9 (/TAS) P03951 (/TAS) P03951 (/TAS) P03951 (/TAS) P03951 (/TAS) Q6TUF8 (/TAS)
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.
8 P03951 (/TAS) P03951 (/TAS) P03951 (/TAS) P03951 (/TAS) P03952 (/TAS) P03952 (/TAS) P03952 (/TAS) P03952 (/TAS)
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.
8 P03951 (/IDA) P03951 (/IDA) P03951 (/IDA) P03951 (/IDA) P03952 (/IDA) P03952 (/IDA) P03952 (/IDA) P03952 (/IDA)
Positive regulation of fibrinolysis GO:0051919
Any process that activates, maintains or increases the frequency, rate or extent of fibrinolysis, an ongoing process that solubilizes fibrin, resulting in the removal of small blood clots.
8 P03951 (/IDA) P03951 (/IDA) P03951 (/IDA) P03951 (/IDA) P03952 (/IDA) P03952 (/IDA) P03952 (/IDA) P03952 (/IDA)
Factor XII activation GO:0002542
Any process that activates Factor XII (Hageman factor). Factor XII is a protein synthesized by the liver that circulates in an inactive form until it encounters collagen or basement membrane or activated platelets (as occurs at the site of endothelial injury). Factor XII then undergoes a conformational change (becoming factor XIIa), exposing an active serine center that can subsequently cleave protein substrates and activate a variety of mediator systems. Factor XII is a participant in the clotting cascade as well as the kinin cascade.
4 P03952 (/TAS) P03952 (/TAS) P03952 (/TAS) P03952 (/TAS)
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
4 P03952 (/TAS) P03952 (/TAS) P03952 (/TAS) P03952 (/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.
4 Q91Y47 (/ISO) Q91Y47 (/ISO) Q91Y47 (/ISO) Q91Y47 (/ISO)
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 P03951 (/NAS) P03951 (/NAS) P03951 (/NAS) P03951 (/NAS)
Extracellular matrix disassembly GO:0022617
A process that results in the breakdown of the extracellular matrix.
4 P03952 (/TAS) P03952 (/TAS) P03952 (/TAS) P03952 (/TAS)
Regulation of blood coagulation GO:0030193
Any process that modulates the frequency, rate or extent of blood coagulation.
4 Q91Y47 (/IMP) Q91Y47 (/IMP) Q91Y47 (/IMP) Q91Y47 (/IMP)
Zymogen activation GO:0031638
The proteolytic processing of an inactive enzyme to an active form.
4 P03952 (/TAS) P03952 (/TAS) P03952 (/TAS) P03952 (/TAS)
Liver regeneration GO:0097421
The regrowth of lost or destroyed liver.
4 P14272 (/IEP) P14272 (/IEP) P14272 (/IEP) P14272 (/IEP)

There are 7 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.
17 A0A0G2K4I9 (/IDA) A0A0G2K4I9 (/IDA) A0A0G2K4I9 (/IDA) A0A0G2K4I9 (/IDA) P03951 (/IDA) P03951 (/IDA) P03951 (/IDA) P03951 (/IDA) P03952 (/IDA) P03952 (/IDA)
(7 more)
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.
12 P26262 (/ISO) P26262 (/ISO) P26262 (/ISO) P26262 (/ISO) P26262 (/ISO) P26262 (/ISO) P26262 (/ISO) P26262 (/ISO) Q91Y47 (/ISO) Q91Y47 (/ISO)
(2 more)
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.
8 P03951 (/NAS) P03951 (/NAS) P03951 (/NAS) P03951 (/NAS) P03952 (/NAS) P03952 (/NAS) P03952 (/NAS) P03952 (/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.
8 P03951 (/TAS) P03951 (/TAS) P03951 (/TAS) P03951 (/TAS) P03952 (/TAS) P03952 (/TAS) P03952 (/TAS) P03952 (/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.
8 P03951 (/TAS) P03951 (/TAS) P03951 (/TAS) P03951 (/TAS) P03952 (/TAS) P03952 (/TAS) P03952 (/TAS) P03952 (/TAS)
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.
8 P03951 (/HDA) P03951 (/HDA) P03951 (/HDA) P03951 (/HDA) P03952 (/HDA) P03952 (/HDA) P03952 (/HDA) P03952 (/HDA)
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
4 P03951 (/NAS) P03951 (/NAS) P03951 (/NAS) P03951 (/NAS)
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