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:

"
Collagenase (Catalytic Domain)
".

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 5: Matrix metallopeptidase 16

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 15 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
Metalloendopeptidase activity GO:0004222
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain 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.
17 P51511 (/TAS) P51511 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS)
(7 more)
Enzyme activator activity GO:0008047
Binds to and increases the activity of an enzyme.
17 P51511 (/TAS) P51511 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS)
(7 more)
Zinc ion binding GO:0008270
Interacting selectively and non-covalently with zinc (Zn) ions.
15 P51511 (/TAS) P51511 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS)
(5 more)
Metalloaminopeptidase activity GO:0070006
Catalysis of the hydrolysis of N-terminal amino acid residues from a polypeptide chain 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.
15 P51511 (/TAS) P51511 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS)
(5 more)
Metalloendopeptidase activity GO:0004222
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain 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.
14 P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA)
(4 more)
Zinc ion binding GO:0008270
Interacting selectively and non-covalently with zinc (Zn) ions.
13 P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA)
(3 more)
Metalloaminopeptidase activity GO:0070006
Catalysis of the hydrolysis of N-terminal amino acid residues from a polypeptide chain 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.
13 P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA)
(3 more)
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.
5 B0R0I1 (/NAS) B3DFR2 (/NAS) F1Q899 (/NAS) Q7T2J1 (/NAS) Q7T2J2 (/NAS)
Metalloendopeptidase activity GO:0004222
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain 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.
4 O54732 (/ISS) Q99PW6 (/ISS) Q9Y5R2 (/ISS) Q9Y5R2 (/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).
2 P51511 (/IPI) P51511 (/IPI)
Metalloendopeptidase activity GO:0004222
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain 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 Q9WTR0 (/ISO)
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 Q99PW6 (/TAS)
Zinc ion binding GO:0008270
Interacting selectively and non-covalently with zinc (Zn) ions.
1 Q9WTR0 (/ISO)
Cadherin binding GO:0045296
Interacting selectively and non-covalently with cadherin, a type I membrane protein involved in cell adhesion.
1 Q9R0S2 (/IPI)
Metalloaminopeptidase activity GO:0070006
Catalysis of the hydrolysis of N-terminal amino acid residues from a polypeptide chain 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 Q9WTR0 (/ISO)

There are 45 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.
17 P51511 (/TAS) P51511 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS)
(7 more)
Extracellular matrix disassembly GO:0022617
A process that results in the breakdown of the extracellular matrix.
15 P51511 (/TAS) P51511 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS)
(5 more)
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
13 P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA)
(3 more)
Protein processing GO:0016485
Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a protein. Protein maturation is the process leading to the attainment of the full functional capacity of a protein.
13 P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA)
(3 more)
Protein metabolic process GO:0019538
The chemical reactions and pathways involving a protein. Includes protein modification.
13 P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS)
(3 more)
Anterior/posterior axis specification GO:0009948
The establishment, maintenance and elaboration of the anterior/posterior axis. The anterior-posterior axis is defined by a line that runs from the head or mouth of an organism to the tail or opposite end of the organism.
5 B0R0I1 (/IMP) B3DFR2 (/IMP) F1Q899 (/IMP) Q7T2J1 (/IMP) Q7T2J2 (/IMP)
Establishment of cell polarity GO:0030010
The specification and formation of anisotropic intracellular organization or cell growth patterns.
5 B0R0I1 (/IGI) B3DFR2 (/IGI) F1Q899 (/IGI) Q7T2J1 (/IGI) Q7T2J2 (/IGI)
Cell migration involved in gastrulation GO:0042074
The migration of individual cells within the blastocyst to help establish the multi-layered body plan of the organism (gastrulation). For example, the migration of cells from the surface to the interior of the embryo (ingression).
5 B0R0I1 (/IGI) B3DFR2 (/IGI) F1Q899 (/IGI) Q7T2J1 (/IGI) Q7T2J2 (/IGI)
Cartilage development GO:0051216
The process whose specific outcome is the progression of a cartilage element over time, from its formation to the mature structure. Cartilage elements are skeletal elements that consist of connective tissue dominated by extracellular matrix containing collagen type II and large amounts of proteoglycan, particularly chondroitin sulfate.
5 B0R0I1 (/IMP) B3DFR2 (/IMP) F1Q899 (/IMP) Q7T2J1 (/IMP) Q7T2J2 (/IMP)
Convergent extension GO:0060026
The morphogenetic process in which an epithelium narrows along one axis and lengthens in a perpendicular axis.
5 B0R0I1 (/IGI) B3DFR2 (/IGI) F1Q899 (/IGI) Q7T2J1 (/IGI) Q7T2J2 (/IGI)
Convergent extension involved in gastrulation GO:0060027
The morphogenetic process in which an epithelium narrows along one axis and lengthens in a perpendicular axis usually resulting in the formation of the three primary germ layers, ectoderm, mesoderm and endoderm.
5 B0R0I1 (/IGI) B3DFR2 (/IGI) F1Q899 (/IGI) Q7T2J1 (/IGI) Q7T2J2 (/IGI)
Convergent extension involved in gastrulation GO:0060027
The morphogenetic process in which an epithelium narrows along one axis and lengthens in a perpendicular axis usually resulting in the formation of the three primary germ layers, ectoderm, mesoderm and endoderm.
5 B0R0I1 (/IMP) B3DFR2 (/IMP) F1Q899 (/IMP) Q7T2J1 (/IMP) Q7T2J2 (/IMP)
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
3 Q99PW6 (/ISS) Q9Y5R2 (/ISS) Q9Y5R2 (/ISS)
Glial cell differentiation GO:0010001
The process in which a relatively unspecialized cell acquires the specialized features of a glial cell.
3 Q99PW6 (/ISS) Q9Y5R2 (/ISS) Q9Y5R2 (/ISS)
Cell-cell adhesion mediated by cadherin GO:0044331
The attachment of one cell to another cell via a cadherin, transmembrane proteins having repeating extracellular calcium ion binding domains.
3 Q99PW6 (/ISS) Q9Y5R2 (/ISS) Q9Y5R2 (/ISS)
Detection of temperature stimulus involved in sensory perception of pain GO:0050965
The series of events involved in the perception of pain in which a temperature stimulus is received and converted into a molecular signal.
3 Q99PW6 (/ISS) Q9Y5R2 (/ISS) Q9Y5R2 (/ISS)
Neuronal stem cell population maintenance GO:0097150
Any process in by an organism or tissue maintains a population of neuronal stem cells.
3 Q99PW6 (/ISS) Q9Y5R2 (/ISS) Q9Y5R2 (/ISS)
Cell-cell adhesion via plasma-membrane adhesion molecules GO:0098742
The attachment of one cell to another cell via adhesion molecules that are at least partially embedded in the plasma membrane.
3 Q99PW6 (/ISS) Q9Y5R2 (/ISS) Q9Y5R2 (/ISS)
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.
2 F1Q899 (/IDA) Q7T2J2 (/IDA)
Neural retina development GO:0003407
The progression of the neural retina over time from its initial formation to the mature structure. The neural retina is the part of the retina that contains neurons and photoreceptor cells.
2 F1Q899 (/IMP) Q7T2J2 (/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).
2 P51511 (/TAS) P51511 (/TAS)
Retina layer formation GO:0010842
The process in which the vertebrate retina is organized into three laminae: the outer nuclear layer (ONL), which contains photoreceptor nuclei; the inner nuclear layer (INL), which contains amacrine, bipolar and horizontal cells; and the retinal ganglion cell (RGC) layer. Between the inner and outer nuclear layers, the outer plexiform layer (OPL) contains connections between the photoreceptors and bipolar and horizontal cells. The inner plexiform layer (IPL) is positioned between the INL and the ganglion cell layer and contains the dendrites of RGCs and processes of bipolar and amacrine cells. Spanning all layers of the retina are the radially oriented Mueller glia.
2 F1Q899 (/IMP) Q7T2J2 (/IMP)
Collagen catabolic process GO:0030574
The proteolytic chemical reactions and pathways resulting in the breakdown of collagen in the extracellular matrix, usually carried out by proteases secreted by nearby cells.
2 P51511 (/TAS) P51511 (/TAS)
Retinal ganglion cell axon guidance GO:0031290
The process in which the migration of an axon growth cone of a retinal ganglion cell (RGC) is directed to its target in the brain in response to a combination of attractive and repulsive cues.
2 F1Q899 (/IGI) Q7T2J2 (/IGI)
Retinal ganglion cell axon guidance GO:0031290
The process in which the migration of an axon growth cone of a retinal ganglion cell (RGC) is directed to its target in the brain in response to a combination of attractive and repulsive cues.
2 F1Q899 (/IMP) Q7T2J2 (/IMP)
Endodermal cell differentiation GO:0035987
The process in which a relatively unspecialized cell acquires the specialized features of an endoderm cell, a cell of the inner of the three germ layers of the embryo.
2 P51511 (/IEP) P51511 (/IEP)
Embryonic cranial skeleton morphogenesis GO:0048701
The process in which the anatomical structures of the cranial skeleton are generated and organized during the embryonic phase.
2 F1Q899 (/IMP) Q7T2J2 (/IMP)
Ossification GO:0001503
The formation of bone or of a bony substance, or the conversion of fibrous tissue or of cartilage into bone or a bony substance.
1 Q9WTR0 (/IGI)
Endochondral ossification GO:0001958
Replacement ossification wherein bone tissue replaces cartilage.
1 Q9WTR0 (/IGI)
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
1 Q9R0S2 (/IMP)
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
1 Q9WTR0 (/ISO)
Glial cell differentiation GO:0010001
The process in which a relatively unspecialized cell acquires the specialized features of a glial cell.
1 Q9R0S2 (/IDA)
Protein processing GO:0016485
Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a protein. Protein maturation is the process leading to the attainment of the full functional capacity of a protein.
1 Q9WTR0 (/ISO)
Collagen catabolic process GO:0030574
The proteolytic chemical reactions and pathways resulting in the breakdown of collagen in the extracellular matrix, usually carried out by proteases secreted by nearby cells.
1 Q9WTR0 (/IDA)
Collagen catabolic process GO:0030574
The proteolytic chemical reactions and pathways resulting in the breakdown of collagen in the extracellular matrix, usually carried out by proteases secreted by nearby cells.
1 Q9WTR0 (/IGI)
Response to estradiol GO:0032355
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 stimulus by estradiol, a C18 steroid hormone hydroxylated at C3 and C17 that acts as a potent estrogen.
1 D3ZCG5 (/IEP)
Chondrocyte proliferation GO:0035988
The multiplication or reproduction of chondrocytes by cell division, resulting in the expansion of their population. A chondrocyte is a polymorphic cell that forms cartilage.
1 Q9WTR0 (/IGI)
Cell-cell adhesion mediated by cadherin GO:0044331
The attachment of one cell to another cell via a cadherin, transmembrane proteins having repeating extracellular calcium ion binding domains.
1 Q9R0S2 (/IDA)
Embryonic cranial skeleton morphogenesis GO:0048701
The process in which the anatomical structures of the cranial skeleton are generated and organized during the embryonic phase.
1 Q9WTR0 (/IGI)
Detection of temperature stimulus involved in sensory perception of pain GO:0050965
The series of events involved in the perception of pain in which a temperature stimulus is received and converted into a molecular signal.
1 Q9R0S2 (/IMP)
Bone development GO:0060348
The process whose specific outcome is the progression of bone over time, from its formation to the mature structure. Bone is the hard skeletal connective tissue consisting of both mineral and cellular components.
1 Q9WTR0 (/IGI)
Craniofacial suture morphogenesis GO:0097094
The process in which any suture between cranial and/or facial bones is generated and organized.
1 Q9WTR0 (/IGI)
Neuronal stem cell population maintenance GO:0097150
Any process in by an organism or tissue maintains a population of neuronal stem cells.
1 Q9R0S2 (/IDA)
Cell-cell adhesion via plasma-membrane adhesion molecules GO:0098742
The attachment of one cell to another cell via adhesion molecules that are at least partially embedded in the plasma membrane.
1 Q9R0S2 (/IMP)
Response to odorant GO:1990834
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 odorant stimulus. An odorant is any substance capable of stimulating the sense of smell.
1 O35548 (/IEP)

There are 10 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.
15 P51511 (/TAS) P51511 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS)
(5 more)
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.
14 P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA)
(4 more)
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.
13 P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS)
(3 more)
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.
4 P51511 (/TAS) P51511 (/TAS) Q9Y5R2 (/TAS) Q9Y5R2 (/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.
3 Q99PW6 (/ISS) Q9Y5R2 (/ISS) Q9Y5R2 (/ISS)
Trans-Golgi network membrane GO:0032588
The lipid bilayer surrounding any of the compartments that make up the trans-Golgi network.
3 Q99PW6 (/ISS) Q9Y5R2 (/ISS) Q9Y5R2 (/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.
2 Q9Y5R2 (/HDA) Q9Y5R2 (/HDA)
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 Q9WTR0 (/ISO)
Integral component of membrane GO:0016021
The component of a 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 Q99PW6 (/TAS)
Trans-Golgi network membrane GO:0032588
The lipid bilayer surrounding any of the compartments that make up the trans-Golgi network.
1 Q9R0S2 (/IDA)