The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:

"
Mannose-6-phosphate receptor binding 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 2112: Endoplasmic reticulum lectin 1

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 9 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
Glycoprotein binding GO:0001948
Interacting selectively and non-covalently with a glycoprotein, a protein that contains covalently bound glycose (monosaccharide) residues. These also include proteoglycans.
7 Q08B78 (/ISS) Q28IT1 (/ISS) Q3MHX6 (/ISS) Q5R8S4 (/ISS) Q5RKH6 (/ISS) Q8K2C7 (/ISS) Q8VEH8 (/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).
6 F1SQJ5 (/IPI) Q13438 (/IPI) Q8GWH3 (/IPI) Q8K2C7 (/IPI) Q96DZ1 (/IPI) Q99220 (/IPI)
Glycoprotein binding GO:0001948
Interacting selectively and non-covalently with a glycoprotein, a protein that contains covalently bound glycose (monosaccharide) residues. These also include proteoglycans.
2 Q13438 (/IDA) Q96DZ1 (/IDA)
Glycoprotein binding GO:0001948
Interacting selectively and non-covalently with a glycoprotein, a protein that contains covalently bound glycose (monosaccharide) residues. These also include proteoglycans.
2 Q8K2C7 (/ISO) Q8VEH8 (/ISO)
Glycoprotein binding GO:0001948
Interacting selectively and non-covalently with a glycoprotein, a protein that contains covalently bound glycose (monosaccharide) residues. These also include proteoglycans.
1 Q9UTC8 (/ISM)
Protease binding GO:0002020
Interacting selectively and non-covalently with any protease or peptidase.
1 Q5RKH6 (/IPI)
Unfolded protein binding GO:0051082
Interacting selectively and non-covalently with an unfolded protein.
1 Q96DZ1 (/IDA)
Unfolded protein binding GO:0051082
Interacting selectively and non-covalently with an unfolded protein.
1 Q8VEH8 (/ISO)
Oligosaccharide binding GO:0070492
Interacting selectively and non-covalently with any oligosaccharide, a molecule with between two and (about) 20 monosaccharide residues connected by glycosidic linkages.
1 Q99220 (/IDA)

There are 28 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
Ubiquitin-dependent ERAD pathway GO:0030433
The series of steps necessary to target endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. Begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein ubiquitination necessary for correct substrate transfer, transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome.
7 Q08B78 (/ISS) Q28IT1 (/ISS) Q3MHX6 (/ISS) Q5R8S4 (/ISS) Q5RKH6 (/ISS) Q8K2C7 (/ISS) Q8VEH8 (/ISS)
Protein retention in ER lumen GO:0006621
The retention in the endoplasmic reticulum (ER) lumen of soluble resident proteins. Sorting receptors retrieve proteins with ER localization signals, such as KDEL and HDEL sequences or some transmembrane domains, that have escaped to the cis-Golgi network and return them to the ER. Abnormally folded proteins and unassembled subunits are also selectively retained in the ER.
3 Q3MHX6 (/ISS) Q5RKH6 (/ISS) Q8K2C7 (/ISS)
Ubiquitin-dependent ERAD pathway GO:0030433
The series of steps necessary to target endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. Begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein ubiquitination necessary for correct substrate transfer, transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome.
3 Q13438 (/IMP) Q8GWH3 (/IMP) Q99220 (/IMP)
Ubiquitin-dependent ERAD pathway GO:0030433
The series of steps necessary to target endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. Begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein ubiquitination necessary for correct substrate transfer, transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome.
3 Q8K2C7 (/ISO) Q8VEH8 (/ISO) Q9UTC8 (/ISO)
Protein ubiquitination involved in ubiquitin-dependent protein catabolic process GO:0042787
The process in which a ubiquitin group, or multiple groups, are covalently attached to the target protein, thereby initiating the degradation of that protein.
3 Q3MHX6 (/ISS) Q5RKH6 (/ISS) Q8K2C7 (/ISS)
Response to endoplasmic reticulum stress GO:0034976
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 stress acting at the endoplasmic reticulum. ER stress usually results from the accumulation of unfolded or misfolded proteins in the ER lumen.
2 Q3MHX6 (/ISS) Q8K2C7 (/ISS)
Transmembrane transport GO:0055085
The process in which a solute is transported across a lipid bilayer, from one side of a membrane to the other
2 Q13438 (/TAS) Q96DZ1 (/TAS)
Negative regulation of retrograde protein transport, ER to cytosol GO:1904153
Any process that stops, prevents or reduces the frequency, rate or extent of retrograde protein transport, ER to cytosol.
2 Q13438 (/IMP) Q96DZ1 (/IMP)
Negative regulation of retrograde protein transport, ER to cytosol GO:1904153
Any process that stops, prevents or reduces the frequency, rate or extent of retrograde protein transport, ER to cytosol.
2 Q8K2C7 (/ISO) Q8VEH8 (/ISO)
Protein targeting GO:0006605
The process of targeting specific proteins to particular regions of the cell, typically membrane-bounded subcellular organelles. Usually requires an organelle specific protein sequence motif.
1 Q5RKH6 (/IDA)
Protein retention in ER lumen GO:0006621
The retention in the endoplasmic reticulum (ER) lumen of soluble resident proteins. Sorting receptors retrieve proteins with ER localization signals, such as KDEL and HDEL sequences or some transmembrane domains, that have escaped to the cis-Golgi network and return them to the ER. Abnormally folded proteins and unassembled subunits are also selectively retained in the ER.
1 Q13438 (/IDA)
Protein retention in ER lumen GO:0006621
The retention in the endoplasmic reticulum (ER) lumen of soluble resident proteins. Sorting receptors retrieve proteins with ER localization signals, such as KDEL and HDEL sequences or some transmembrane domains, that have escaped to the cis-Golgi network and return them to the ER. Abnormally folded proteins and unassembled subunits are also selectively retained in the ER.
1 Q8K2C7 (/ISO)
Response to salt stress GO:0009651
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 an increase or decrease in the concentration of salt (particularly but not exclusively sodium and chloride ions) in the environment.
1 Q8GWH3 (/IMP)
Protein ubiquitination GO:0016567
The process in which one or more ubiquitin groups are added to a protein.
1 Q13438 (/IMP)
Protein ubiquitination GO:0016567
The process in which one or more ubiquitin groups are added to a protein.
1 Q8K2C7 (/ISO)
Protein ubiquitination GO:0016567
The process in which one or more ubiquitin groups are added to a protein.
1 Q8K2C7 (/ISS)
Ubiquitin-dependent ERAD pathway GO:0030433
The series of steps necessary to target endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. Begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein ubiquitination necessary for correct substrate transfer, transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome.
1 Q96DZ1 (/IDA)
Ubiquitin-dependent ERAD pathway GO:0030433
The series of steps necessary to target endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. Begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein ubiquitination necessary for correct substrate transfer, transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome.
1 Q8GWH3 (/IGI)
Endoplasmic reticulum unfolded protein response GO:0030968
The series of molecular signals generated as a consequence of the presence of unfolded proteins in the endoplasmic reticulum (ER) or other ER-related stress; results in changes in the regulation of transcription and translation.
1 Q99220 (/IMP)
Endoplasmic reticulum unfolded protein response GO:0030968
The series of molecular signals generated as a consequence of the presence of unfolded proteins in the endoplasmic reticulum (ER) or other ER-related stress; results in changes in the regulation of transcription and translation.
1 Q9UTC8 (/ISO)
Retrograde protein transport, ER to cytosol GO:0030970
The directed movement of unfolded or misfolded proteins from the endoplasmic reticulum to the cytosol through the translocon.
1 Q99220 (/IMP)
Response to endoplasmic reticulum stress GO:0034976
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 stress acting at the endoplasmic reticulum. ER stress usually results from the accumulation of unfolded or misfolded proteins in the ER lumen.
1 Q13438 (/IDA)
Response to endoplasmic reticulum stress GO:0034976
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 stress acting at the endoplasmic reticulum. ER stress usually results from the accumulation of unfolded or misfolded proteins in the ER lumen.
1 Q8K2C7 (/ISO)
ERAD pathway GO:0036503
The protein catabolic pathway which targets endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. It begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein modifications necessary for correct substrate transfer (e.g. ubiquitination), transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome.
1 Q96DZ1 (/TAS)
Protein ubiquitination involved in ubiquitin-dependent protein catabolic process GO:0042787
The process in which a ubiquitin group, or multiple groups, are covalently attached to the target protein, thereby initiating the degradation of that protein.
1 Q13438 (/IMP)
Protein ubiquitination involved in ubiquitin-dependent protein catabolic process GO:0042787
The process in which a ubiquitin group, or multiple groups, are covalently attached to the target protein, thereby initiating the degradation of that protein.
1 Q8K2C7 (/ISO)
Ubiquitin-dependent glycoprotein ERAD pathway GO:0097466
An ERAD pathway whereby endoplasmic reticulum (ER)-resident glycoproteins are targeted for degradation. Includes differential processing of the glycoprotein sugar chains, retrotranslocation to the cytosol and degradation by the ubiquitin-proteasome pathway. A glycoprotein is a compound in which a carbohydrate component is covalently bound to a protein component.
1 Q99220 (/IMP)
Endoplasmic reticulum mannose trimming GO:1904380
Any protein alpha-1,2-demannosylation that takes place in the endoplasmic reticulum quality control compartment (ERQC).
1 Q13438 (/TAS)

There are 11 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
Endoplasmic reticulum lumen GO:0005788
The volume enclosed by the membranes of the endoplasmic reticulum.
6 Q08B78 (/ISS) Q28IT1 (/ISS) Q3MHX6 (/ISS) Q5R8S4 (/ISS) Q8K2C7 (/ISS) Q8VEH8 (/ISS)
Endoplasmic reticulum lumen GO:0005788
The volume enclosed by the membranes of the endoplasmic reticulum.
4 Q13438 (/IDA) Q5RKH6 (/IDA) Q96DZ1 (/IDA) Q99220 (/IDA)
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 Q5RKH6 (/IDA) Q8GWH3 (/IDA)
Endoplasmic reticulum lumen GO:0005788
The volume enclosed by the membranes of the endoplasmic reticulum.
2 Q8K2C7 (/ISO) Q8VEH8 (/ISO)
Hrd1p ubiquitin ligase complex GO:0000836
A multiprotein complex that recognizes and ubiquitinates proteins with misfolded luminal and membrane domains during ER-associated protein degradation (ERAD). In S. cerevisiae, this complex contains the ubiquitin ligase Hrd1p. In mammals, this complex contains the ubiquitin ligase HRD1 (Synoviolin) or AMFR (gp78).
1 Q13438 (/NAS)
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 Q9UTC8 (/ISO)
Endoplasmic reticulum membrane GO:0005789
The lipid bilayer surrounding the endoplasmic reticulum.
1 Q13438 (/TAS)
Endomembrane system GO:0012505
A collection of membranous structures involved in transport within the cell. The main components of the endomembrane system are endoplasmic reticulum, Golgi bodies, vesicles, cell membrane and nuclear envelope. Members of the endomembrane system pass materials through each other or though the use of vesicles.
1 Q9VKC7 (/IDA)
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
1 Q9UTC8 (/NAS)
Luminal surveillance complex GO:0034099
A multiprotein complex that recognizes ERAD-luminal misfolded substrates and brings them to the ubiquitination/extraction machinery. In yeast, this complex consists of Yos9p, Kar2p and Hrd3p proteins.
1 Q99220 (/IDA)
Endoplasmic reticulum quality control compartment GO:0044322
A subcompartment of the endoplasmic reticulum in which proteins with improper or incorrect folding accumulate. Enzymes in this compartment direct proteins with major folding problems to translocation to the cytosol and degradation, and proteins with minor folding problems to the ER, to interact with chaperon proteins.
1 Q96DZ1 (/TAS)
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