Summary: Endoplasmic Reticulum Oxidoreductin 1 (ERO1)
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This is the Wikipedia entry entitled "ER Oxidoreductin". More...
ER Oxidoreductin Edit Wikipedia article
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This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.
This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
Endoplasmic Reticulum Oxidoreductin 1 (ERO1) Provide feedback
Members of this family are required for the formation of disulphide bonds in the ER [1,2].
Literature references
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Frand AR, Cuozzo JW, Kaiser CA; , Trends Cell Biol 2000;10:203-210.: Pathways for protein disulphide bond formation. PUBMED:10754564 EPMC:10754564
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Frand AR, Kaiser CA; , Mol Biol Cell 2000;11:2833-2843.: Two pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulum. PUBMED:10982384 EPMC:10982384
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Pollard MG, Travers KJ, Weissman JS; , Mol Cell 1998;1:171-182.: Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum. PUBMED:9659914 EPMC:9659914
This tab holds annotation information from the InterPro database.
InterPro entry IPR007266
This entry represents endoplasmic oxidoreductin-1 (Ero1) from yeast and its homologues from mammals, Ero1-Lalpha and Ero1-Lbeta. Ero1 is an essential oxidoreductase that oxidises proteins in the endoplasmic reticulum to produce disulfide bonds [PUBMED:10754564, PUBMED:10982384, PUBMED:22412017]. The activity of Ero1 is regulated by Pdi1, which is a protein disulfide isomerase. This regulation of Ero1 through reduction and oxidation of regulatory bonds within Ero1 is essential for maintaining the proper redox balance in the ER [PUBMED:22412017, PUBMED:18971943].
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
Cellular component | endoplasmic reticulum (GO:0005783) |
Molecular function | oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor (GO:0016671) |
protein disulfide isomerase activity (GO:0003756) | |
Biological process | oxidation-reduction process (GO:0055114) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Alignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the UniProtKB sequence database, the NCBI sequence database, and our metagenomics sequence database. More...
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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
Seed (166) |
Full (1562) |
Representative proteomes | UniProt (2243) |
NCBI (2747) |
Meta (6) |
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RP15 (441) |
RP35 (846) |
RP55 (1204) |
RP75 (1448) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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Seed (166) |
Full (1562) |
Representative proteomes | UniProt (2243) |
NCBI (2747) |
Meta (6) |
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RP15 (441) |
RP35 (846) |
RP55 (1204) |
RP75 (1448) |
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Raw Stockholm | |||||||||
Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
Seed source: | Pfam-B_4729 (release 7.3); |
Previous IDs: | none |
Type: | Family |
Sequence Ontology: | SO:0100021 |
Author: |
Wood V |
Number in seed: | 166 |
Number in full: | 1562 |
Average length of the domain: | 340.30 aa |
Average identity of full alignment: | 36 % |
Average coverage of the sequence by the domain: | 72.73 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 45638612 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 354 | ||||||||||||
Family (HMM) version: | 15 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the ERO1 domain has been found. There are 6 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.
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