Summary: Oligosaccaryltransferase
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This is the Wikipedia entry entitled "OST4". More...
OST4 Edit Wikipedia article
| Oligosaccaryltransferase | |||||||||
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| nmr structure of yeast oligosaccharyltransferase subunit ost4p | |||||||||
| Identifiers | |||||||||
| Symbol | Ost4 | ||||||||
| Pfam | PF10215 | ||||||||
| InterPro | IPR018943 | ||||||||
| OPM superfamily | 274 | ||||||||
| OPM protein | 2lat | ||||||||
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In molecular biology, OST4 (Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 4) is a subunit of the oligosaccharyltransferase complex.[1] OST4 is a very short, approximately 30 amino acids, protein found from fungi to vertebrates. It appears to be an integral membrane protein that mediates the en bloc transfer of a pre-assembled high-mannose oligosaccharide onto asparagine residues of nascent polypeptides as they enter the lumen of the rough endoplasmic reticulum.[2][3]
[edit] References
- ^ Kelleher DJ, Gilmore R (2006). "An evolving view of the eukaryotic oligosaccharyltransferase.". Glycobiology 16 (4): 47R-62R. doi:10.1093/glycob/cwj066. PMID 16317064. http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=16317064.
- ^ Gayen S, Kang C (2011). "Solution structure of a human minimembrane protein Ost4, a subunit of the oligosaccharyltransferase complex.". Biochem Biophys Res Commun 409 (3): 5726. doi:10.1016/j.bbrc.2011.05.050. PMID 21609714. http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=21609714.
- ^ Spirig U, Bodmer D, Wacker M, Burda P, Aebi M (2005). "The 3.4-kDa Ost4 protein is required for the assembly of two distinct oligosaccharyltransferase complexes in yeast.". Glycobiology 15 (12): 1396406. doi:10.1093/glycob/cwj025. PMID 16096346. http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=16096346.
This article incorporates text from the public domain Pfam and InterPro IPR018943
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.
Oligosaccaryltransferase Provide feedback
Ost4 is a very short, approximately 30 residues, enzyme found from fungi to vertebrates. It is a member of the ER oligosaccaryltansferase complex, EC 2.4.1.119, that catalyses the asparagine-linked glycosylation of proteins. It appears to be an integral membrane protein that mediates the en bloc transfer of a preassembled high-mannose oligosaccharide onto asparagine residues of nascent polypeptides as they enter the lumen of the rough endoplasmic reticulum (RER).
Literature references
-
Kelleher DJ, Gilmore R; , Glycobiology. 2006;16:47.: An evolving view of the eukaryotic oligosaccharyltransferase. PUBMED:16317064 EPMC:16317064
External database links
| PANDIT: | PF10215 |
| Pseudofam: | PF10215 |
| SYSTERS: | Ost4 |
This tab holds annotation information from the InterPro database.
InterPro entry IPR018943
Ost4 is a very short, approximately 30 residues, enzyme found from fungi to vertebrates. It is a member of the ER oligosaccaryltansferase complex, EC, that catalyses the asparagine-linked glycosylation of proteins. It appears to be an integral membrane protein that mediates the en bloc transfer of a pre-assembled high-mannose oligosaccharide onto asparagine residues of nascent polypeptides as they enter the lumen of the rough endoplasmic reticulum.
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 using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...
View options
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 (12) |
Full (156) |
Representative proteomes | NCBI (156) |
Meta (1) |
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| RP15 (28) |
RP35 (56) |
RP55 (83) |
RP75 (105) |
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| Jalview | ||||||||
| HTML | ||||||||
| PP/heatmap | 1 | |||||||
| Pfam viewer | ||||||||
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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Format an alignment
Download options
We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
| Seed (12) |
Full (156) |
Representative proteomes | NCBI (156) |
Meta (1) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (28) |
RP35 (56) |
RP55 (83) |
RP75 (105) |
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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.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.
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: | Wood V |
| Previous IDs: | none |
| Type: | Family |
| Author: | Wood V, Coggill P |
| Number in seed: | 12 |
| Number in full: | 156 |
| Average length of the domain: | 34.50 aa |
| Average identity of full alignment: | 44 % |
| Average coverage of the sequence by the domain: | 50.21 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 35 | ||||||||||||
| Family (HMM) version: | 4 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
Sunburst controls
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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 Ost4 domain has been found. There are 2 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 seqence.
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Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence