Summary: Uso1 / p115 like vesicle tethering protein, head region
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Uso1 / p115 like vesicle tethering protein, head region Provide feedback
Also known as General vesicular transport factor, Transcytosis associated protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerisation, and a short C-terminal acidic region [1]. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of part of the head region. The head region is highly conserved, but its function is unknown. It does not seem to be essential for vesicle tethering [1]. The N-terminal part of the head region, not within this family, contains context-detected Armadillo/beta-catenin-like repeats (PF00514).
Literature references
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Shorter J, Beard MB, Seemann J, Dirac-Svejstrup AB, Warren G; , J Cell Biol 2002;157:45-62.: Sequential tethering of Golgins and catalysis of SNAREpin assembly by the vesicle-tethering protein p115. PUBMED:11927603 EPMC:11927603
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Whyte JR, Munro S; , J Cell Sci 2002;115:2627-2637.: Vesicle tethering complexes in membrane traffic. PUBMED:12077354 EPMC:12077354
External database links
| PANDIT: | PF04869 |
| Pseudofam: | PF04869 |
| SYSTERS: | Uso1_p115_head |
This tab holds annotation information from the InterPro database.
InterPro entry IPR006953
This domain identifies a group of proteins, which are described as: General vesicular transport factor, Transcytosis associated protein (TAP) or Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerisation, and a short C-terminal acidic region [PUBMED:11927603]. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the Golgi stack. This domain is found in the head region. The head region is highly conserved, but its function is unknown. It does not seem to be essential for vesicle tethering [PUBMED:11927603]. The N-terminal part of the head region contains context-detected Armadillo/beta-catenin-like repeats.Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Cellular component | cytoplasm (GO:0005737) |
| Golgi membrane (GO:0000139) | |
| Biological process | intracellular protein transport (GO:0006886) |
| vesicle fusion with Golgi apparatus (GO:0048280) |
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
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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 (26) |
Full (295) |
Representative proteomes | NCBI (303) |
Meta (1) |
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| RP15 (68) |
RP35 (111) |
RP55 (170) |
RP75 (205) |
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| PP/heatmap | 1 | |||||||
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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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 (26) |
Full (295) |
Representative proteomes | NCBI (303) |
Meta (1) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (68) |
RP35 (111) |
RP55 (170) |
RP75 (205) |
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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: | Pfam-B_6073 (release 7.6) |
| Previous IDs: | none |
| Type: | Family |
| Author: | Kerrison ND |
| Number in seed: | 26 |
| Number in full: | 295 |
| Average length of the domain: | 289.20 aa |
| Average identity of full alignment: | 30 % |
| Average coverage of the sequence by the domain: | 29.08 % |
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: | 312 | ||||||||||||
| Family (HMM) version: | 9 | ||||||||||||
| 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 Uso1_p115_head domain has been found. There are 4 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