Please note: this site relies heavily on the use of javascript. Without a javascript-enabled browser, this site will not function correctly. Please enable javascript and reload the page, or switch to a different browser.
10  structures 312  species 0  interactions 2468  sequences 56  architectures

Family: Oxysterol_BP (PF01237)

Summary: Oxysterol-binding protein

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "Oxysterol-binding protein". More...

Oxysterol-binding protein Edit Wikipedia article

Oxysterol-binding protein
1ZHT.png
Crystallographic structure of the oxysterol-binding protein (rainbow color cartoon, N-terminus = blue, C-terminus = red) bound to 7-hydroxycholesterol (stick diagram, carbon = white, oxygen = red).[1]
Identifiers
Symbol Oxysterol_BP
Pfam PF01237
InterPro IPR000648
PROSITE PDOC00774
OPM superfamily 173
OPM protein 1zi7

Oxysterol-binding proteins, or Oxysterol-binding protein related-proteins, or simply ORPs, are evolutionary related proteins involved in sterol synthesis and/or its regulation.[2] These include mammalian oxysterol-binding protein (OSBP), a protein of about 800 amino-acid residues that binds oxysterols (oxygenated derivatives of cholesterol), cholesterol and phosphatidylinositol 4-phosphate (PI4P); yeast Osh1, a protein of 859 residues that plays a role in ergosterol synthesis; and yeast proteins HES1 and KES1, highly related proteins of 434 residues that seem to play a role in ergosterol synthesis[3]

References[edit]

  1. ^ Im, Y. J.; Raychaudhuri, S.; Prinz, W. A.; Hurley, J. H. (2005). "Structural mechanism for sterol sensing and transport by OSBP-related proteins". Nature 437 (7055): 154–158. doi:10.1038/nature03923. PMC 1431608. PMID 16136145.  PDB 1ZHT; Im, Y. J.; Raychaudhuri, S.; Prinz, W. A.; Hurley, J. H. (2005). Structure of yeast oxysterol binding protein Osh4 in complex with 7-hydroxycholesterol. doi:10.2210/pdb1zht/pdb. 
  2. ^ Jiang, B.; Brown, J. L.; Sheraton, J.; Fortin, N.; Bussey, H. (1994). "A new family of yeast genes implicated in ergosterol synthesis is related to the human oxysterol binding protein". Yeast 10 (3): 341–353. doi:10.1002/yea.320100307. PMID 8017104. 
  3. ^ Li, X.; Rivas, M. P.; Fang, M.; Marchena, J.; Mehrotra, B.; Chaudhary, A.; Feng, L.; Prestwich, G. D.; Bankaitis, V. A. (2002). "Analysis of oxysterol binding protein homologue Kes1p function in regulation of Sec14p-dependent protein transport from the yeast Golgi complex". The Journal of Cell Biology 157 (1): 63–77. doi:10.1083/jcb.200201037. PMC 2173257. PMID 11916983. 

Human proteins from this family[edit]

OBPH1; OSBP; OSBP2; OSBPL10; OSBPL11; OSBPL1A; OSBPL2; OSBPL3; OSBPL5; OSBPL6; OSBPL7; OSBPL8; OSBPL9;

This article incorporates text from the public domain Pfam and InterPro IPR000648


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.

Oxysterol-binding protein Provide feedback

No Pfam abstract.

Literature references

  1. Li X, Rivas MP, Fang M, Marchena J, Mehrotra B, Chaudhary A, Feng L, Prestwich GD, Bankaitis VA; , J Cell Biol 2002;157:63-77.: Analysis of oxysterol binding protein homologue Kes1p function in regulation of Sec14p-dependent protein transport from the yeast Golgi complex. PUBMED:11916983 EPMC:11916983


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR000648

A number of eukaryotic proteins that seem to be involved with sterol synthesis and/or its regulation have been found [PUBMED:8017104] to be evolutionary related. These include mammalian oxysterol-binding protein (OSBP), a protein of about 800 amino-acid residues that binds a variety of oxysterols (oxygenated derivatives of cholesterol); yeast OSH1, a protein of 859 residues that also plays a role in ergosterol synthesis; yeast proteins HES1 and KES1, highly related proteins of 434 residues that seem to play a role in ergosterol synthesis; and yeast hypothetical proteins YHR001w, YHR073w and YKR003w.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

Loading domain graphics...

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
(149)
Full
(2468)
Representative proteomes NCBI
(2357)
Meta
(5)
RP15
(500)
RP35
(792)
RP55
(1157)
RP75
(1498)
Jalview View  View  View  View  View  View  View  View 
HTML View  View  View  View  View  View     
PP/heatmap 1 View  View  View  View  View     
Pfam viewer View  View             

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(149)
Full
(2468)
Representative proteomes NCBI
(2357)
Meta
(5)
RP15
(500)
RP35
(792)
RP55
(1157)
RP75
(1498)
Alignment:
Format:
Order:
Sequence:
Gaps:
Download/view:

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
(149)
Full
(2468)
Representative proteomes NCBI
(2357)
Meta
(5)
RP15
(500)
RP35
(792)
RP55
(1157)
RP75
(1498)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download  

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.

Pfam alignments:

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 View help on the curation process

Seed source: Prosite
Previous IDs: none
Type: Family
Author: Finn RD, Bateman A
Number in seed: 149
Number in full: 2468
Average length of the domain: 330.10 aa
Average identity of full alignment: 27 %
Average coverage of the sequence by the domain: 52.43 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 25.4 25.4
Trusted cut-off 25.4 25.5
Noise cut-off 25.3 25.3
Model length: 354
Family (HMM) version: 13
Download: download the raw HMM for this family

Species distribution

Sunburst controls

Show

This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

Loading sunburst data...

Tree controls

Hide

The tree shows the occurrence of this domain across different species. More...

Loading...

Please note: for large trees this can take some time. While the tree is loading, you can safely switch away from this tab but if you browse away from the family page entirely, the tree will not be loaded.

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 Oxysterol_BP domain has been found. There are 10 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.

Loading structure mapping...