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.
24  structures 780  species 1  interaction 5768  sequences 137  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

The oxysterol-binding protein (OSBP)-related proteins (ORPs) are a family of lipid transfer proteins (LTPs). Concretely, they constitute a family of sterol and phosphoinositide binding and transfer proteins in eukaryotes[2] that are conserved from yeast to humans. They are lipid-binding proteins implicated in many cellular processes related with oxysterol, including signaling, vesicular trafficking, lipid metabolism, and nonvesicular sterol transport.

In yeast cells, it is probable that ORPs function as sterol transporters, perhaps in regions where organelle membranes are closely apposed. Various ORPs confine at membrane contacts sites (MCS), where endoplasmic reticulum (ER) is apposed with other organelle limiting membranes. Yeast ORPs also participate in vesicular trafficking, although their role is unclear. In mammalian cells, some ORPs function as sterol sensors that regulate the assembly of protein complexes in response to changes in cholesterol levels.[3] By that means, ORPs most likely affect organelle membrane lipid compositions, with impacts on signaling and vesicle transport, but also cellular lipid metabolism.[4]

Oxysterol is a cholesterol metabolite that can be produced through enzymatic or radical processes. Oxysterols, that are the 27-carbon products of cholesterol oxidation by both enzymic and non-enzymic mechanisms, constitute a large family of lipids involved in a plethora of physiological processes. Studies identifying the specific cellular targets of oxysterol indicate that several oxysterols may be regulators of cellular lipid metabolism via control of gene transcription. In addition, they were shown to be involved in other processes such as immune regulatory functions and brain homeostasis.[5][6]

Structure

Domain organization of the oxysterol-binding protein (OSBP)-related proteins (ORPs) from humans.

All oxysterol related proteins (ORP) contain a core lipid-binding domain (ORD), which has a characteristic amino acids sequence, EQVSHHPP. The most studied ORP are human and yeast ones, and the only OSBP-ORP whose structure is completely known is the Kes1p, also called Osh4p, a yeast one. Six different protein domains and structural motifs types are found in OSBP-ORPs.[7]

Domain organization of the oxysterol-binding protein (OSBP)-related proteins (ORPs) from S.cervisiae.
Legend of OSBP-ORPs Domain Structure

FFAT motif

This is two phenylalanines in an acidic tract. It is bound by the endoplasmic reticulum to a lot of proteins involved in lipid metabolism. It is contained in most mammalian ORPs and in about 40% of yeast's ORPs.

Ankyrin motif

It is thought that it takes part in protein-protein interactions, but it is not known for certain. In some proteins, it also contributes to the localization of each protein to a membrane contact site (zone of close contact between the endoplasmic reticulum and a second organelle).

Transmembrane domain

It is only present in some human proteins. It is an hydrophobic region which holds the protein to the cell membrane.

PH (pleckstrin homology) domain

It binds phosphoinositides, usually only the ones which have low affinity and other ligands. It also recognizes organelles enriched in the PIPs.

GOLD (Golgi dynamics) domain

As well as Ankyrin motif, it probably mediates interactions between proteins. It is only found in one yeast protein and it is not found in any human ORP.

ORD (OSBP-related domain)

It contains the EQVSHHPP sequence. It has an hydrophobic pocket that binds a sterol and also contains multiple membrane binding surfaces which permit the protein to have the ability to cause liposome aggregation.

Main functions

Lipids movement between cellular membranes.

As part of the Lipid Transfer proteins (LTPs) family, ORPs have different and variate functions. This functions include signaling, vesicular trafficking, lipid metabolism and nonvesicular sterol transport.[8] ORPs have been studied in many organisms cells as human cells or yeast. In yeast, where organelle membranes are closely apposed ORPs work as sterol transporters. They are also part of vesicular trafficking but their role is not clear yet. In mammalian, ORPs participate as sterol sensors.This sensors regulate the assembly of protein complexes when cholesterol levels fluctuate.[9]

OSBP-ORPs help stablish the membrane when transient changes in the distribution of lipids occur.
They could function as lipid sensors that alter their interactions with other proteins in response to binding or releasing lipid ligands.
ORPs could regulate the access of other lipid-binding proteins to the membrane by presenting a lipid to a second lipid-binding protein.
ORPs could regulate the access of other lipid-binding proteins to the membrane by preventing the lipid-binding protein from accessing a lipid in the membrane.

They use the following mechanisms:

1-They could extract and deliver lipids from one membrane to another. Probably at membrane contact site.

2-ORPs help establish the membrane when transient changes in the distribution of lipids occur. They add or remove lipids within different regions of the membrane. The exclusion of certain lipids in particular regions drive to processes such as membrane binding or signaling.

3-They work as lipid sensors altering interactions with other proteins due to binding or releasing lipid ligands. It occurs mainly at inally organelle contact sites.

4-The access of other lipid-binding proteins to the membrane is regulated by ORPs in two ways. One way is by presenting a lipid to a second lipid-binding protein. (5)Another way is preventing the lipid-binding protein from accessing a lipid in the membrane. This two mechanisms are not mutually exclusive so ORPs might use both.

OSBP-ORPs human proteins

In humans there are 12 ORP genes, and splicing generates 16 different protein products.[10][11] [12]

Symbol Name Length (aa) Chromosome Molecular function
OSBP [13]

(OSBP1)

Oxysterol-binding protein 1 807 11q12.1
  • oxysterol binding
  • phosphatidylinositol-4-phosphate binding
  • protein domain specific binding
  • sterol transporter activity
OSBP2 [14]

(KIAA1664, ORP-4, ORP4)

Oxysterol-binding protein 2 916 22q12.2
  • cholesterol binding
OSBPL1A [15]

(ORP-1, ORP1)

Oxysterol-binding protein-related protein 1 950 18q11.2
  • cholesterol binding
  • phospholipid binding
OSBPL2 [16]

"(KIAA0772, ORP2)" [17]

Oxysterol-binding protein-related protein 2 480 20q13.33
  • choresterol binding
OSBPL3 [18]

(ORP-3, ORP3, KIAA0704)

Oxysterol-binding protein-related protein 3 887 7p15.3
  • choresterol binding
OSBPL5 [19]

(KIAA1534, ORP5)

Oxysterol-binding protein-related protein 5 879 11p15.4
  • choresterol binding
  • oxysterol binding
  • phosphatidylinositol-4-phosphate binding
  • phosphatidylserine binding
  • phospholipid transporter activity
OSBPL6 [20]

(ORP6)

Oxysterol-binding protein-related protein 6 934 2q31.2
  • lipid binding
OSBPL7 [21]

(ORP7, MGC71150)

Oxysterol-binding protein-related protein 7 842 17q21
  • choresterol binding
OSBPL8 [22]

(OSBP10, ORP8, MST120, MSTP120)

Oxysterol-binding protein-related protein 8 889 12q14
  • cholesterol binding
  • phosphatidylinositol-4-phosphate binding
  • phosphatidylserine binding
  • phospholipid transporter activity
OSBPL9 [23]

(ORP9, OSBP4)

Oxysterol-binding protein-related protein 9 736 1p32.3
  • lipid binding
OSBPL10 [24]

(ORP10, OSBP9)

Oxysterol-binding protein-related protein 10 764 3p23
  • cholesterol binding
  • phosphatidylserine binding
OSBPL11 [25]

(ORP-11, ORP11, FLJ13012, FLJ13164)

Oxysterol-binding protein-related protein 11 747 3q21.2
  • lipid binding

OSBP-ORPs yeast proteins

In yeast (Saccharomyces cerevisiæ) we can find 7 ORP genes called OSH1-7, but they have some additional names as well.[26][27]

Symbol Name Length (aa) Molecular function Subcellular location
OSH1 [28]

(SWH1, YAR042W, YAR044W)

Oxysterol-binding protein homolog 1 1188
  • 1-phosphatidylinositol binding
  • lipid binding
  • oxysterol binding
  • sterol transporter activity
  • Cytoplasm
  • Golgi apparatus membrane
  • Nucleus outer membrane
OSH2 [29]

(YDL019C, D2845)

Oxysterol-binding protein homolog 2 1283
  • 1-phosphatidylinositol binding
  • lipid binding
  • oxysterol binding
  • sterol transporter activity
  • Cell membrane
OSH3 [30]

(YHR073W)

Oxysterol-binding protein homolog 3 996
  • 1-phosphatidylinositol binding
  • lipid binding
  • oxysterol binding
  • sterol transporter activity
  • Cytoplasm
OSH4 [31]

(KES1, YPL145C, LPI3C, P2614)

Oxysterol-binding protein homolog 4 434
  • lipid binding
  • oxysterol binding
  • phosphatidic acid binding
  • phosphatidylinositol-4,5-bisphosphate binding
  • phosphatidylinositol-4-phosphate binding
  • sterol transporter activity
  • Golgi apparatus membrane
OSH5 [32]

(HES1, YOR237W, O5234)

Oxysterol-binding protein homolog 5 434
  • lipid binding
  • oxysterol binding
  • sterol transporter activity
-
OSH6 [33]

(YKR003W, YK102)

Oxysterol-binding protein homolog 6 448
  • lipid binding
  • oxysterol binding
  • phosphatidic acid binding
  • phosphatidylinositol-3,4-bisphosphate binding
  • phosphatidylinositol-3,5-bisphosphate binding
  • phosphatidylinositol-4-phosphate binding
  • phosphatidylinositol-5-phosphate binding
  • phosphatidylserine binding
  • phospholipid transporter activity
  • Endoplasmic reticulum membrane
OSH7 [34]

(YHR001W)

Oxysterol-binding protein homolog 7 437
  • lipid binding
  • oxysterol binding
  • phosphatidylinositol-4-phosphate binding
  • phosphatidylserine binding
  • phospholipid transporter activity
  • Endoplasmic reticulum membrane

Role in disease

Some oxysterols have been found to contribute to the inflammation and oxidative damage as well as in cell death in the appearance and especially the development of some of the most important chronic diseases, such as atherosclerosis, neurodegenerative diseases, inflammatory bowel diseases, age-related macular degeneration and other pathological conditions related to cholesterol absorption.[35]

Besides, a recent study suggests a method of screening and diagnosing Niemann-Pick C disease by plasma oxysterol screening, which is found to be less invasive, more sensitive and specific and more economical strategy than the current practice.[36]

References

  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 1431608Freely accessible. 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. ^ Weber-Boyvat, Marion; Zhong, Wenbin; Yan, Daoguang; Olkkonen, Vesa M. (1 July 2013). "Oxysterol-binding proteins: functions in cell regulation beyond lipid metabolism". Biochemical Pharmacology. 86: 89–95. doi:10.1016/j.bcp.2013.02.016. PMID 23428468. 
  3. ^ Raychaudhuri, Sumana; Prinz, William A. (10 November 2010). "The Diverse Functions of Oxysterol-Binding Proteins". Annual review of cell and developmental biology. 26: 157–177. doi:10.1146/annurev.cellbio.042308.113334. PMC 3478074Freely accessible. PMID 19575662. 
  4. ^ Weber-Boyvat, Marion; Zhong, Wenbin; Yan, Daoguang; Olkkonen, Vesa M. (1 July 2013). "Oxysterol-binding proteins: functions in cell regulation beyond lipid metabolism". Biochemical Pharmacology. 86: 89–95. doi:10.1016/j.bcp.2013.02.016. PMID 23428468. 
  5. ^ Mutemberezi, Valentin; Guillemot-Legris, Owein; Muccioli, Giulio G. (26 September 2016). "Oxysterols: From cholesterol metabolites to key mediators". Progress in Lipid Research. 64: 152–169. doi:10.1016/j.plipres.2016.09.002. PMID 27687912. 
  6. ^ van Reyk, David M.; Brown, Andrew J.; Hult'en, Lillemor Mattsson; Dean, Roger T.; Jessup, Wendy (1 January 2006). "Oxysterols in biological systems: sources, metabolism and pathophysiological relevance". Redox Report: Communications in Free Radical Research. 11: 255–262. doi:10.1179/135100006X155003. PMID 17207307. 
  7. ^ Raychaudhuri, Sumana; Prinz, William A. (10 November 2010). "The Diverse Functions of Oxysterol-Binding Proteins". Annual review of cell and developmental biology. 26: 157–177. doi:10.1146/annurev.cellbio.042308.113334. PMC 3478074Freely accessible. PMID 19575662. 
  8. ^ Ngo, Mike; Ridgway, Neale D. (1 March 2009). "Oxysterol binding protein-related Protein 9 (ORP9) is a cholesterol transfer protein that regulates Golgi structure and function". Molecular Biology of the Cell. 20: 1388–1399. doi:10.1091/mbc.E08-09-0905. PMC 2649274Freely accessible. PMID 19129476. 
  9. ^ Raychaudhuri, Sumana; Prinz, William A. (10 November 2010). "The Diverse Functions of Oxysterol-Binding Proteins". Annual review of cell and developmental biology. 26: 157–177. doi:10.1146/annurev.cellbio.042308.113334. PMC 3478074Freely accessible. PMID 19575662. 
  10. ^ Lehto, M.; Laitinen, S.; Chinetti, G.; Johansson, M.; Ehnholm, C.; Staels, B.; Ikonen, E.; Olkkonen, V. M. (1 August 2001). "The OSBP-related protein family in humans". Journal of Lipid Research. 42: 1203–1213. PMID 11483621. 
  11. ^ "Oxysterol binding proteins (OSBP) Gene Family | HUGO Gene Nomenclature Committee". www.genenames.org. Retrieved 11 October 2016. 
  12. ^ ""oxysterol binding" proteins in UniProtKB". www.uniprot.org. Retrieved 11 October 2016. 
  13. ^ "OSBP - Oxysterol-binding protein 1 - Homo sapiens (Human) - OSBP gene & protein". www.uniprot.org. 
  14. ^ "OSBP2 - Oxysterol-binding protein 2 - Homo sapiens (Human) - OSBP2 gene & protein". www.uniprot.org. 
  15. ^ "OSBPL1A - Oxysterol-binding protein-related protein 1 - Homo sapiens (Human) - OSBPL1A gene & protein". www.uniprot.org. 
  16. ^ "OSBPL2 - Oxysterol-binding protein-related protein 2 - Homo sapiens (Human) - OSBPL2 gene & protein". www.uniprot.org. 
  17. ^ Escajadillo, Tamara; Wang, Hongxia; Li, Linda; Li, Donghui; Sewer, Marion B. (15 May 2016). "Oxysterol-related-binding-protein related Protein-2 (ORP2) regulates cortisol biosynthesis and cholesterol homeostasis". Molecular and Cellular Endocrinology. 427: 73–85. doi:10.1016/j.mce.2016.03.006. PMC 4833515Freely accessible. PMID 26992564. 
  18. ^ "OSBPL3 - Oxysterol-binding protein-related protein 3 - Homo sapiens (Human) - OSBPL3 gene & protein". www.uniprot.org. 
  19. ^ "OSBPL5 - Oxysterol-binding protein-related protein 5 - Homo sapiens (Human) - OSBPL5 gene & protein". www.uniprot.org. 
  20. ^ "OSBPL6 - Oxysterol-binding protein-related protein 6 - Homo sapiens (Human) - OSBPL6 gene & protein". www.uniprot.org. 
  21. ^ "OSBPL7 - Oxysterol-binding protein-related protein 7 - Homo sapiens (Human) - OSBPL7 gene & protein". www.uniprot.org. 
  22. ^ "OSBPL8 - Oxysterol-binding protein-related protein 8 - Homo sapiens (Human) - OSBPL8 gene & protein". www.uniprot.org. 
  23. ^ "OSBPL9 - Oxysterol-binding protein-related protein 9 - Homo sapiens (Human) - OSBPL9 gene & protein". www.uniprot.org. 
  24. ^ "OSBPL10 - Oxysterol-binding protein-related protein 10 - Homo sapiens (Human) - OSBPL10 gene & protein". www.uniprot.org. 
  25. ^ "OSBPL11 - Oxysterol-binding protein-related protein 11 - Homo sapiens (Human) - OSBPL11 gene & protein". www.uniprot.org. 
  26. ^ Beh, C. T.; Cool, L.; Phillips, J.; Rine, J.; Ehnholm, C.; Staels, B.; Ikonen, E.; Olkkonen, V. M. (1 March 2001). "Overlapping functions of the yeast oxysterol-binding protein homologues". Genetics. 157: 1117–1140. PMC 1461579Freely accessible. PMID 11238399. 
  27. ^ ""oxysterol binding" proteins in UniProtKB". www.uniprot.org. Retrieved 17 October 2016. 
  28. ^ "SWH1 - Oxysterol-binding protein homolog 1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) - SWH1 gene & protein". www.uniprot.org. 
  29. ^ "OSH2 - Oxysterol-binding protein homolog 2 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) - OSH2 gene & protein". www.uniprot.org. 
  30. ^ "OSH3 - Oxysterol-binding protein homolog 3 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) - OSH3 gene & protein". www.uniprot.org. 
  31. ^ "KES1 - Oxysterol-binding protein homolog 4 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) - KES1 gene & protein". www.uniprot.org. 
  32. ^ "HES1 - Protein HES1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) - HES1 gene & protein". www.uniprot.org. 
  33. ^ "OSH6 - Oxysterol-binding protein homolog 6 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) - OSH6 gene & protein". www.uniprot.org. 
  34. ^ "OSH7 - Oxysterol-binding protein homolog 7 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) - OSH7 gene & protein". www.uniprot.org. 
  35. ^ Poli, Giuseppe; Biasi, Fiorella; Leonarduzzi, Gabriella (31 January 2013). "Oxysterols in the pathogenesis of major chronic diseases". Redox Biology. 1: 125–130. doi:10.1016/j.redox.2012.12.001. PMC 3757713Freely accessible. PMID 24024145. 
  36. ^ van Karnebeek, Clara D.M.; Mohammadi, Tima; Tsao, Nicole; Sinclair, Graham; Sirrs, Sandra; Stockler, Sylvia; Marra, Carlo (1 July 2014). "Health economic evaluation of plasma oxysterol screening in the diagnosis of Niemann–Pick Type C disease among intellectually disabled using discrete event simulation". Molecular Genetics and Metabolism. pp. 226–232. doi:10.1016/j.ymgme.2014.07.004. 

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 (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...

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
(407)
Full
(5768)
Representative proteomes UniProt
(8602)
NCBI
(15093)
Meta
(5)
RP15
(1322)
RP35
(2894)
RP55
(4341)
RP75
(5417)
Jalview View  View  View  View  View  View  View  View  View 
HTML View                 
PP/heatmap 1                

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

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

Format an alignment

  Seed
(407)
Full
(5768)
Representative proteomes UniProt
(8602)
NCBI
(15093)
Meta
(5)
RP15
(1322)
RP35
(2894)
RP55
(4341)
RP75
(5417)
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
(407)
Full
(5768)
Representative proteomes UniProt
(8602)
NCBI
(15093)
Meta
(5)
RP15
(1322)
RP35
(2894)
RP55
(4341)
RP75
(5417)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   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.

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: 407
Number in full: 5768
Average length of the domain: 309.70 aa
Average identity of full alignment: 27 %
Average coverage of the sequence by the domain: 50.42 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 26740544 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 28.9 28.9
Trusted cut-off 29.2 28.9
Noise cut-off 28.6 28.8
Model length: 373
Family (HMM) version: 17
Download: download the raw HMM for this family

Species distribution

Sunburst controls

Hide

Weight segments by...


Change the size of the sunburst

Small
Large

Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence

Selections

Align selected sequences to HMM

Generate a FASTA-format file

Clear selection

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.

Interactions

There is 1 interaction for this family. More...

Oxysterol_BP

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 24 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...