Summary: ADP-ribosyl cyclase
This is the Wikipedia entry entitled "BST1". More...
The Wikipedia text that you see displayed here is a download from Wikipedia. This means that the information we display is a copy of the information from the Wikipedia database. The button next to the article title ("Edit Wikipedia article") takes you to the edit page for the article directly within Wikipedia. You should be aware you are not editing our local copy of this information. Any changes that you make to the Wikipedia article will not be displayed here until we next download the article from Wikipedia. We currently download new content on a nightly basis.
Does Pfam agree with the content of the Wikipedia entry ?
Pfam has chosen to link families to Wikipedia articles. In some case we have created or edited these articles but in many other cases we have not made any direct contribution to the content of the article. The Wikipedia community does monitor edits to try to ensure that (a) the quality of article annotation increases, and (b) vandalism is very quickly dealt with. However, we would like to emphasise that Pfam does not curate the Wikipedia entries and we cannot guarantee the accuracy of the information on the Wikipedia page.
Editing Wikipedia articles
Before you edit for the first time
Wikipedia is a free, online encyclopedia. Although anyone can edit or contribute to an article, Wikipedia has some strong editing guidelines and policies, which promote the Wikipedia standard of style and etiquette. Your edits and contributions are more likely to be accepted (and remain) if they are in accordance with this policy.
You should take a few minutes to view the following pages:
How your contribution will be recorded
Anyone can edit a Wikipedia entry. You can do this either as a new user or you can register with Wikipedia and log on. When you click on the "Edit Wikipedia article" button, your browser will direct you to the edit page for this entry in Wikipedia. If you are a registered user and currently logged in, your changes will be recorded under your Wikipedia user name. However, if you are not a registered user or are not logged on, your changes will be logged under your computer's IP address. This has two main implications. Firstly, as a registered Wikipedia user your edits are more likely seen as valuable contribution (although all edits are open to community scrutiny regardless). Secondly, if you edit under an IP address you may be sharing this IP address with other users. If your IP address has previously been blocked (due to being flagged as a source of 'vandalism') your edits will also be blocked. You can find more information on this and creating a user account at Wikipedia.
If you have problems editing a particular page, contact us at email@example.com and we will try to help.
The community annotation is a new facility of the Pfam web site. If you have problems editing or experience problems with these pages please contact us.
|Bone marrow stromal cell antigen 1|
PDB rendering based on 1isf.
|RNA expression pattern|
Bone marrow stromal cell antigen-1 is a stromal cell line-derived glycosylphosphatidylinositol-anchored molecule that facilitates pre-B-cell growth. The deduced amino acid sequence exhibits 33% similarity with CD38. BST1 expression is enhanced in bone marrow stromal cell lines derived from patients with rheumatoid arthritis. The polyclonal B-cell abnormalities in rheumatoid arthritis may be, at least in part, attributed to BST1 overexpression in the stromal cell population.
- Kaisho T, Ishikawa J, Oritani K, Inazawa J, Tomizawa H, Muraoka O, Ochi T, Hirano T (Jul 1994). "BST-1, a surface molecule of bone marrow stromal cell lines that facilitates pre-B-cell growth". Proc Natl Acad Sci U S A 91 (12): 5325–9. doi:10.1073/pnas.91.12.5325. PMC 43987. PMID 8202488.
- "Entrez Gene: BST1 bone marrow stromal cell antigen 1".
- Ortolan E, Vacca P, Capobianco A, et al. (2003). "CD157, the Janus of CD38 but with a unique personality.". Cell Biochem. Funct. 20 (4): 309–22. doi:10.1002/cbf.978. PMID 12415565.
- Lee BO, Ishihara K, Denno K, et al. (1996). "Elevated levels of the soluble form of bone marrow stromal cell antigen 1 in the sera of patients with severe rheumatoid arthritis.". Arthritis Rheum. 39 (4): 629–37. doi:10.1002/art.1780390414. PMID 8630113.
- Kajimoto Y, Miyagawa J, Ishihara K, et al. (1996). "Pancreatic islet cells express BST-1, a CD38-like surface molecule having ADP-ribosyl cyclase activity.". Biochem. Biophys. Res. Commun. 219 (3): 941–6. doi:10.1006/bbrc.1996.0327. PMID 8645283.
- Okuyama Y, Ishihara K, Kimura N, et al. (1997). "Human BST-1 expressed on myeloid cells functions as a receptor molecule.". Biochem. Biophys. Res. Commun. 228 (3): 838–45. doi:10.1006/bbrc.1996.1741. PMID 8941363.
- Muraoka O, Tanaka H, Itoh M, et al. (1997). "Genomic structure of human BST-1.". Immunol. Lett. 54 (1): 1–4. doi:10.1016/S0165-2478(96)02633-8. PMID 9030974.
- Wimazal F, Ghannadan M, Müller MR, et al. (2000). "Expression of homing receptors and related molecules on human mast cells and basophils: a comparative analysis using multi-color flow cytometry and toluidine blue/immunofluorescence staining techniques.". Tissue Antigens 54 (5): 499–507. doi:10.1034/j.1399-0039.1999.540507.x. PMID 10599889.
- Yamamoto-Katayama S, Sato A, Ariyoshi M, et al. (2001). "Site-directed removal of N-glycosylation sites in BST-1/CD157: effects on molecular and functional heterogeneity.". Biochem. J. 357 (Pt 2): 385–92. doi:10.1042/0264-6021:3570385. PMC 1221964. PMID 11439087.
- Liang F, Qi RZ, Chang CF (2001). "Signalling of GPI-anchored CD157 via focal adhesion kinase in MCA102 fibroblasts.". FEBS Lett. 506 (3): 207–10. doi:10.1016/S0014-5793(01)02912-X. PMID 11602246.
- Yamamoto-Katayama S, Ariyoshi M, Ishihara K, et al. (2002). "Crystallographic studies on human BST-1/CD157 with ADP-ribosyl cyclase and NAD glycohydrolase activities.". J. Mol. Biol. 316 (3): 711–23. doi:10.1006/jmbi.2001.5386. PMID 11866528.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Funaro A, Ortolan E, Ferranti B, et al. (2005). "CD157 is an important mediator of neutrophil adhesion and migration.". Blood 104 (13): 4269–78. doi:10.1182/blood-2004-06-2129. PMID 15328157.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Hillier LW, Graves TA, Fulton RS, et al. (2005). "Generation and annotation of the DNA sequences of human chromosomes 2 and 4.". Nature 434 (7034): 724–31. doi:10.1038/nature03466. PMID 15815621.
- Liu T, Qian WJ, Gritsenko MA, et al. (2006). "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.". J. Proteome Res. 4 (6): 2070–80. doi:10.1021/pr0502065. PMC 1850943. PMID 16335952.
|This membrane protein–related article is a stub. You can help Wikipedia by expanding it.|
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.
ADP-ribosyl cyclase Provide feedback
ADP-ribosyl cyclase EC:126.96.36.199 (also know as cyclic ADP-ribose hydrolase or CD38) synthesises cyclic-ADP ribose, a second messenger for glucose-induced insulin secretion.
Prasad GS, McRee DE, Stura EA, Levitt DG, Lee HC, Stout CD; , Nat Struct Biol 1996;3:957-964.: Crystal structure of Aplysia ADP ribosyl cyclase, a homologue of the bifunctional ectozyme CD38. PUBMED:8901875 EPMC:8901875
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR003193
CD38, the HUGO gene name, is also called T10 or ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase (EC). CD38 is a novel enzyme capable of catalysing multiple reactions, including NAD glycohydrolase, ADP-ribosyl cyclase, cyclic ADP ribose hydrolase and base-exchange activities. Two of the enzymatic products, cyclic ADP-ribose (cADPR) and nicotinic acid adenine dinucleotide phosphate (NAADP), are calcium messengers in a wide variety of cells from protist, plant, and mammal to human. CD38 is a positive and negative regulator of cell activation and proliferation, depending on the cellular environment. It is involved in adhesion between human lymphocytes and endothelial cells and is involved in the metabolism of two calcium messengers, cADPR and NAADP.
CD157 (also called BP-3/IF-7, BST-1 or Mo5) has ADP-ribosyl cyclase and cyclic ADP-ribose hydrolase activities. CD157 supports the growth of a pre-B cell line, DW34. Anti-CD157 mAb IF-7 has synergistic effects on anti-CD3-induced growth of T progenitor cells, and facilitates the development of [alpha][beta] TCR+ cells in foetal thymic organ culture system.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||NAD+ nucleosidase activity (GO:0003953)|
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- the UniProt description of the protein sequence
- the number of residues in the sequence
- the Pfam graphic itself.
Loading domain graphics...
This superfamily includes the N-deoxyribosyltransferase and ADP-ribosyl cyclase-like families as well as the family that includes the hypothetical protein PA1492 for which the structure is known. PA1942 has a very similar putative active site and is predicted by SCOP to have a deoxyribosyltransferase activity .
The clan contains the following 4 members:DUF1937 DUF4406 Nuc_deoxyrib_tr Rib_hydrolayse
We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
- the alignment generated by searching the sequence database using the HMM
- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
- alignment generated by searching the NCBI sequence database using the family HMM
- alignment generated by searching the metagenomics sequence database using the family HMM
You can see the alignments as HTML or in three different sequence viewers:
- Pfam viewer
- an HTML-based viewer that uses DAS to retrieve alignment fragments on request
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
Format an alignment
If you find these logos useful in your own work, please consider citing the following article:
Note: You can also download the data file for the tree.
Curation and family details
|Seed source:||Pfam-B_3719 (release 5.2)|
|Author:||Bateman A, Mian N|
|Number in seed:||12|
|Number in full:||149|
|Average length of the domain:||212.20 aa|
|Average identity of full alignment:||38 %|
|Average coverage of the sequence by the domain:||81.23 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||12|
|Download:||download the raw HMM for this family|
Weight segments by...
Change the size of the sunburst
selected sequences to HMM
a FASTA-format file
- 0 sequences
- 0 species
How the sunburst is generated
Colouring and labels
Anomalies in the taxonomy tree
Missing taxonomic levels
Unmapped species names
Too many species/sequences
The tree shows the occurrence of this domain across different species. More...
You can use the tree controls to manipulate how the interactive tree is displayed:
- show/hide the summary boxes
- highlight species that are represented in the seed alignment
- expand/collapse the tree or expand it to a given depth
- select a sub-tree or a set of species within the tree and view them graphically or as an alignment
- save a plain text representation of the tree
There is 1 interaction for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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 Rib_hydrolayse domain has been found. There are 156 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...