Summary: ADP-ribosyl cyclase
This is the Wikipedia entry entitled "BST1". More...
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|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.
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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:220.127.116.11 (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
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This example describes an architecture with one
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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:
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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|
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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.
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