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194  structures 139  species 1  interaction 318  sequences 5  architectures

Family: Rib_hydrolayse (PF02267)

Summary: ADP-ribosyl cyclase

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This is the Wikipedia entry entitled "BST1". More...

BST1 Edit Wikipedia article

Protein BST1 PDB 1isf.png
Available structures
PDB Ortholog search: PDBe RCSB
Aliases BST1, CD157, bone marrow stromal cell antigen 1
External IDs MGI: 105370 HomoloGene: 3198 GeneCards: BST1
Gene location (Human)
Chromosome 4 (human)
Chr. Chromosome 4 (human)[1]
Chromosome 4 (human)
Genomic location for BST1
Genomic location for BST1
Band No data available Start 15,702,950 bp[1]
End 15,738,313 bp[1]
RNA expression pattern
PBB GE BST1 205715 at fs.png
More reference expression data
Species Human Mouse
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC) Chr 4: 15.7 – 15.74 Mb Chr 4: 43.82 – 43.84 Mb
PubMed search [3] [4]
View/Edit Human View/Edit Mouse

ADP-ribosyl cyclase 2 is an enzyme that in humans is encoded by the BST1 gene.[5][6]

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.[6]

See also


External links

Further reading

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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.

ADP-ribosyl cyclase Provide feedback

ADP-ribosyl cyclase EC: (also know as cyclic ADP-ribose hydrolase or CD38) synthesises cyclic-ADP ribose, a second messenger for glucose-induced insulin secretion.

Literature references

  1. 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.

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

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

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Pfam Clan

This family is a member of clan Nribosyltransf (CL0498), which has the following description:

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 [1].

The clan contains the following 6 members:

DUF1937 DUF4406 Nuc_deoxyri_tr2 Nuc_deoxyri_tr3 Nuc_deoxyrib_tr Rib_hydrolayse


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...

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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...


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.

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Curation and family details

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Seed source: Pfam-B_3719 (release 5.2)
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Bateman A , Mian N
Number in seed: 36
Number in full: 318
Average length of the domain: 196.50 aa
Average identity of full alignment: 35 %
Average coverage of the sequence by the domain: 77.92 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 45638612 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 25.0 25.0
Trusted cut-off 25.0 25.6
Noise cut-off 23.8 24.1
Model length: 241
Family (HMM) version: 17
Download: download the raw HMM for this family

Species distribution

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



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 194 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 sequence.

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