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156  structures 48  species 1  interaction 149  sequences 3  architectures

Family: Rib_hydrolayse (PF02267)

Summary: ADP-ribosyl cyclase

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 "BST1". More...

BST1 Edit Wikipedia article

Bone marrow stromal cell antigen 1

PDB rendering based on 1isf.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols BST1; CD157
External IDs OMIM600387 MGI105370 HomoloGene3198 GeneCards: BST1 Gene
EC number 3.2.2.5
RNA expression pattern
PBB GE BST1 205715 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 683 12182
Ensembl ENSG00000109743 ENSMUSG00000029082
UniProt Q10588 Q64277
RefSeq (mRNA) NM_004334 NM_009763
RefSeq (protein) NP_004325 NP_033893
Location (UCSC) Chr 4:
15.7 – 15.74 Mb
Chr 5:
43.82 – 43.84 Mb
PubMed search [1] [2]

ADP-ribosyl cyclase 2 is an enzyme that in humans is encoded by the BST1 gene.[1][2]

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.[2]

See also[edit]

References[edit]

  1. ^ 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. 
  2. ^ a b "Entrez Gene: BST1 bone marrow stromal cell antigen 1". 

Further reading[edit]

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:3.2.2.5 (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 contains the following 4 members:

DUF1937 DUF4406 Nuc_deoxyrib_tr Rib_hydrolayse

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...

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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
(12)
Full
(149)
Representative proteomes NCBI
(136)
Meta
(0)
RP15
(22)
RP35
(23)
RP55
(41)
RP75
(78)
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available

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

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  Seed
(12)
Full
(149)
Representative proteomes NCBI
(136)
Meta
(0)
RP15
(22)
RP35
(23)
RP55
(41)
RP75
(78)
Alignment:
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Sequence:
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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
(12)
Full
(149)
Representative proteomes NCBI
(136)
Meta
(0)
RP15
(22)
RP35
(23)
RP55
(41)
RP75
(78)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download    
Gzipped 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

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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.

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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: Pfam-B_3719 (release 5.2)
Previous IDs: none
Type: Domain
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 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 25.0 25.0
Trusted cut-off 45.7 37.2
Noise cut-off 19.6 18.8
Model length: 243
Family (HMM) version: 12
Download: download the raw HMM for this family

Species distribution

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Interactions

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

Rib_hydrolayse

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 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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