Reviewed, UniProtKB/Swiss-Prot Q10588 (BST1_HUMAN)

Names and origin

Protein names

Recommended name:
    ADP-ribosyl cyclase 2
    EC=3.2.2.5
Alternative name(s):
    Cyclic ADP-ribose hydrolase 2
      Short name=cADPr hydrolase 2
    Bone marrow stromal antigen 1
      Short name=BST-1
    CD_antigen=CD157

Gene names

Name:

BST1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	318 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Synthesizes cyclic ADP-ribose, a second messenger that elicits calcium release from intracellular stores. May be involved in pre-B-cell growth.
Catalytic activity	NAD+ + H2O = ADP-ribose + nicotinamide.
Subunit structure	Homodimer.
Subcellular location	Cell membrane; Lipid-anchor › GPI-anchor.
Tissue specificity	Widely expressed.
Involvement in disease	Rheumatoid arthritis (RA) patients show enhanced expression of BST-1 transcripts in bone marrow stromal cell lines. This suggests that BST-1 overexpression may play a role in B-cell abnormalities in RA.
Sequence similarities	Belongs to the ADP-ribosyl cyclase family.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Coding sequence diversity	Polymorphism
Domain	Signal
Ligand	NAD
Molecular function	Hydrolase
PTM	Disulfide bond GPI-anchor Glycoprotein Lipoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	humoral immune response Ref.1 Traceable author statement. Source: ProtInc metabolic process Inferred from electronic annotation. Source: InterPro multicellular organismal development Ref.1 Traceable author statement. Source: ProtInc
Cellular component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-KW extrinsic to membrane Ref.1 Traceable author statement. Source: ProtInc plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	NAD+ nucleosidase activity Inferred from electronic annotation. Source: EC binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 28

28

Potential

Chain

29 – 293

265

ADP-ribosyl cyclase 2

PRO_0000004032

Propeptide

294 – 318

25

Removed in mature form Potential

PRO_0000004033

Sites

Site

109

1

Crucial for NAD binding and catalysis

Site

172

1

Crucial for NAD binding and catalysis

Site

210

1

Crucial for NAD binding and catalysis

Amino acid modifications

Lipidation

293

1

GPI-anchor amidated alanine Potential

Glycosylation

66

1

N-linked (GlcNAc...) Potential

Glycosylation

95

1

N-linked (GlcNAc...)

Glycosylation

148

1

N-linked (GlcNAc...) Potential

Glycosylation

192

1

N-linked (GlcNAc...) Ref.5

Disulfide bond

51 ↔ 67

Disulfide bond

83 ↔ 163

Disulfide bond

144 ↔ 157

Disulfide bond

238 ↔ 259

Disulfide bond

271 ↔ 280

Natural variations

Natural variant

77

1

A → V: dbSNP rs2302466.

VAR_028438

Natural variant

101

1

I → V: dbSNP rs6840615.

VAR_028439

Natural variant

125

1

R → H: dbSNP rs2302465.

VAR_021964

Natural variant

145

1

R → Q: dbSNP rs2302464.

VAR_021965

Experimental info

Sequence conflict

36

1

G → A in BAA04885. Ref.1

Secondary structure

1

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318

Helix Strand Turn

Details...

Helix

43 – 57

15

Helix

67 – 74

8

Helix

75 – 79

5

Helix

91 – 96

6

Beta strand

107 – 110

4

Helix

114 – 117

4

Turn

121 – 124

4

Helix

133 – 136

4

Turn

137 – 140

4

Turn

167 – 169

3

Helix

172 – 175

4

Beta strand

186 – 192

7

Beta strand

202 – 204

3

Helix

205 – 209

5

Helix

211 – 213

3

Helix

216 – 218

3

Beta strand

221 – 227

7

Helix

244 – 252

9

Beta strand

257 – 261

5

Helix

264 – 271

8

Helix

278 – 280

3

Sequences

	Sequence		Length	Mass (Da)
	Q10588-1 [UniParc]. Last modified October 17, 2006. Version 2. Checksum: E0DD04C89A8F4215	FASTA	318	35,724
	10 20 30 40 50 60 MAAQGCAASR LLQLLLQLLL LLLLLAAGGA RARWRGEGTS AHLRDIFLGR CAEYRALLSP 70 80 90 100 110 120 EQRNKNCTAI WEAFKVALDK DPCSVLPSDY DLFINLSRHS IPRDKSLFWE NSHLLVNSFA 130 140 150 160 170 180 DNTRRFMPLS DVLYGRVADF LSWCRQKNDS GLDYQSCPTS EDCENNPVDS FWKRASIQYS 190 200 210 220 230 240 KDSSGVIHVM LNGSEPTGAY PIKGFFADYE IPNLQKEKIT RIEIWVMHEI GGPNVESCGE 250 260 270 280 290 300 GSMKVLEKRL KDMGFQYSCI NDYRPVKLLQ CVDHSTHPDC ALKSAAAATQ RKAPSLYTEQ 310 RAGLIIPLFL VLASRTQL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"BST-1, a surface molecule of bone marrow stromal cell lines that facilitates pre-B-cell growth." Kaisho T., Ishikawa J., Oritani K., Inazawa J., Tomizawa H., Muraoka O., Ochi T., Hirano T. Proc. Natl. Acad. Sci. U.S.A. 91:5325-5329(1994) [PubMed: 8202488] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
[5]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed: 16335952] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-192, MASS SPECTROMETRY. Tissue: Plasma.
[6]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-95, MASS SPECTROMETRY. Tissue: Liver.
[7]	"Crystallographic studies on human BST-1/CD157 with ADP-ribosyl cyclase and NAD glycohydrolase activities." Yamamoto-Katayama S., Ariyoshi M., Ishihara K., Hirano T., Jingami H., Morikawa K. J. Mol. Biol. 316:711-723(2002) [PubMed: 11866528] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 33-297.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

D21878 mRNA. Translation: BAA04885.1.
BT019502 mRNA. Translation: AAV38309.1.
AC114744 Genomic DNA. Translation: AAY40930.1.
BC012095 mRNA. Translation: AAH12095.1.

IPI

IPI00026240.

PIR

I59301.

RefSeq

NP_004325.2.

UniGene

Hs.714863

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ISF	X-ray	2.50	A/B	33-297	[»]
1ISG	X-ray	2.60	A/B	33-297	[»]
1ISH	X-ray	2.40	A/B	33-297	[»]
1ISI	X-ray	2.10	A/B	33-297	[»]
1ISJ	X-ray	2.30	A/B	33-297	[»]
1ISM	X-ray	3.00	A/B	33-297	[»]

SMR

Q10588. Positions 34-283.

ModBase

Search...

Proteomic databases

PRIDE

Q10588.

Genome annotation databases

Ensembl

ENSG00000109743. Homo sapiens. [Contig view]

GeneID

683.

KEGG

hsa:683.

NMPDR

fig|9606.3.peg.23951.

UCSC

uc003goh.2. human.

Organism-specific databases

GeneCards

GC04P015380.

H-InvDB

HIX0004111.

HGNC

HGNC:1118. BST1.

MIM

600387. gene.

PharmGKB

PA25435.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q10588.

Enzyme and pathway databases

BRENDA

3.2.2.5. 247.

Gene expression databases

ArrayExpress

Q10588.

Bgee

Q10588.

CleanEx

HS_BST1.

GermOnline

ENSG00000109743. Homo sapiens.

Family and domain databases

InterPro

IPR003193. ADP-ribosyl_cyclase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

PANTHER

PTHR10912. Rib_hydrolayse. 1 hit.

Pfam

PF02267. Rib_hydrolayse. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

2812.

SOURCE

Search...

Entry information

Entry name

BST1_HUMAN

Accession

Primary (citable) accession number: Q10588
Secondary accession number(s): Q5U0K0, Q96EN3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 17, 2006
Last modified:	July 7, 2009
This is version 94 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)