[1]	NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND FUNCTION. TISSUE=Osteoclast; DOI=10.1083/jcb.146.5.1161; PubMed=10477767 [NCBI, ExPASy, EBI, Israel, Japan] Sun L., Adebanjo O.A., Moonga B.S., Corisdeo S., Anandatheerthavarada H.K., Biswas G., Arakawa T., Hakeda Y., Koval A., Sodam B., Bevis P.J.R., Moser A.J., Lai F.A., Epstein S., Troen B.R., Kumegawa M., Zaidi M.; "CD38/ADP-ribosyl cyclase: a new role in the regulation of osteoclastic bone resorption."; J. Cell Biol. 146:1161-1172(1999).
[2]	ERRATUM. Sun L., Adebanjo O.A., Moonga B.S., Corisdeo S., Anandatheerthavarada H.K., Biswas G., Arakawa T., Hakeda Y., Koval A., Sodam B., Bevis P.J.R., Moser A.J., Lai F.A., Epstein S., Troen B.R., Kumegawa M., Zaidi M.; J. Cell Biol. 146:1391-1392(1999).
[3]	NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION. TISSUE=Osteoclast; DOI=10.1006/bbrc.2000.3041; PubMed=10891341 [NCBI, ExPASy, EBI, Israel, Japan] Adebanjo O.A., Koval A., Moonga B.S., Wu X.B., Yao S., Bevis P.J.R., Kumegawa M., Zaidi M., Sun L.; "Molecular cloning, expression, and functional characterization of a novel member of the CD38 family of ADP-ribosyl cyclases."; Biochem. Biophys. Res. Commun. 273:884-889(2000).

Comments

FUNCTION: Synthesizes cyclic ADP-ribose, a second messenger for glucose-induced insulin secretion. Also has cADPr hydrolase activity.
CATALYTIC ACTIVITY: NAD⁺ + H₂O = ADP-ribose + nicotinamide.
SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. Microsome membrane; Single-pass type II membrane protein. Endoplasmic reticulum membrane; Single-pass type II membrane protein.
TISSUE SPECIFICITY: Osteoclasts.
SIMILARITY: Belongs to the ADP-ribosyl cyclase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF272974; AAF87715.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

JC7323; JC7323.

NP_001076152.1; -.

3D structure databases

HSSP

Q10588; 1ISI. [HSSP ENTRY / PDB]

ModBase

Q9MZ03.

Ontologies

GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005792;	Cellular component: microsome (inferred from direct assay from UniProtKB).
GO:0005886;	Cellular component: plasma membrane (inferred from direct assay from UniProtKB).
GO:0005488;	Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0003953;	Molecular function: NAD+ nucleosidase activity (inferred from direct assay from UniProtKB).
GO:0007242;	Biological process: intracellular signaling cascade (inferred from direct assay from UniProtKB).
GO:0008152;	Biological process: metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR016040; NAD(P)-bd.
IPR003193; Rib_hydrolayse.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 2.

PANTHER

PTHR10912; Rib_hydrolayse; 1.

Pfam

PF02267; Rib_hydrolayse; 1.
Pfam graphical view of domain structure.

ProtoNet

Q9MZ03.

Genome annotation databases

GeneID

100009409; -.

Phylogenomic databases

HOVERGEN

Q9MZ03; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cell membrane; Endoplasmic reticulum; Glycoprotein; Hydrolase; Membrane; Microsome; NAD; Signal-anchor; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 298`	`298`	`ADP-ribosyl cyclase 1.`	`PRO_0000144069`
`TOPO_DOM`	`1 21`	`21`	`Cytoplasmic (Potential).`
`TRANSMEM`	`22 42`	`21`	`Signal-anchor for type II membrane protein (Potential).`
`TOPO_DOM`	`43 298`	`256`	`Extracellular (Potential).`
`ACT_SITE`	`117 117`		`By similarity.`
`ACT_SITE`	`199 199`		`By similarity.`
`CARBOHYD`	`98 98`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`118 118`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`177 177`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`207 207`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`268 268`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`64 80`		`By similarity.`
`DISULFID`	`97 178`		`By similarity.`
`DISULFID`	`158 171`		`By similarity.`
`DISULFID`	`252 273`		`By similarity.`
`DISULFID`	`285 294`		`By similarity.`

Sequence information

Length: 298 AA [This is the length of the unprocessed precursor]

Molecular weight: 33637 Da [This is the MW of the unprocessed precursor]

CRC64: 7A4942F5A4625B60 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPDYEFSPAS GDRPRSWISK QVLIVLGVCL PVILALAIWV GVLTWRQSSM GATDHVSAIV 

        70         80         90        100        110        120 
LGRCLTYTRN MHPELRNQDC KKILNTFTSA FVSKDPCNIT KEDYQPLIDL VTQTVPCNKT 

       130        140        150        160        170        180 
LFWSRSKELA HQYSGIQKEM FTLEDTLLGY IADNLVWCGD PRTSEVKEEF CPYRNENCSS 

       190        200        210        220        230        240 
TATSVFWTVV SQKFAESACG TVYVMLNGSR TTAFSKASTF GSVEVFNLHP DRVHTLHAWV 

       250        260        270        280        290 
MHDIGGVERD SCLGSSIKEL KSIVNQRNIS FFCQDDYRPA RFVQCVRHPE HPSCSVLM

Q9MZ03 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools