[1]	NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. TISSUE=Ovotestis; PubMed=1650255 [NCBI, ExPASy, EBI, Israel, Japan] Glick D.L., Hellmich M.R., Beushausen S., Tempst P.J., Bayley H., Strumwasser F.; "Primary structure of a molluscan egg-specific NADase, a second-messenger enzyme."; Cell Regul. 2:211-218(1991).
[2]	CHARACTERIZATION. PubMed=1650254 [NCBI, ExPASy, EBI, Israel, Japan] Hellmich M.R., Strumwasser F.; "Purification and characterization of a molluscan egg-specific NADase, a second-messenger enzyme."; Cell Regul. 2:193-202(1991).
[3]	SIMILARITY TO CD38. DOI=10.1016/0968-0004(92)90337-9; PubMed=1471258 [NCBI, ExPASy, EBI, Israel, Japan] States D.J., Walseth T.F., Lee H.C.; "Similarities in amino acid sequences of Aplysia ADP-ribosyl cyclase and human lymphocyte antigen CD38."; Trends Biochem. Sci. 17:495-495(1992).
[4]	X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). DOI=10.1038/nsb1196-957; PubMed=8901875 [NCBI, ExPASy, EBI, Israel, Japan] Prasad G.S., McRee D.E., Stura E.A., Levitt D.G., Lee H.C., Stout C.D.; "Crystal structure of Aplysia ADP ribosyl cyclase, a homologue of the bifunctional ectozyme CD38."; Nat. Struct. Biol. 3:957-964(1996).

Comments

FUNCTION: Synthesizes cyclic ADP-ribose, a second messenger for calcium mobilization from endoplasmic reticulum.
CATALYTIC ACTIVITY: NAD⁺ + H₂O = ADP-ribose + nicotinamide.
ENZYME REGULATION: Activity is presumably regulated by its sequestration in vesicles before egg fertilization. After fertilization and upon NADase release, it could then be regulated via its potential phosphorylation sites.
SUBCELLULAR LOCATION: Note=Localized to vesicles or granules within ova of all stages.
TISSUE SPECIFICITY: Oocytes.
DEVELOPMENTAL STAGE: Immature eggs have higher levels of NADase transcripts than the mature ones.
PTM: Has different isoforms which may be the result of different amounts of phosphorylation.
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

M85206; AAA65698.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S27769; S27769.

3D structure databases

PDB

1LBE; X-ray; 2.40 A; A/B=25-282.	[ExPASy / RCSB / EBI]
1R0S; X-ray; 2.00 A; A/B=25-282.	[ExPASy / RCSB / EBI]
1R12; X-ray; 1.70 A; A/B=25-282.	[ExPASy / RCSB / EBI]
1R15; X-ray; 2.40 A; A/B/C/D/E/F/G/H=25-282.	[ExPASy / RCSB / EBI]
1R16; X-ray; 2.00 A; A/B=25-282.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1LBE; -.
1R0S; -.
1R12; -.
1R15; -.
1R16; -.

ModBase

P29241.

Ontologies

GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0003953;	Molecular function: NAD+ nucleosidase activity (inferred from electronic annotation from InterPro).
GO:0008152;	Biological process: metabolic process (inferred from electronic annotation from InterPro).
GO:0007338;	Biological process: single fertilization (inferred from electronic annotation from UniProtKB-KW).
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; 1.

PANTHER

PTHR10912; Rib_hydrolayse; 1.

Pfam

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

Other

P29241; -.

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

Keywords

3D-structure; Calcium; Direct protein sequencing; Fertilization; Hydrolase; NAD; Phosphoprotein; Signal.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 24`	`24`
`CHAIN`	`25 282`	`258`	`ADP-ribosyl cyclase.`	`PRO_0000004030`
`DISULFID`	`39 58`
`DISULFID`	`75 155`
`DISULFID`	`136 149`
`DISULFID`	`230 251`
`DISULFID`	`263 272`
`HELIX`	`31 45`	`15`
`TURN`	`48 50`	`3`
`HELIX`	`58 69`	`12`
`HELIX`	`79 81`	`3`
`HELIX`	`83 89`	`7`
`TURN`	`95 97`	`3`
`STRAND`	`98 103`	`6`
`HELIX`	`105 112`	`8`
`TURN`	`113 116`	`4`
`HELIX`	`121 123`	`3`
`HELIX`	`125 130`	`6`
`HELIX`	`157 160`	`4`
`HELIX`	`164 173`	`10`
`STRAND`	`177 184`	`8`
`STRAND`	`188 190`	`3`
`STRAND`	`195 197`	`3`
`HELIX`	`198 201`	`4`
`HELIX`	`204 206`	`3`
`STRAND`	`211 219`	`9`
`STRAND`	`222 224`	`3`
`TURN`	`230 232`	`3`
`HELIX`	`234 244`	`11`
`STRAND`	`248 254`	`7`
`HELIX`	`256 265`	`10`
`HELIX`	`270 272`	`3`

Sequence information

Length: 282 AA [This is the length of the unprocessed precursor]

Molecular weight: 31899 Da [This is the MW of the unprocessed precursor]

CRC64: 4CF809DF4E30A824 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSPVAIIACV CLAVTLTSIS PSEAIVPTRE LENVFLGRCK DYEITRYLDI LPRVRSDCSA 

        70         80         90        100        110        120 
LWKDFFKAFS FKNPCDLDLG SYKDFFTSAQ QQLPKNKVMF WSGVYDEAHD YANTGRKYIT 

       130        140        150        160        170        180 
LEDTLPGYML NSLVWCGQRA NPGFNEKVCP DFKTCPVQAR ESFWGMASSS YAHSAEGEVT 

       190        200        210        220        230        240 
YMVDGSNPKV PAYRPDSFFG KYELPNLTNK VTRVKVIVLH RLGEKIIEKC GAGSLLDLEK 

       250        260        270        280 
LVKAKHFAFD CVENPRAVLF LLCSDNPNAR ECRLAKRFYR IA

P29241 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