Reviewed, UniProtKB/Swiss-Prot P29241 (NADA_APLCA)

Names and origin

Protein names	Recommended name:     ADP-ribosyl cyclase       Short name=ADRC     EC=3.2.2.5 Alternative name(s):     NAD(+) nucleosidase       Short name=NADase     NAD glycohydrolase
Organism	Aplysia californica (California sea hare)
Taxonomic identifier	6500 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Mollusca › Gastropoda › Orthogastropoda › Apogastropoda › Heterobranchia › Euthyneura › Opisthobranchia › Anaspidea › Aplysioidea › Aplysiidae › Aplysia

Protein attributes

Sequence length	282 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 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.
Post-translational modification	Has different isoforms which may be the result of different amounts of phosphorylation.
Sequence similarities	Belongs to the ADP-ribosyl cyclase family.

Ontologies

Keywords
Biological process	Fertilization
Domain	Signal
Ligand	Calcium NAD
Molecular function	Hydrolase
PTM	Disulfide bond Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	metabolic process Inferred from electronic annotation. Source: InterPro single fertilization Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	NAD+ nucleosidase activity Inferred from electronic annotation. Source: EC calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

24

Chain

25 – 282

258

ADP-ribosyl cyclase

PRO_0000004030

Amino acid modifications

Disulfide bond

39 ↔ 58

Disulfide bond

75 ↔ 155

Disulfide bond

136 ↔ 149

Disulfide bond

230 ↔ 251

Disulfide bond

263 ↔ 272

Secondary structure

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282

Helix Strand Turn

Details...

Helix

31 – 45

15

Turn

48 – 50

3

Helix

58 – 69

12

Helix

79 – 81

3

Helix

83 – 89

7

Turn

95 – 97

3

Beta 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

Beta strand

177 – 184

8

Beta strand

188 – 190

3

Beta strand

195 – 197

3

Helix

198 – 201

4

Helix

204 – 206

3

Beta strand

211 – 219

9

Beta strand

222 – 224

3

Turn

230 – 232

3

Helix

234 – 244

11

Beta strand

248 – 254

7

Helix

256 – 265

10

Helix

270 – 272

3

Sequences

	Sequence		Length	Mass (Da)
	P29241-1 [UniParc]. Last modified December 1, 1992. Version 1. Checksum: 4CF809DF4E30A824	FASTA	282	31,899
	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

References

[1]	"Primary structure of a molluscan egg-specific NADase, a second-messenger enzyme." Glick D.L., Hellmich M.R., Beushausen S., Tempst P.J., Bayley H., Strumwasser F. Cell Regul. 2:211-218(1991) [PubMed: 1650255] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Tissue: Ovotestis.
[2]	"Purification and characterization of a molluscan egg-specific NADase, a second-messenger enzyme." Hellmich M.R., Strumwasser F. Cell Regul. 2:193-202(1991) [PubMed: 1650254] [Abstract] Cited for: CHARACTERIZATION.
[3]	"Similarities in amino acid sequences of Aplysia ADP-ribosyl cyclase and human lymphocyte antigen CD38." States D.J., Walseth T.F., Lee H.C. Trends Biochem. Sci. 17:495-495(1992) [PubMed: 1471258] [Abstract] Cited for: SIMILARITY TO CD38.
[4]	"Crystal structure of Aplysia ADP ribosyl cyclase, a homologue of the bifunctional ectozyme CD38." Prasad G.S., McRee D.E., Stura E.A., Levitt D.G., Lee H.C., Stout C.D. Nat. Struct. Biol. 3:957-964(1996) [PubMed: 8901875] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M85206 mRNA. Translation: AAA65698.1.

PIR

S27769.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LBE	X-ray	2.40	A/B	25-282	[»]
1R0S	X-ray	2.00	A/B	25-282	[»]
1R12	X-ray	1.70	A/B	25-282	[»]
1R15	X-ray	2.40	A/B/C/D/E/F/G/H	25-282	[»]
1R16	X-ray	2.00	A/B	25-282	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

3.2.2.5. 629.

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...

Entry information

Entry name

NADA_APLCA

Accession

Primary (citable) accession number: P29241

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	December 1, 1992
Last modified:	June 16, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)