P29241 (NADA_APLCA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: ADP-ribosyl cyclase Short name=ADRC EC=3.2.2.5 Alternative name(s): NAD glycohydrolase NAD(+) nucleosidase Short name=NADase
Organism	Aplysia californica (California sea hare)
Taxonomic identifier	6500 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Lophotrochozoa › Mollusca › Gastropoda › Heterobranchia › Euthyneura › Euopisthobranchia › Aplysiomorpha › 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	Cytoplasmic vesicle. 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
Cellular component	Cytoplasmic vesicle
Domain	Signal
Ligand	Calcium NAD
Molecular function	Hydrolase
PTM	Disulfide bond Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	single fertilization Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasmic membrane-bounded vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	NAD+ nucleosidase activity Inferred from electronic annotation. Source: EC nucleotide 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 – 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

74 – 76

3

Turn

79 – 82

4

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

152 – 154

3

Helix

157 – 160

4

Helix

162 – 174

13

Beta strand

177 – 186

10

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

Beta strand

230 – 232

3

Helix

233 – 244

12

Beta strand

248 – 254

7

Helix

256 – 264

9

Helix

270 – 272

3

Sequences

	Sequence		Length	Mass (Da)
	P29241 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M85206 mRNA. Translation: AAA65698.1.

PIR

S27769.

RefSeq

NP_001191476.1. NM_001204547.1.

UniGene

Acl.44579.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]
3I9J	X-ray	2.18	A/B	25-282	[»]
3I9K	X-ray	1.83	A/B	25-282	[»]
3I9L	X-ray	1.75	A/B	25-282	[»]
3I9O	X-ray	3.00	A/B	25-282	[»]
3ZWM	X-ray	2.50	A/B/C/D/E/F/G/H	24-282	[»]
3ZWN	X-ray	1.80	A/B	24-282	[»]
3ZWO	X-ray	2.00	A/B/C/D/E/F/G/H	24-282	[»]
3ZWP	X-ray	2.11	A/B/C/D/E/F/G/H	24-282	[»]
3ZWV	X-ray	2.30	A/B/C/D/E/F/G/H	24-282	[»]
3ZWW	X-ray	2.30	A/B/C/D/E/F/G/H	24-282	[»]
3ZWX	X-ray	2.60	A/B/C/D/E/F/G/H	24-282	[»]
3ZWY	X-ray	2.40	A/B/C/D/E/F/G/H	24-282	[»]

ProteinModelPortal

P29241.

SMR

P29241. Positions 25-275.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

100533234.

Organism-specific databases

CTD

100533234.

Family and domain databases

Gene3D

3.40.50.720. 1 hit.

InterPro

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

PANTHER

PTHR10912. PTHR10912. 1 hit.

Pfam

PF02267. Rib_hydrolayse. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P29241.

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:	April 3, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)