Q27312 (NADA_APLKU) 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 kurodai (Kuroda's sea hare)
Taxonomic identifier	6501 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › 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	Ovotestis.
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
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	Potential
	Chain	25 – 282	258	ADP-ribosyl cyclase		PRO_0000004031
Amino acid modifications
	Disulfide bond	39 ↔ 58		By similarity
	Disulfide bond	75 ↔ 155		By similarity
	Disulfide bond	136 ↔ 149		By similarity
	Disulfide bond	230 ↔ 251		By similarity
	Disulfide bond	263 ↔ 272		By similarity
Experimental info
	Mutagenesis	95	1	K → C: Has also cADPR hydrolase activity; when associated with C-176. Ref.2
	Mutagenesis	176	1	E → C: Has also cADPR hydrolase activity; when associated with C-95. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q27312 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 9725E7B00A16F97E	FASTA	282	31,889
	10 20 30 40 50 60 MSPVAIVACV CLAVTLTRIS PSEAIFPTPE LQNVFLGRCK DYEITRYLTI LPRVKSDCRA 70 80 90 100 110 120 LWTNFFKAFS FKAPCNLDLG SYKDFFQRAQ QTLPKNKVMF WSGVYDEAHD FADDGRKYIT 130 140 150 160 170 180 LEDTLPGYML NSLVWCGQRD KPGFNQKVCP DFKDCPVQAR ESFWGTASSS YAHSAEGDVT 190 200 210 220 230 240 YMVDGSNPKV PAYRPDSFFG KYELPNLTNK VTKVKVIVLH QLGQKIIERC GAGSLLDLEM 250 260 270 280 VVKAKKFGFD CVENPKSVLF LLCADNPNAR ECQLAKRYYR IA

References

[1]	"The structure of the Aplysia kurodai gene encoding ADP-ribosyl cyclase, a second-messenger enzyme." Nata K., Sugimoto T., Tohgo A., Takamura T., Noguchi N., Matsuoka A., Numakunai T., Shikama K., Yonekura H., Takasawa S., Okamoto H. Gene 158:213-218(1995) [PubMed: 7607544] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Tissue: Ovotestis.
[2]	"Essential cysteine residues for cyclic ADP-ribose synthesis and hydrolysis by CD38." Tohgo A., Takasawa S., Noguchi N., Koguma T., Nata K., Sugimoto T., Furuya Y., Yonekura H., Okamoto H. J. Biol. Chem. 269:28555-28557(1994) [PubMed: 7961800] [Abstract] Cited for: MUTAGENESIS OF LYS-95 AND GLU-176.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D30048 mRNA. Translation: BAA06284.1. D38536 Genomic DNA. Translation: BAA07537.1.
PIR	JC4134.
3D structure databases
ProteinModelPortal	Q27312.
SMR	Q27312. Positions 25-275.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
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. 2 hits.
PANTHER	PTHR10912. Rib_hydrolayse. 1 hit.
Pfam	PF02267. Rib_hydrolayse. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NADA_APLKU

Accession

Primary (citable) accession number: Q27312

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	December 14, 2011
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)