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P29241 (NADA_APLCA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase

EC=3.2.2.6
Alternative name(s):
2'-phospho-ADP-ribosyl cyclase
2'-phospho-ADP-ribosyl cyclase/2'-phospho-cyclic-ADP-ribose transferase
EC=2.4.99.20
2'-phospho-cyclic-ADP-ribose transferase
ADP-ribosyl cyclase
Short name=ADPRC
Short name=ADRC
NAD glycohydrolase
NAD(+) nucleosidase
Short name=NADase
OrganismAplysia californica (California sea hare)
Taxonomic identifier6500 [NCBI]
Taxonomic lineageEukaryotaMetazoaLophotrochozoaMolluscaGastropodaHeterobranchiaEuthyneuraEuopisthobranchiaAplysiomorphaAplysioideaAplysiidaeAplysia

Protein attributes

Sequence length282 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Synthesizes the second messagers cyclic ADP-ribose and nicotinate-adenine dinucleotide phosphate, the former a second messenger for calcium mobilization from endoplasmic reticulum. Also has cADPr hydrolase activity. Ref.5

Catalytic activity

NAD+ + H2O = ADP-D-ribose + nicotinamide. Ref.2

NADP+ + nicotinate = nicotinate-adenine dinucleotide phosphate + nicotinamide. Ref.2

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 processFertilization
   Cellular componentCytoplasmic vesicle
   DomainSignal
   LigandCalcium
NAD
NADP
   Molecular functionHydrolase
Transferase
   PTMDisulfide bond
Phosphoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processsingle fertilization

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasmic membrane-bounded vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionNAD(P)+ nucleosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

NAD+ nucleosidase activity

Inferred from electronic annotation. Source: InterPro

transferase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Ref.1 Ref.2
Chain25 – 282258ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
PRO_0000004030

Amino acid modifications

Disulfide bond39 ↔ 58
Disulfide bond75 ↔ 155
Disulfide bond136 ↔ 149
Disulfide bond230 ↔ 251
Disulfide bond263 ↔ 272

Secondary structure

.................................................. 282
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P29241 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 4CF809DF4E30A824

FASTA28231,899
        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 

« Hide

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], PROTEIN SEQUENCE OF 25-72; 84-95; 98-114; 190-209 AND 216-225.
Tissue: Ovotestis.
[2]"Unifying mechanism for Aplysia ADP-ribosyl cyclase and CD38/NAD(+) glycohydrolases."
Cakir-Kiefer C., Muller-Steffner H., Schuber F.
Biochem. J. 349:203-210(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-42, CATALYTIC ACTIVITY.
[3]"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.
[4]"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.
[5]"CD38 is the major enzyme responsible for synthesis of nicotinic acid-adenine dinucleotide phosphate in mammalian tissues."
Chini E.N., Chini C.C., Kato I., Takasawa S., Okamoto H.
Biochem. J. 362:125-130(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN SYNTHESIS OF NICOTINIC ACID-ADENINE DINUCLEOTIDE PHOSPHATE.
[6]"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.
PIRS27769.
RefSeqNP_001191476.1. NM_001204547.1.
UniGeneAcl.44579.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LBEX-ray2.40A/B25-282[»]
1R0SX-ray2.00A/B25-282[»]
1R12X-ray1.70A/B25-282[»]
1R15X-ray2.40A/B/C/D/E/F/G/H25-282[»]
1R16X-ray2.00A/B25-282[»]
3I9JX-ray2.18A/B25-282[»]
3I9KX-ray1.83A/B25-282[»]
3I9LX-ray1.75A/B25-282[»]
3I9OX-ray3.00A/B25-282[»]
3ZWMX-ray2.50A/B/C/D/E/F/G/H25-282[»]
3ZWNX-ray1.80A/B25-282[»]
3ZWOX-ray2.00A/B/C/D/E/F/G/H24-282[»]
3ZWPX-ray2.11A/B/C/D/E/F/G/H25-282[»]
3ZWVX-ray2.30A/B/C/D/E/F/G/H25-282[»]
3ZWWX-ray2.30A/B/C/D/E/F/G/H25-282[»]
3ZWXX-ray2.60A/B/C/D/E/F/G/H25-282[»]
3ZWYX-ray2.40A/B/C/D/E/F/G/H25-282[»]
ProteinModelPortalP29241.
SMRP29241. Positions 25-275.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100533234.

Organism-specific databases

CTD100533234.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR003193. ADP-ribosyl_cyclase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR10912. PTHR10912. 1 hit.
PfamPF02267. Rib_hydrolayse. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP29241.

Entry information

Entry nameNADA_APLCA
AccessionPrimary (citable) accession number: P29241
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: July 9, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references