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P29241

- NADA_APLCA

UniProt

P29241 - NADA_APLCA

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Protein
ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
Gene
N/A
Organism
Aplysia californica (California sea hare)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

NAD+ + H2O = ADP-D-ribose + nicotinamide.1 Publication
NADP+ + nicotinate = nicotinate-adenine dinucleotide phosphate + nicotinamide.1 Publication

Enzyme regulationi

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.

GO - Molecular functioni

  1. NAD(P)+ nucleosidase activity Source: UniProtKB-EC
  2. NAD+ nucleosidase activity Source: InterPro
  3. transferase activity Source: UniProtKB-KW
Complete GO annotation...

GO - Biological processi

  1. single fertilization Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transferase

Keywords - Biological processi

Fertilization

Keywords - Ligandi

Calcium, NAD, NADP

Names & Taxonomyi

Protein namesi
Recommended 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
OrganismiAplysia californica (California sea hare)
Taxonomic identifieri6500 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaHeterobranchiaEuthyneuraEuopisthobranchiaAplysiomorphaAplysioideaAplysiidaeAplysia

Subcellular locationi

Cytoplasmic vesicle
Note: Localized to vesicles or granules within ova of all stages.

GO - Cellular componenti

  1. cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 24242 Publications
Add
BLAST
Chaini25 – 282258ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
PRO_0000004030Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi39 ↔ 58
Disulfide bondi75 ↔ 155
Disulfide bondi136 ↔ 149
Disulfide bondi230 ↔ 251
Disulfide bondi263 ↔ 272

Post-translational modificationi

Has different isoforms which may be the result of different amounts of phosphorylation.

Keywords - PTMi

Disulfide bond, Phosphoprotein

Expressioni

Tissue specificityi

Oocytes.

Developmental stagei

Immature eggs have higher levels of NADase transcripts than the mature ones.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi31 – 4515
Turni48 – 503
Helixi58 – 6912
Helixi74 – 763
Turni79 – 824
Helixi83 – 897
Turni95 – 973
Beta strandi98 – 1036
Helixi105 – 1128
Turni113 – 1164
Helixi121 – 1233
Helixi125 – 1306
Helixi152 – 1543
Helixi157 – 1604
Helixi162 – 17413
Beta strandi177 – 18610
Beta strandi188 – 1903
Beta strandi195 – 1973
Helixi198 – 2014
Helixi204 – 2063
Beta strandi211 – 2199
Beta strandi222 – 2243
Beta strandi230 – 2323
Helixi233 – 24412
Beta strandi248 – 2547
Helixi256 – 2649
Helixi270 – 2723

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP29241.
SMRiP29241. Positions 25-275.

Miscellaneous databases

EvolutionaryTraceiP29241.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR003193. ADP-ribosyl_cyclase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR10912. PTHR10912. 1 hit.
PfamiPF02267. Rib_hydrolayse. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P29241-1 [UniParc]FASTAAdd to Basket

« Hide

MSPVAIIACV CLAVTLTSIS PSEAIVPTRE LENVFLGRCK DYEITRYLDI    50
LPRVRSDCSA LWKDFFKAFS FKNPCDLDLG SYKDFFTSAQ QQLPKNKVMF 100
WSGVYDEAHD YANTGRKYIT LEDTLPGYML NSLVWCGQRA NPGFNEKVCP 150
DFKTCPVQAR ESFWGMASSS YAHSAEGEVT YMVDGSNPKV PAYRPDSFFG 200
KYELPNLTNK VTRVKVIVLH RLGEKIIEKC GAGSLLDLEK LVKAKHFAFD 250
CVENPRAVLF LLCSDNPNAR ECRLAKRFYR IA 282
Length:282
Mass (Da):31,899
Last modified:December 1, 1992 - v1
Checksum:i4CF809DF4E30A824
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M85206 mRNA. Translation: AAA65698.1.
PIRiS27769.
RefSeqiNP_001191476.1. NM_001204547.1.
UniGeneiAcl.44579.

Genome annotation databases

GeneIDi100533234.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M85206 mRNA. Translation: AAA65698.1 .
PIRi S27769.
RefSeqi NP_001191476.1. NM_001204547.1.
UniGenei Acl.44579.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 25-282 [» ]
3ZWN X-ray 1.80 A/B 25-282 [» ]
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 25-282 [» ]
3ZWV X-ray 2.30 A/B/C/D/E/F/G/H 25-282 [» ]
3ZWW X-ray 2.30 A/B/C/D/E/F/G/H 25-282 [» ]
3ZWX X-ray 2.60 A/B/C/D/E/F/G/H 25-282 [» ]
3ZWY X-ray 2.40 A/B/C/D/E/F/G/H 25-282 [» ]
ProteinModelPortali P29241.
SMRi P29241. Positions 25-275.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100533234.

Organism-specific databases

CTDi 100533234.

Miscellaneous databases

EvolutionaryTracei P29241.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
InterProi IPR003193. ADP-ribosyl_cyclase.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
PANTHERi PTHR10912. PTHR10912. 1 hit.
Pfami PF02267. Rib_hydrolayse. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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).

Entry informationi

Entry nameiNADA_APLCA
AccessioniPrimary (citable) accession number: P29241
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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