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ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase (EC 3.2.2.6) (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) (ADPRC) (ADRC) (NAD glycohydrolase) (NAD( ) nucleosidase) (NADase)

 NADA_APLCA              Reviewed;         282 AA.
P29241;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
01-DEC-1992, sequence version 1.
27-SEP-2017, entry version 106.
RecName: Full=ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase;
EC=3.2.2.6;
AltName: Full=2'-phospho-ADP-ribosyl cyclase;
AltName: Full=2'-phospho-ADP-ribosyl cyclase/2'-phospho-cyclic-ADP-ribose transferase;
EC=2.4.99.20;
AltName: Full=2'-phospho-cyclic-ADP-ribose transferase;
AltName: Full=ADP-ribosyl cyclase;
Short=ADPRC;
Short=ADRC;
AltName: Full=NAD glycohydrolase;
AltName: Full=NAD(+) nucleosidase;
Short=NADase;
Flags: Precursor;
Aplysia californica (California sea hare).
Eukaryota; Metazoa; Lophotrochozoa; Mollusca; Gastropoda;
Heterobranchia; Euthyneura; Euopisthobranchia; Aplysiomorpha;
Aplysioidea; Aplysiidae; Aplysia.
NCBI_TaxID=6500;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 25-72; 84-95;
98-114; 190-209 AND 216-225.
TISSUE=Ovotestis;
PubMed=1650255;
Glick D.L., Hellmich M.R., Beushausen S., Tempst P.J., Bayley H.,
Strumwasser F.;
"Primary structure of a molluscan egg-specific NADase, a second-
messenger enzyme.";
Cell Regul. 2:211-218(1991).
[2]
PROTEIN SEQUENCE OF 25-42, AND CATALYTIC ACTIVITY.
PubMed=10861229; DOI=10.1042/0264-6021:3490203;
Cakir-Kiefer C., Muller-Steffner H., Schuber F.;
"Unifying mechanism for Aplysia ADP-ribosyl cyclase and CD38/NAD(+)
glycohydrolases.";
Biochem. J. 349:203-210(2000).
[3]
CHARACTERIZATION.
PubMed=1650254;
Hellmich M.R., Strumwasser F.;
"Purification and characterization of a molluscan egg-specific NADase,
a second-messenger enzyme.";
Cell Regul. 2:193-202(1991).
[4]
SIMILARITY TO CD38.
PubMed=1471258; DOI=10.1016/0968-0004(92)90337-9;
States D.J., Walseth T.F., Lee H.C.;
"Similarities in amino acid sequences of Aplysia ADP-ribosyl cyclase
and human lymphocyte antigen CD38.";
Trends Biochem. Sci. 17:495-495(1992).
[5]
FUNCTION IN SYNTHESIS OF NICOTINIC ACID-ADENINE DINUCLEOTIDE
PHOSPHATE.
PubMed=11829748; DOI=10.1042/0264-6021:3620125;
Chini E.N., Chini C.C., Kato I., Takasawa S., Okamoto H.;
"CD38 is the major enzyme responsible for synthesis of nicotinic acid-
adenine dinucleotide phosphate in mammalian tissues.";
Biochem. J. 362:125-130(2002).
[6]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
PubMed=8901875; DOI=10.1038/nsb1196-957;
Prasad G.S., McRee D.E., Stura E.A., Levitt D.G., Lee H.C.,
Stout C.D.;
"Crystal structure of Aplysia ADP ribosyl cyclase, a homologue of the
bifunctional ectozyme CD38.";
Nat. Struct. Biol. 3:957-964(1996).
-!- 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. {ECO:0000269|PubMed:11829748}.
-!- CATALYTIC ACTIVITY: NAD(+) + H(2)O = ADP-D-ribose + nicotinamide.
{ECO:0000269|PubMed:10861229}.
-!- CATALYTIC ACTIVITY: NADP(+) + nicotinate = nicotinate-adenine
dinucleotide phosphate + nicotinamide.
{ECO:0000269|PubMed:10861229}.
-!- 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.
-!- PTM: Has different isoforms which may be the result of different
amounts of phosphorylation.
-!- SIMILARITY: Belongs to the ADP-ribosyl cyclase family.
{ECO:0000305}.
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EMBL; M85206; AAA65698.1; -; mRNA.
PIR; S27769; S27769.
RefSeq; NP_001191476.1; NM_001204547.1.
UniGene; Acl.44579; -.
PDB; 1LBE; X-ray; 2.40 A; A/B=25-282.
PDB; 1R0S; X-ray; 2.00 A; A/B=25-282.
PDB; 1R12; X-ray; 1.70 A; A/B=25-282.
PDB; 1R15; X-ray; 2.40 A; A/B/C/D/E/F/G/H=25-282.
PDB; 1R16; X-ray; 2.00 A; A/B=25-282.
PDB; 3I9J; X-ray; 2.18 A; A/B=25-282.
PDB; 3I9K; X-ray; 1.83 A; A/B=25-282.
PDB; 3I9L; X-ray; 1.75 A; A/B=25-282.
PDB; 3I9O; X-ray; 3.00 A; A/B=25-282.
PDB; 3ZWM; X-ray; 2.50 A; A/B/C/D/E/F/G/H=25-282.
PDB; 3ZWN; X-ray; 1.80 A; A/B=25-282.
PDB; 3ZWO; X-ray; 2.00 A; A/B/C/D/E/F/G/H=24-282.
PDB; 3ZWP; X-ray; 2.11 A; A/B/C/D/E/F/G/H=25-282.
PDB; 3ZWV; X-ray; 2.30 A; A/B/C/D/E/F/G/H=25-282.
PDB; 3ZWW; X-ray; 2.30 A; A/B/C/D/E/F/G/H=25-282.
PDB; 3ZWX; X-ray; 2.60 A; A/B/C/D/E/F/G/H=25-282.
PDB; 3ZWY; X-ray; 2.40 A; A/B/C/D/E/F/G/H=25-282.
PDBsum; 1LBE; -.
PDBsum; 1R0S; -.
PDBsum; 1R12; -.
PDBsum; 1R15; -.
PDBsum; 1R16; -.
PDBsum; 3I9J; -.
PDBsum; 3I9K; -.
PDBsum; 3I9L; -.
PDBsum; 3I9O; -.
PDBsum; 3ZWM; -.
PDBsum; 3ZWN; -.
PDBsum; 3ZWO; -.
PDBsum; 3ZWP; -.
PDBsum; 3ZWV; -.
PDBsum; 3ZWW; -.
PDBsum; 3ZWX; -.
PDBsum; 3ZWY; -.
ProteinModelPortal; P29241; -.
SMR; P29241; -.
GeneID; 100533234; -.
CTD; 100533234; -.
BRENDA; 2.4.99.20; 390.
EvolutionaryTrace; P29241; -.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
GO; GO:0050135; F:NAD(P)+ nucleosidase activity; IEA:UniProtKB-EC.
GO; GO:0061809; F:NAD+ nucleotidase, cyclic ADP-ribose generating; IEA:UniProtKB-EC.
GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
CDD; cd04759; Rib_hydrolase; 1.
InterPro; IPR003193; ADP-ribosyl_cyclase.
PANTHER; PTHR10912; PTHR10912; 1.
Pfam; PF02267; Rib_hydrolayse; 1.
1: Evidence at protein level;
3D-structure; Calcium; Cytoplasmic vesicle; Direct protein sequencing;
Disulfide bond; Fertilization; Hydrolase; NAD; NADP; Phosphoprotein;
Signal; Transferase.
SIGNAL 1 24 {ECO:0000269|PubMed:10861229,
ECO:0000269|PubMed:1650255}.
CHAIN 25 282 ADP-ribosyl cyclase/cyclic ADP-ribose
hydrolase.
/FTId=PRO_0000004030.
DISULFID 39 58
DISULFID 75 155
DISULFID 136 149
DISULFID 230 251
DISULFID 263 272
HELIX 31 45 {ECO:0000244|PDB:1R12}.
TURN 48 50 {ECO:0000244|PDB:1R12}.
HELIX 58 69 {ECO:0000244|PDB:1R12}.
HELIX 74 76 {ECO:0000244|PDB:1R12}.
TURN 79 82 {ECO:0000244|PDB:1R12}.
HELIX 83 89 {ECO:0000244|PDB:1R12}.
TURN 95 97 {ECO:0000244|PDB:1LBE}.
STRAND 98 103 {ECO:0000244|PDB:1R12}.
HELIX 105 112 {ECO:0000244|PDB:1R12}.
TURN 113 116 {ECO:0000244|PDB:1R12}.
HELIX 121 123 {ECO:0000244|PDB:1R12}.
HELIX 125 130 {ECO:0000244|PDB:1R12}.
HELIX 152 154 {ECO:0000244|PDB:1R12}.
HELIX 157 160 {ECO:0000244|PDB:1R12}.
HELIX 162 174 {ECO:0000244|PDB:1R12}.
STRAND 177 186 {ECO:0000244|PDB:1R12}.
STRAND 188 190 {ECO:0000244|PDB:1R12}.
STRAND 195 197 {ECO:0000244|PDB:1LBE}.
HELIX 198 201 {ECO:0000244|PDB:1R12}.
HELIX 204 206 {ECO:0000244|PDB:1R12}.
STRAND 211 219 {ECO:0000244|PDB:1R12}.
STRAND 222 224 {ECO:0000244|PDB:1LBE}.
STRAND 230 232 {ECO:0000244|PDB:3I9J}.
HELIX 233 244 {ECO:0000244|PDB:1R12}.
STRAND 248 254 {ECO:0000244|PDB:1R12}.
HELIX 256 264 {ECO:0000244|PDB:1R12}.
HELIX 270 272 {ECO:0000244|PDB:1R12}.
SEQUENCE 282 AA; 31899 MW; 4CF809DF4E30A824 CRC64;
MSPVAIIACV CLAVTLTSIS PSEAIVPTRE LENVFLGRCK DYEITRYLDI LPRVRSDCSA
LWKDFFKAFS FKNPCDLDLG SYKDFFTSAQ QQLPKNKVMF WSGVYDEAHD YANTGRKYIT
LEDTLPGYML NSLVWCGQRA NPGFNEKVCP DFKTCPVQAR ESFWGMASSS YAHSAEGEVT
YMVDGSNPKV PAYRPDSFFG KYELPNLTNK VTRVKVIVLH RLGEKIIEKC GAGSLLDLEK
LVKAKHFAFD CVENPRAVLF LLCSDNPNAR ECRLAKRFYR IA


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