ID   NADA_APLKU              Reviewed;         282 AA.
AC   Q27312;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase;
DE            EC=3.2.2.6;
DE   AltName: Full=2'-phospho-ADP-ribosyl cyclase;
DE   AltName: Full=2'-phospho-ADP-ribosyl cyclase/2'-phospho-cyclic-ADP-ribose transferase;
DE            EC=2.4.99.20;
DE   AltName: Full=2'-phospho-cyclic-ADP-ribose transferase;
DE   AltName: Full=ADP-ribosyl cyclase;
DE            Short=ADPRC;
DE            Short=ADRC;
DE   AltName: Full=NAD glycohydrolase;
DE   AltName: Full=NAD(+) nucleosidase;
DE            Short=NADase;
DE   Flags: Precursor;
OS   Aplysia kurodai (Kuroda's sea hare).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Tectipleura; Aplysiida; Aplysioidea;
OC   Aplysiidae; Aplysia.
OX   NCBI_TaxID=6501;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   TISSUE=Ovotestis;
RX   PubMed=7607544; DOI=10.1016/0378-1119(95)00095-n;
RA   Nata K., Sugimoto T., Tohgo A., Takamura T., Noguchi N., Matsuoka A.,
RA   Numakunai T., Shikama K., Yonekura H., Takasawa S., Okamoto H.;
RT   "The structure of the Aplysia kurodai gene encoding ADP-ribosyl cyclase, a
RT   second-messenger enzyme.";
RL   Gene 158:213-218(1995).
RN   [2]
RP   MUTAGENESIS OF LYS-95 AND GLU-176.
RX   PubMed=7961800; DOI=10.1016/s0021-9258(19)61940-x;
RA   Tohgo A., Takasawa S., Noguchi N., Koguma T., Nata K., Sugimoto T.,
RA   Furuya Y., Yonekura H., Okamoto H.;
RT   "Essential cysteine residues for cyclic ADP-ribose synthesis and hydrolysis
RT   by CD38.";
RL   J. Biol. Chem. 269:28555-28557(1994).
CC   -!- FUNCTION: Synthesizes the second messengers cyclic ADP-ribose and
CC       nicotinate-adenine dinucleotide phosphate, the former a second
CC       messenger for calcium mobilization from endoplasmic reticulum. Also has
CC       cADPr hydrolase activity.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide;
CC         Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + nicotinate = nicotinamide + nicotinate-adenine
CC         dinucleotide phosphate; Xref=Rhea:RHEA:38599, ChEBI:CHEBI:17154,
CC         ChEBI:CHEBI:32544, ChEBI:CHEBI:58349, ChEBI:CHEBI:75967;
CC         EC=2.4.99.20;
CC   -!- ACTIVITY REGULATION: Activity is presumably regulated by its
CC       sequestration in vesicles before egg fertilization. After fertilization
CC       and upon NADase release, it could then be regulated via its potential
CC       phosphorylation sites.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle. Note=Localized to vesicles
CC       or granules within ova of all stages.
CC   -!- TISSUE SPECIFICITY: Ovotestis.
CC   -!- SIMILARITY: Belongs to the ADP-ribosyl cyclase family. {ECO:0000305}.
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DR   EMBL; D30048; BAA06284.1; -; mRNA.
DR   EMBL; D38536; BAA07537.1; -; Genomic_DNA.
DR   PIR; JC4134; JC4134.
DR   AlphaFoldDB; Q27312; -.
DR   SMR; Q27312; -.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProt.
DR   GO; GO:0050135; F:NAD(P)+ nucleosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0061809; F:NAD+ nucleotidase, cyclic ADP-ribose generating; IEA:UniProtKB-EC.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
DR   CDD; cd04759; Rib_hydrolase; 1.
DR   InterPro; IPR003193; ADP-ribosyl_cyclase.
DR   PANTHER; PTHR10912; PTHR10912; 1.
DR   Pfam; PF02267; Rib_hydrolayse; 1.
PE   1: Evidence at protein level;
KW   Calcium; Cytoplasmic vesicle; Disulfide bond; Fertilization; Hydrolase;
KW   NAD; NADP; Signal; Transferase.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..282
FT                   /note="ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase"
FT                   /id="PRO_0000004031"
FT   DISULFID        39..58
FT                   /evidence="ECO:0000250"
FT   DISULFID        75..155
FT                   /evidence="ECO:0000250"
FT   DISULFID        136..149
FT                   /evidence="ECO:0000250"
FT   DISULFID        230..251
FT                   /evidence="ECO:0000250"
FT   DISULFID        263..272
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         95
FT                   /note="K->C: Has also cADPR hydrolase activity; when
FT                   associated with C-176."
FT                   /evidence="ECO:0000269|PubMed:7961800"
FT   MUTAGEN         176
FT                   /note="E->C: Has also cADPR hydrolase activity; when
FT                   associated with C-95."
FT                   /evidence="ECO:0000269|PubMed:7961800"
SQ   SEQUENCE   282 AA;  31889 MW;  9725E7B00A16F97E CRC64;
     MSPVAIVACV CLAVTLTRIS PSEAIFPTPE LQNVFLGRCK DYEITRYLTI LPRVKSDCRA
     LWTNFFKAFS FKAPCNLDLG SYKDFFQRAQ QTLPKNKVMF WSGVYDEAHD FADDGRKYIT
     LEDTLPGYML NSLVWCGQRD KPGFNQKVCP DFKDCPVQAR ESFWGTASSS YAHSAEGDVT
     YMVDGSNPKV PAYRPDSFFG KYELPNLTNK VTKVKVIVLH QLGQKIIERC GAGSLLDLEM
     VVKAKKFGFD CVENPKSVLF LLCADNPNAR ECQLAKRYYR IA