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 16-JUN-2009, entry version 42. DE RecName: Full=ADP-ribosyl cyclase; DE Short=ADRC; DE EC=3.2.2.5; DE AltName: Full=NAD(+) nucleosidase; DE Short=NADase; DE AltName: Full=NAD glycohydrolase; DE Flags: Precursor; OS Aplysia kurodai (Kuroda's sea hare). OC Eukaryota; Metazoa; Mollusca; Gastropoda; Orthogastropoda; OC Apogastropoda; Heterobranchia; Euthyneura; Opisthobranchia; Anaspidea; OC Aplysioidea; Aplysiidae; Aplysia. OX NCBI_TaxID=6501; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RC TISSUE=Ovotestis; RX MEDLINE=95331619; 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 RT cyclase, a second-messenger enzyme."; RL Gene 158:213-218(1995). RN [2] RP MUTAGENESIS OF LYS-95 AND GLU-176. RX MEDLINE=95050652; PubMed=7961800; 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 RT hydrolysis by CD38."; RL J. Biol. Chem. 269:28555-28557(1994). CC -!- FUNCTION: Synthesizes cyclic ADP-ribose, a second messenger for CC calcium mobilization from endoplasmic reticulum. CC -!- CATALYTIC ACTIVITY: NAD(+) + H(2)O = ADP-ribose + nicotinamide. CC -!- ENZYME REGULATION: Activity is presumably regulated by its CC sequestration in vesicles before egg fertilization. After CC fertilization and upon NADase release, it could then be regulated CC via its potential phosphorylation sites. CC -!- SUBCELLULAR LOCATION: Note=Localized to vesicles or granules CC within ova of all stages. CC -!- TISSUE SPECIFICITY: Ovotestis. CC -!- SIMILARITY: Belongs to the ADP-ribosyl cyclase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D30048; BAA06284.1; -; mRNA. DR EMBL; D38536; BAA07537.1; -; Genomic_DNA. DR PIR; JC4134; JC4134. DR HSSP; P29241; 1LBE. DR SMR; Q27312; 25-275. DR BRENDA; 3.2.2.5; 290610. DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-KW. DR GO; GO:0003953; F:NAD+ nucleosidase activity; IEA:EC. DR GO; GO:0008152; P:metabolic process; IEA:InterPro. DR GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW. DR InterPro; IPR003193; ADP-ribosyl_cyclase. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR PANTHER; PTHR10912; Rib_hydrolayse; 1. DR Pfam; PF02267; Rib_hydrolayse; 1. PE 1: Evidence at protein level; KW Calcium; Disulfide bond; Fertilization; Hydrolase; NAD; Signal. FT SIGNAL 1 24 Potential. FT CHAIN 25 282 ADP-ribosyl cyclase. FT /FTId=PRO_0000004031. FT DISULFID 39 58 By similarity. FT DISULFID 75 155 By similarity. FT DISULFID 136 149 By similarity. FT DISULFID 230 251 By similarity. FT DISULFID 263 272 By similarity. FT MUTAGEN 95 95 K->C: Has also cADPR hydrolase activity; FT when associated with C-176. FT MUTAGEN 176 176 E->C: Has also cADPR hydrolase activity; FT when associated with C-95. 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 //