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ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1 (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 1) (ADPRC 1) (Cyclic ADP-ribose hydrolase 1) (cADPr hydrolase 1) (CD antigen CD38)

 CD38_MACFA              Reviewed;         301 AA.
Q5VAN0;
29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
07-DEC-2004, sequence version 1.
27-SEP-2017, entry version 62.
RecName: Full=ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1;
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 1;
Short=ADPRC 1;
AltName: Full=Cyclic ADP-ribose hydrolase 1;
Short=cADPr hydrolase 1;
AltName: CD_antigen=CD38;
Name=CD38;
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
NCBI_TaxID=9541;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=15383153; DOI=10.1186/1471-2172-5-21;
Ferrero E., Orciani M., Vacca P., Ortolan E., Crovella S., Titti F.,
Saccucci F., Malavasi F.;
"Characterization and phylogenetic epitope mapping of CD38 ADPR
cyclase in the cynomolgus macaque.";
BMC Immunol. 5:21-21(2004).
-!- FUNCTION: Synthesizes the second messagers cyclic ADP-ribose and
nicotinate-adenine dinucleotide phosphate, the former a second
messenger for glucose-induced insulin secretion. Also has cADPr
hydrolase activity. Also moonlights as a receptor in cells of the
immune system (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: NAD(+) + H(2)O = ADP-D-ribose + nicotinamide.
-!- CATALYTIC ACTIVITY: NADP(+) + nicotinate = nicotinate-adenine
dinucleotide phosphate + nicotinamide.
-!- ENZYME REGULATION: ATP inhibits the hydrolyzing activity.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II
membrane protein {ECO:0000250}.
-!- SIMILARITY: Belongs to the ADP-ribosyl cyclase family.
{ECO:0000305}.
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EMBL; AY555148; AAT36330.1; -; mRNA.
RefSeq; NP_001274206.1; NM_001287277.1.
UniGene; Mfa.6349; -.
ProteinModelPortal; Q5VAN0; -.
SMR; Q5VAN0; -.
GeneID; 102126394; -.
KEGG; mcf:102126394; -.
CTD; 952; -.
HOVERGEN; HBG005277; -.
KO; K01242; -.
GO; GO:0016021; C:integral component of membrane; 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.
CDD; cd04759; Rib_hydrolase; 1.
InterPro; IPR003193; ADP-ribosyl_cyclase.
InterPro; IPR033567; CD38.
PANTHER; PTHR10912; PTHR10912; 1.
PANTHER; PTHR10912:SF9; PTHR10912:SF9; 1.
Pfam; PF02267; Rib_hydrolayse; 1.
2: Evidence at transcript level;
Disulfide bond; Glycoprotein; Hydrolase; Membrane; NAD; NADP;
Receptor; Signal-anchor; Transferase; Transmembrane;
Transmembrane helix.
CHAIN 1 301 ADP-ribosyl cyclase/cyclic ADP-ribose
hydrolase 1.
/FTId=PRO_0000144067.
TOPO_DOM 1 21 Cytoplasmic. {ECO:0000255}.
TRANSMEM 22 43 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 44 301 Extracellular. {ECO:0000255}.
ACT_SITE 120 120 {ECO:0000250}.
ACT_SITE 202 202 {ECO:0000250}.
CARBOHYD 101 101 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 121 121 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 210 210 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 220 220 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 68 83 {ECO:0000250}.
DISULFID 100 181 {ECO:0000250}.
DISULFID 161 174 {ECO:0000250}.
DISULFID 255 276 {ECO:0000250}.
DISULFID 288 297 {ECO:0000250}.
SEQUENCE 301 AA; 34422 MW; E659212B926165B1 CRC64;
MANCEFSPVS GDKPCCRLSR RAQVCLGVCL LVLLILVVVV AVVLPRWRQQ WSGSGTTSRF
PETVLARCVK YTEVHPEMRH VDCQSVWDAF KGAFISKYPC NITEEDYQPL VKLGTQTVPC
NKTLLWSRIK DLAHQFTQVQ RDMFTLEDML LGYLADDLTW CGEFNTFEIN YQSCPDWRKD
CSNNPVSVFW KTVSRRFAET ACGVVHVMLN GSRSKIFDKN STFGSVEVHN LQPEKVQALE
AWVIHGGRED SRDLCQDPTI KELESIISKR NIRFFCKNIY RPDKFLQCVK NPEDSSCLSG
I


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