CD38_MACFA
ID CD38_MACFA Reviewed; 301 AA.
AC Q5VAN0;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1;
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 1;
DE Short=ADPRC 1;
DE AltName: Full=Cyclic ADP-ribose hydrolase 1;
DE Short=cADPr hydrolase 1;
DE AltName: CD_antigen=CD38;
GN Name=CD38;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15383153; DOI=10.1186/1471-2172-5-21;
RA Ferrero E., Orciani M., Vacca P., Ortolan E., Crovella S., Titti F.,
RA Saccucci F., Malavasi F.;
RT "Characterization and phylogenetic epitope mapping of CD38 ADPR cyclase in
RT the cynomolgus macaque.";
RL BMC Immunol. 5:21-21(2004).
CC -!- FUNCTION: Synthesizes the second messengers cyclic ADP-ribose and
CC nicotinate-adenine dinucleotide phosphate, the former a second
CC messenger for glucose-induced insulin secretion. Also has cADPr
CC hydrolase activity. Also moonlights as a receptor in cells of the
CC immune system (By similarity). {ECO:0000250}.
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: ATP inhibits the hydrolyzing activity.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ADP-ribosyl cyclase family. {ECO:0000305}.
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DR EMBL; AY555148; AAT36330.1; -; mRNA.
DR RefSeq; NP_001274206.1; NM_001287277.1.
DR AlphaFoldDB; Q5VAN0; -.
DR SMR; Q5VAN0; -.
DR STRING; 9541.XP_005554571.1; -.
DR ABCD; Q5VAN0; 1 sequenced antibody.
DR Ensembl; ENSMFAT00000026853; ENSMFAP00000003193; ENSMFAG00000034115.
DR GeneID; 102126394; -.
DR CTD; 952; -.
DR VEuPathDB; HostDB:ENSMFAG00000034115; -.
DR eggNOG; ENOG502S1HV; Eukaryota.
DR GeneTree; ENSGT00390000017291; -.
DR OMA; MNYDSCP; -.
DR OrthoDB; 1460460at2759; -.
DR Proteomes; UP000233100; Chromosome 5.
DR Bgee; ENSMFAG00000034115; Expressed in thymus and 13 other tissues.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
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:0016849; F:phosphorus-oxygen lyase activity; IEA:Ensembl.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0042100; P:B cell proliferation; IEA:Ensembl.
DR GO; GO:0050853; P:B cell receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR CDD; cd04759; Rib_hydrolase; 1.
DR InterPro; IPR003193; ADP-ribosyl_cyclase.
DR InterPro; IPR033567; CD38.
DR PANTHER; PTHR10912; PTHR10912; 1.
DR PANTHER; PTHR10912:SF5; PTHR10912:SF5; 1.
DR Pfam; PF02267; Rib_hydrolayse; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Membrane; NAD; NADP; Receptor;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..301
FT /note="ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1"
FT /id="PRO_0000144067"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..43
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..301
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT ACT_SITE 120
FT /evidence="ECO:0000250"
FT ACT_SITE 202
FT /evidence="ECO:0000250"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 68..83
FT /evidence="ECO:0000250"
FT DISULFID 100..181
FT /evidence="ECO:0000250"
FT DISULFID 161..174
FT /evidence="ECO:0000250"
FT DISULFID 255..276
FT /evidence="ECO:0000250"
FT DISULFID 288..297
FT /evidence="ECO:0000250"
SQ 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
