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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) (CD38H) (Cyclic ADP-ribose hydrolase 1) (cADPr hydrolase 1) (CD antigen CD38)

 CD38_RAT                Reviewed;         303 AA.
Q64244;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
23-MAY-2018, entry version 141.
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=CD38H;
AltName: Full=Cyclic ADP-ribose hydrolase 1;
Short=cADPr hydrolase 1;
AltName: CD_antigen=CD38;
Name=Cd38;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Wistar; TISSUE=Brain;
PubMed=8037769; DOI=10.1006/bbrc.1994.1974;
Li Q., Yamada Y., Yasuda K., Ihara Y., Okamoto Y., Kaisaki P.J.,
Watanabe R., Ikeda H., Tsuda K., Seino Y.;
"A cloned rat CD38-homologous protein and its expression in pancreatic
islets.";
Biochem. Biophys. Res. Commun. 202:629-636(1994).
[2]
ERRATUM.
Li Q., Yamada Y., Yasuda K., Ihara Y., Okamoto Y., Kaisaki P.J.,
Watanabe R., Ikeda H., Tsuda K., Seino Y.;
Biochem. Biophys. Res. Commun. 204:1001-1001(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Wistar; TISSUE=Pancreatic islet;
PubMed=8061050; DOI=10.1016/0167-4889(94)90087-6;
Koguma T., Takasawa S., Tohgo A., Karasawa T., Furuya Y., Yonekura H.,
Okamoto H.;
"Cloning and characterization of cDNA encoding rat ADP-ribosyl
cyclase/cyclic ADP-ribose hydrolase (homologue to human CD38) from
islets of Langerhans.";
Biochim. Biophys. Acta 1223:160-162(1994).
[4]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=10477767; DOI=10.1083/jcb.146.5.1161;
Sun L., Adebanjo O.A., Moonga B.S., Corisdeo S.,
Anandatheerthavarada H.K., Biswas G., Arakawa T., Hakeda Y., Koval A.,
Sodam B., Bevis P.J.R., Moser A.J., Lai F.A., Epstein S., Troen B.R.,
Kumegawa M., Zaidi M.;
"CD38/ADP-ribosyl cyclase: a new role in the regulation of
osteoclastic bone resorption.";
J. Cell Biol. 146:1161-1172(1999).
[5]
ERRATUM.
Sun L., Adebanjo O.A., Moonga B.S., Corisdeo S.,
Anandatheerthavarada H.K., Biswas G., Arakawa T., Hakeda Y., Koval A.,
Sodam B., Bevis P.J.R., Moser A.J., Lai F.A., Epstein S., Troen B.R.,
Kumegawa M., Zaidi M.;
J. Cell Biol. 146:1391-1392(1999).
[6]
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).
-!- 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.
-!- FUNCTION: Regulates osteoclastic bone resorption, probably via
production of cyclic ADP-ribose and triggering of a cytosolic
calcium ion signal through ryanodine receptor activation.
-!- CATALYTIC ACTIVITY: NAD(+) + H(2)O = ADP-D-ribose + nicotinamide.
-!- CATALYTIC ACTIVITY: NADP(+) + nicotinate = nicotinate-adenine
dinucleotide phosphate + nicotinamide.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane
protein.
-!- TISSUE SPECIFICITY: Spleen, liver, heart, thymus, thyroid gland,
ileum, colon, cerebellum, salivary gland, adrenal gland, jejunum,
islets of Langerhans and osteoclasts.
{ECO:0000269|PubMed:10477767}.
-!- SIMILARITY: Belongs to the ADP-ribosyl cyclase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; D30795; BAA06457.1; -; mRNA.
EMBL; D29646; BAA06129.1; -; mRNA.
PIR; JC2410; JC2410.
RefSeq; NP_037259.1; NM_013127.1.
UniGene; Rn.11414; -.
ProteinModelPortal; Q64244; -.
SMR; Q64244; -.
STRING; 10116.ENSRNOP00000004121; -.
iPTMnet; Q64244; -.
PhosphoSitePlus; Q64244; -.
SwissPalm; Q64244; -.
UniCarbKB; Q64244; -.
PaxDb; Q64244; -.
PRIDE; Q64244; -.
Ensembl; ENSRNOT00000004121; ENSRNOP00000004121; ENSRNOG00000003069.
GeneID; 25668; -.
KEGG; rno:25668; -.
CTD; 952; -.
RGD; 2303; Cd38.
eggNOG; ENOG410IH8E; Eukaryota.
eggNOG; ENOG4111W33; LUCA.
GeneTree; ENSGT00390000017291; -.
HOGENOM; HOG000293141; -.
HOVERGEN; HBG005277; -.
InParanoid; Q64244; -.
KO; K01242; -.
OMA; QCVKNPE; -.
OrthoDB; EOG091G0GI3; -.
PhylomeDB; Q64244; -.
TreeFam; TF332530; -.
BRENDA; 2.4.99.20; 5301.
Reactome; R-RNO-196807; Nicotinate metabolism.
SABIO-RK; Q64244; -.
PRO; PR:Q64244; -.
Proteomes; UP000002494; Chromosome 14.
Bgee; ENSRNOG00000003069; -.
Genevisible; Q64244; RN.
GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0030667; C:secretory granule membrane; IDA:RGD.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0050135; F:NAD(P)+ nucleosidase activity; IEA:UniProtKB-EC.
GO; GO:0003953; F:NAD+ nucleosidase activity; IDA:RGD.
GO; GO:0061809; F:NAD+ nucleotidase, cyclic ADP-ribose generating; IEA:UniProtKB-EC.
GO; GO:0016849; F:phosphorus-oxygen lyase activity; IBA:GO_Central.
GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
GO; GO:0014824; P:artery smooth muscle contraction; IMP:RGD.
GO; GO:0050853; P:B cell receptor signaling pathway; IEA:Ensembl.
GO; GO:0007565; P:female pregnancy; IEP:RGD.
GO; GO:0060292; P:long term synaptic depression; IMP:RGD.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0045779; P:negative regulation of bone resorption; IDA:RGD.
GO; GO:0010977; P:negative regulation of neuron projection development; IMP:RGD.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl.
GO; GO:0030890; P:positive regulation of B cell proliferation; IBA:GO_Central.
GO; GO:0030307; P:positive regulation of cell growth; IMP:RGD.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:RGD.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IMP:RGD.
GO; GO:0032024; P:positive regulation of insulin secretion; IMP:RGD.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
GO; GO:0045907; P:positive regulation of vasoconstriction; IMP:RGD.
GO; GO:0034097; P:response to cytokine; IEP:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0009725; P:response to hormone; IDA:RGD.
GO; GO:0033194; P:response to hydroperoxide; IDA:RGD.
GO; GO:0001666; P:response to hypoxia; IDA:RGD.
GO; GO:0070555; P:response to interleukin-1; IEP:RGD.
GO; GO:0032570; P:response to progesterone; IEP:RGD.
GO; GO:0032526; P:response to retinoic acid; IEP:RGD.
CDD; cd04759; Rib_hydrolase; 1.
InterPro; IPR003193; ADP-ribosyl_cyclase.
InterPro; IPR033567; CD38.
PANTHER; PTHR10912; PTHR10912; 1.
PANTHER; PTHR10912:SF5; PTHR10912:SF5; 1.
Pfam; PF02267; Rib_hydrolayse; 1.
1: Evidence at protein level;
Complete proteome; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
NAD; NADP; Reference proteome; Signal-anchor; Transferase;
Transmembrane; Transmembrane helix.
CHAIN 1 303 ADP-ribosyl cyclase/cyclic ADP-ribose
hydrolase 1.
/FTId=PRO_0000144070.
TOPO_DOM 1 21 Cytoplasmic. {ECO:0000255}.
TRANSMEM 22 44 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 45 303 Extracellular. {ECO:0000255}.
ACT_SITE 122 122 {ECO:0000250}.
ACT_SITE 204 204 {ECO:0000250}.
CARBOHYD 103 103 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 123 123 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 212 212 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 222 222 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 69 85 {ECO:0000250}.
DISULFID 102 183 {ECO:0000250}.
DISULFID 163 176 {ECO:0000250}.
DISULFID 257 278 {ECO:0000250}.
DISULFID 290 299 {ECO:0000250}.
SEQUENCE 303 AA; 34436 MW; 84F23AD3094871C5 CRC64;
MANYEFSQVS EDRPGCRLTR KAQIGLGVGL LLLVALVVVV VIVLWPRSPL VWKGKPTTKH
FADIILGRCL IYTQILRPEM RDQDCKKILS TFKRGFISKN PCNITNEDYA PLVKLVTQTI
PCNKTLFWSK SKHLAHQYTW IQGKMFTLED TLLGYIADDL RWCGDPSTSD MNYDSCPHWS
ENCPNNPVAV FWNVISQKFA EDACGVVQVM LNGSLSEPFY RNSTFGSVEV FNLDPNKVHK
LQAWVMHDIK GTSSNACSSP SINELKSIVN KRNMIFACQD NYRPVRFLQC VKNPEHPSCR
LNV


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