CD38_RAT
ID CD38_RAT Reviewed; 303 AA.
AC Q64244;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 160.
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=CD38H;
DE AltName: Full=Cyclic ADP-ribose hydrolase 1;
DE Short=cADPr hydrolase 1;
DE AltName: CD_antigen=CD38;
GN Name=Cd38;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=8037769; DOI=10.1006/bbrc.1994.1974;
RA Li Q., Yamada Y., Yasuda K., Ihara Y., Okamoto Y., Kaisaki P.J.,
RA Watanabe R., Ikeda H., Tsuda K., Seino Y.;
RT "A cloned rat CD38-homologous protein and its expression in pancreatic
RT islets.";
RL Biochem. Biophys. Res. Commun. 202:629-636(1994).
RN [2]
RP ERRATUM OF PUBMED:8037769.
RA Li Q., Yamada Y., Yasuda K., Ihara Y., Okamoto Y., Kaisaki P.J.,
RA Watanabe R., Ikeda H., Tsuda K., Seino Y.;
RL Biochem. Biophys. Res. Commun. 204:1001-1001(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Pancreatic islet;
RX PubMed=8061050; DOI=10.1016/0167-4889(94)90087-6;
RA Koguma T., Takasawa S., Tohgo A., Karasawa T., Furuya Y., Yonekura H.,
RA Okamoto H.;
RT "Cloning and characterization of cDNA encoding rat ADP-ribosyl
RT cyclase/cyclic ADP-ribose hydrolase (homologue to human CD38) from islets
RT of Langerhans.";
RL Biochim. Biophys. Acta 1223:160-162(1994).
RN [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=10477767; DOI=10.1083/jcb.146.5.1161;
RA Sun L., Adebanjo O.A., Moonga B.S., Corisdeo S., Anandatheerthavarada H.K.,
RA Biswas G., Arakawa T., Hakeda Y., Koval A., Sodam B., Bevis P.J.R.,
RA Moser A.J., Lai F.A., Epstein S., Troen B.R., Kumegawa M., Zaidi M.;
RT "CD38/ADP-ribosyl cyclase: a new role in the regulation of osteoclastic
RT bone resorption.";
RL J. Cell Biol. 146:1161-1172(1999).
RN [5]
RP ERRATUM OF PUBMED:10477767.
RA Sun L., Adebanjo O.A., Moonga B.S., Corisdeo S., Anandatheerthavarada H.K.,
RA Biswas G., Arakawa T., Hakeda Y., Koval A., Sodam B., Bevis P.J.R.,
RA Moser A.J., Lai F.A., Epstein S., Troen B.R., Kumegawa M., Zaidi M.;
RL J. Cell Biol. 146:1391-1392(1999).
RN [6]
RP FUNCTION IN SYNTHESIS OF NICOTINIC ACID-ADENINE DINUCLEOTIDE PHOSPHATE.
RX PubMed=11829748; DOI=10.1042/0264-6021:3620125;
RA Chini E.N., Chini C.C., Kato I., Takasawa S., Okamoto H.;
RT "CD38 is the major enzyme responsible for synthesis of nicotinic acid-
RT adenine dinucleotide phosphate in mammalian tissues.";
RL Biochem. J. 362:125-130(2002).
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.
CC -!- FUNCTION: Regulates osteoclastic bone resorption, probably via
CC production of cyclic ADP-ribose and triggering of a cytosolic calcium
CC ion signal through ryanodine receptor activation.
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 -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.
CC -!- TISSUE SPECIFICITY: Spleen, liver, heart, thymus, thyroid gland, ileum,
CC colon, cerebellum, salivary gland, adrenal gland, jejunum, islets of
CC Langerhans and osteoclasts. {ECO:0000269|PubMed:10477767}.
CC -!- SIMILARITY: Belongs to the ADP-ribosyl cyclase family. {ECO:0000305}.
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DR EMBL; D30795; BAA06457.1; -; mRNA.
DR EMBL; D29646; BAA06129.1; -; mRNA.
DR PIR; JC2410; JC2410.
DR RefSeq; NP_037259.1; NM_013127.1.
DR AlphaFoldDB; Q64244; -.
DR SMR; Q64244; -.
DR STRING; 10116.ENSRNOP00000004121; -.
DR GlyGen; Q64244; 4 sites, 4 N-linked glycans (1 site).
DR iPTMnet; Q64244; -.
DR PhosphoSitePlus; Q64244; -.
DR SwissPalm; Q64244; -.
DR PaxDb; Q64244; -.
DR Ensembl; ENSRNOT00000004121; ENSRNOP00000004121; ENSRNOG00000003069.
DR GeneID; 25668; -.
DR KEGG; rno:25668; -.
DR CTD; 952; -.
DR RGD; 2303; Cd38.
DR eggNOG; ENOG502S1HV; Eukaryota.
DR GeneTree; ENSGT00390000017291; -.
DR HOGENOM; CLU_067834_0_1_1; -.
DR InParanoid; Q64244; -.
DR OMA; MNYDSCP; -.
DR OrthoDB; 1460460at2759; -.
DR PhylomeDB; Q64244; -.
DR TreeFam; TF332530; -.
DR BRENDA; 2.4.99.20; 5301.
DR Reactome; R-RNO-196807; Nicotinate metabolism.
DR SABIO-RK; Q64244; -.
DR PRO; PR:Q64244; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000003069; Expressed in spleen and 18 other tissues.
DR Genevisible; Q64244; RN.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0030667; C:secretory granule membrane; IDA:RGD.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0050135; F:NAD(P)+ nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0003953; F:NAD+ nucleosidase activity; IDA:RGD.
DR GO; GO:0061809; F:NAD+ nucleotidase, cyclic ADP-ribose generating; IEA:UniProtKB-EC.
DR GO; GO:0016849; F:phosphorus-oxygen lyase activity; ISO:RGD.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0014824; P:artery smooth muscle contraction; IMP:RGD.
DR GO; GO:0042100; P:B cell proliferation; IEA:Ensembl.
DR GO; GO:0050853; P:B cell receptor signaling pathway; ISO:RGD.
DR GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR GO; GO:0060292; P:long-term synaptic depression; IMP:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:0045779; P:negative regulation of bone resorption; IDA:RGD.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IMP:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; ISO:RGD.
DR GO; GO:0030307; P:positive regulation of cell growth; IMP:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IMP:RGD.
DR GO; GO:0032024; P:positive regulation of insulin secretion; IMP:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; IMP:RGD.
DR GO; GO:0034097; P:response to cytokine; IEP:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0009725; P:response to hormone; IDA:RGD.
DR GO; GO:0033194; P:response to hydroperoxide; IDA:RGD.
DR GO; GO:0001666; P:response to hypoxia; IDA:RGD.
DR GO; GO:0070555; P:response to interleukin-1; IEP:RGD.
DR GO; GO:0032570; P:response to progesterone; IEP:RGD.
DR GO; GO:0032526; P:response to retinoic acid; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:RGD.
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 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Hydrolase; Membrane; NAD; NADP;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..303
FT /note="ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1"
FT /id="PRO_0000144070"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..44
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..303
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT ACT_SITE 122
FT /evidence="ECO:0000250"
FT ACT_SITE 204
FT /evidence="ECO:0000250"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 69..85
FT /evidence="ECO:0000250"
FT DISULFID 102..183
FT /evidence="ECO:0000250"
FT DISULFID 163..176
FT /evidence="ECO:0000250"
FT DISULFID 257..278
FT /evidence="ECO:0000250"
FT DISULFID 290..299
FT /evidence="ECO:0000250"
SQ 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
