ID CD38_MOUSE Reviewed; 304 AA. AC P56528; Q8BFY8; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 2. DT 26-FEB-2020, entry version 154. 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: Full=I-19; DE AltName: Full=NIM-R5 antigen; DE AltName: CD_antigen=CD38; GN Name=Cd38; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=B-cell; RX PubMed=8376770; RA Harada N., Santos-Argumedo L., Chang R., Grimaldi J.C., Lund F.E., RA Brannan C.I., Copeland N.G., Jenkins N.A., Heath A.W., Parkhouse R.M.E., RA Howard M.; RT "Expression cloning of a cDNA encoding a novel murine B cell activation RT marker. Homology to human CD38."; RL J. Immunol. 151:3111-3118(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Hypothalamus, and Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Olfactory epithelium; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] 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). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and Spleen; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 48-288, AND DISULFIDE BONDS. RG RIKEN structural genomics initiative (RSGI); RT "Crystal structure of the truncated extracellular domain of mouse Cd38."; RL Submitted (FEB-2009) to the PDB data bank. 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 (By similarity). {ECO:0000250, CC ECO:0000269|PubMed:11829748}. 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 -!- INTERACTION: CC Self; NbExp=5; IntAct=EBI-8401721, EBI-8401721; CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. CC -!- SIMILARITY: Belongs to the ADP-ribosyl cyclase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L11332; AAA03163.1; -; mRNA. DR EMBL; AK038439; BAC30000.1; -; mRNA. DR EMBL; AK040498; BAC30607.1; -; mRNA. DR EMBL; AK042970; BAC31423.1; -; mRNA. DR EMBL; BC046312; AAH46312.1; -; mRNA. DR CCDS; CCDS19265.1; -. DR PIR; I49586; I49586. DR RefSeq; NP_031672.2; NM_007646.5. DR PDB; 2EG9; X-ray; 2.80 A; A/B=48-288. DR PDBsum; 2EG9; -. DR SMR; P56528; -. DR BioGrid; 198590; 1. DR DIP; DIP-59864N; -. DR IntAct; P56528; 1. DR MINT; P56528; -. DR STRING; 10090.ENSMUSP00000030964; -. DR BindingDB; P56528; -. DR ChEMBL; CHEMBL3425388; -. DR GlyConnect; 2113; -. DR iPTMnet; P56528; -. DR PhosphoSitePlus; P56528; -. DR SwissPalm; P56528; -. DR jPOST; P56528; -. DR PaxDb; P56528; -. DR PeptideAtlas; P56528; -. DR PRIDE; P56528; -. DR Ensembl; ENSMUST00000030964; ENSMUSP00000030964; ENSMUSG00000029084. DR GeneID; 12494; -. DR KEGG; mmu:12494; -. DR UCSC; uc008xic.2; mouse. DR CTD; 952; -. DR MGI; MGI:107474; Cd38. DR eggNOG; ENOG410IH8E; Eukaryota. DR eggNOG; ENOG4111W33; LUCA. DR GeneTree; ENSGT00390000017291; -. DR HOGENOM; CLU_067834_0_1_1; -. DR InParanoid; P56528; -. DR KO; K01242; -. DR OMA; EMNYQSC; -. DR OrthoDB; 1460460at2759; -. DR PhylomeDB; P56528; -. DR TreeFam; TF332530; -. DR BRENDA; 2.4.99.20; 3474. DR Reactome; R-MMU-196807; Nicotinate metabolism. DR ChiTaRS; Cd38; mouse. DR EvolutionaryTrace; P56528; -. DR PRO; PR:P56528; -. DR Proteomes; UP000000589; Chromosome 5. DR RNAct; P56528; protein. DR Bgee; ENSMUSG00000029084; Expressed in stroma of bone marrow and 251 other tissues. DR ExpressionAtlas; P56528; baseline and differential. DR Genevisible; P56528; MM. DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0009986; C:cell surface; IDA:MGI. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI. DR GO; GO:0016020; C:membrane; IDA:MGI. DR GO; GO:0005634; C:nucleus; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; ISO:MGI. DR GO; GO:0030667; C:secretory granule membrane; ISO:MGI. DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IMP:MGI. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0050135; F:NAD(P)+ nucleosidase activity; IEA:UniProtKB-EC. DR GO; GO:0003953; F:NAD+ nucleosidase activity; ISO:MGI. DR GO; GO:0061809; F:NAD+ nucleotidase, cyclic ADP-ribose generating; IEA:UniProtKB-EC. DR GO; GO:0016849; F:phosphorus-oxygen lyase activity; IMP:MGI. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0014824; P:artery smooth muscle contraction; ISO:MGI. DR GO; GO:0050853; P:B cell receptor signaling pathway; ISO:MGI. DR GO; GO:0007565; P:female pregnancy; IEA:Ensembl. DR GO; GO:0060292; P:long-term synaptic depression; ISO:MGI. DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI. DR GO; GO:0045779; P:negative regulation of bone resorption; ISO:MGI. DR GO; GO:0010977; P:negative regulation of neuron projection development; ISO:MGI. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI. DR GO; GO:0030890; P:positive regulation of B cell proliferation; IDA:MGI. DR GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI. DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI. DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI. DR GO; GO:0032024; P:positive regulation of insulin secretion; ISO:MGI. DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI. DR GO; GO:0045907; P:positive regulation of vasoconstriction; ISO:MGI. DR GO; GO:0042493; P:response to drug; ISO:MGI. DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl. DR GO; GO:0009725; P:response to hormone; ISO:MGI. DR GO; GO:0033194; P:response to hydroperoxide; ISO:MGI. DR GO; GO:0001666; P:response to hypoxia; ISO:MGI. DR GO; GO:0070555; P:response to interleukin-1; IEA:Ensembl. DR GO; GO:0032570; P:response to progesterone; IEA:Ensembl. DR GO; GO:0032526; P:response to retinoic acid; 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 1: Evidence at protein level; KW 3D-structure; Disulfide bond; Glycoprotein; Hydrolase; Membrane; NAD; NADP; KW Reference proteome; Signal-anchor; Transferase; Transmembrane; KW Transmembrane helix. FT CHAIN 1..304 FT /note="ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1" FT /id="PRO_0000144068" 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..304 FT /note="Extracellular" FT /evidence="ECO:0000255" FT ACT_SITE 123 FT /evidence="ECO:0000250" FT ACT_SITE 205 FT /evidence="ECO:0000250" FT CARBOHYD 104 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 124 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 213 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 223 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 70..86 FT /evidence="ECO:0000269|Ref.6" FT DISULFID 103..184 FT /evidence="ECO:0000269|Ref.6" FT DISULFID 164..177 FT /evidence="ECO:0000269|Ref.6" FT DISULFID 258..279 FT /evidence="ECO:0000269|Ref.6" FT DISULFID 291..300 FT /evidence="ECO:0000269|Ref.6" FT CONFLICT 191 FT /note="V -> M (in Ref. 1; AAA03163)" FT /evidence="ECO:0000305" FT CONFLICT 229 FT /note="V -> L (in Ref. 1; AAA03163)" FT /evidence="ECO:0000305" FT HELIX 62..75 FT /evidence="ECO:0000244|PDB:2EG9" FT HELIX 79..81 FT /evidence="ECO:0000244|PDB:2EG9" FT HELIX 86..97 FT /evidence="ECO:0000244|PDB:2EG9" FT HELIX 107..110 FT /evidence="ECO:0000244|PDB:2EG9" FT HELIX 111..116 FT /evidence="ECO:0000244|PDB:2EG9" FT HELIX 149..151 FT /evidence="ECO:0000244|PDB:2EG9" FT HELIX 153..158 FT /evidence="ECO:0000244|PDB:2EG9" FT HELIX 188..203 FT /evidence="ECO:0000244|PDB:2EG9" FT STRAND 206..219 FT /evidence="ECO:0000244|PDB:2EG9" FT HELIX 225..228 FT /evidence="ECO:0000244|PDB:2EG9" FT HELIX 230..233 FT /evidence="ECO:0000244|PDB:2EG9" FT TURN 236..238 FT /evidence="ECO:0000244|PDB:2EG9" FT STRAND 239..247 FT /evidence="ECO:0000244|PDB:2EG9" FT STRAND 250..252 FT /evidence="ECO:0000244|PDB:2EG9" FT HELIX 257..259 FT /evidence="ECO:0000244|PDB:2EG9" FT HELIX 261..271 FT /evidence="ECO:0000244|PDB:2EG9" FT TURN 272..274 FT /evidence="ECO:0000244|PDB:2EG9" FT STRAND 276..282 FT /evidence="ECO:0000244|PDB:2EG9" SQ SEQUENCE 304 AA; 34408 MW; DD0A7747C5F67D6F CRC64; MANYEFSQVS GDRPGCRLSR KAQIGLGVGL LVLIALVVGI VVILLRPRSL LVWTGEPTTK HFSDIFLGRC LIYTQILRPE MRDQNCQEIL STFKGAFVSK NPCNITREDY APLVKLVTQT IPCNKTLFWS KSKHLAHQYT WIQGKMFTLE DTLLGYIADD LRWCGDPSTS DMNYVSCPHW SENCPNNPIT VFWKVISQKF AEDACGVVQV MLNGSLREPF YKNSTFGSVE VFSLDPNKVH KLQAWVMHDI EGASSNACSS SSLNELKMIV QKRNMIFACV DNYRPARFLQ CVKNPEHPSC RLNT //