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 12-SEP-2018, entry version 144. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; 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., RA Parkhouse R.M.E., Howard M.; RT "Expression cloning of a cDNA encoding a novel murine B cell RT activation 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP FUNCTION IN SYNTHESIS OF NICOTINIC ACID-ADENINE DINUCLEOTIDE RP 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 RC 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 RT 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 RT Cd38."; RL Submitted (FEB-2009) to the PDB data bank. CC -!- FUNCTION: Synthesizes the second messagers 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: NAD(+) + H(2)O = ADP-D-ribose + nicotinamide. CC -!- CATALYTIC ACTIVITY: NADP(+) + nicotinate = nicotinate-adenine CC dinucleotide phosphate + nicotinamide. CC -!- INTERACTION: CC Self; NbExp=5; IntAct=EBI-8401721, EBI-8401721; CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane CC protein. CC -!- SIMILARITY: Belongs to the ADP-ribosyl cyclase family. CC {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 UniGene; Mm.249873; -. DR PDB; 2EG9; X-ray; 2.80 A; A/B=48-288. DR PDBsum; 2EG9; -. DR ProteinModelPortal; P56528; -. 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 iPTMnet; P56528; -. DR PhosphoSitePlus; P56528; -. DR SwissPalm; 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; HOG000293141; -. DR HOVERGEN; HBG005277; -. DR InParanoid; P56528; -. DR KO; K01242; -. DR OMA; QCVKNPE; -. DR OrthoDB; EOG091G0GI3; -. 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 Bgee; ENSMUSG00000029084; Expressed in 252 organ(s), highest expression level in stroma of bone marrow. DR CleanEx; MM_CD38; -. DR ExpressionAtlas; P56528; baseline and differential. DR Genevisible; P56528; MM. DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI. 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 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; Complete proteome; Disulfide bond; Glycoprotein; KW Hydrolase; Membrane; NAD; NADP; Reference proteome; Signal-anchor; KW Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1 304 ADP-ribosyl cyclase/cyclic ADP-ribose FT hydrolase 1. FT /FTId=PRO_0000144068. FT TOPO_DOM 1 21 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 22 44 Helical; Signal-anchor for type II FT membrane protein. {ECO:0000255}. FT TOPO_DOM 45 304 Extracellular. {ECO:0000255}. FT ACT_SITE 123 123 {ECO:0000250}. FT ACT_SITE 205 205 {ECO:0000250}. FT CARBOHYD 104 104 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 124 124 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 213 213 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 223 223 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 70 86 {ECO:0000269|Ref.6}. FT DISULFID 103 184 {ECO:0000269|Ref.6}. FT DISULFID 164 177 {ECO:0000269|Ref.6}. FT DISULFID 258 279 {ECO:0000269|Ref.6}. FT DISULFID 291 300 {ECO:0000269|Ref.6}. FT CONFLICT 191 191 V -> M (in Ref. 1; AAA03163). FT {ECO:0000305}. FT CONFLICT 229 229 V -> L (in Ref. 1; AAA03163). FT {ECO:0000305}. FT HELIX 62 75 {ECO:0000244|PDB:2EG9}. FT HELIX 79 81 {ECO:0000244|PDB:2EG9}. FT HELIX 86 97 {ECO:0000244|PDB:2EG9}. FT HELIX 107 110 {ECO:0000244|PDB:2EG9}. FT HELIX 111 116 {ECO:0000244|PDB:2EG9}. FT HELIX 149 151 {ECO:0000244|PDB:2EG9}. FT HELIX 153 158 {ECO:0000244|PDB:2EG9}. FT HELIX 188 203 {ECO:0000244|PDB:2EG9}. FT STRAND 206 219 {ECO:0000244|PDB:2EG9}. FT HELIX 225 228 {ECO:0000244|PDB:2EG9}. FT HELIX 230 233 {ECO:0000244|PDB:2EG9}. FT TURN 236 238 {ECO:0000244|PDB:2EG9}. FT STRAND 239 247 {ECO:0000244|PDB:2EG9}. FT STRAND 250 252 {ECO:0000244|PDB:2EG9}. FT HELIX 257 259 {ECO:0000244|PDB:2EG9}. FT HELIX 261 271 {ECO:0000244|PDB:2EG9}. FT TURN 272 274 {ECO:0000244|PDB:2EG9}. FT STRAND 276 282 {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 //