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 11-JUN-2014, entry version 111. 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; Sciurognathi; 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 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). CC -!- CATALYTIC ACTIVITY: NAD(+) + H(2)O = ADP-D-ribose + nicotinamide. CC -!- CATALYTIC ACTIVITY: NADP(+) + nicotinate = nicotinate-adenine CC dinucleotide phosphate + nicotinamide. CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane CC protein. CC -!- SIMILARITY: Belongs to the ADP-ribosyl cyclase family. 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 PIR; I49586; I49586. DR RefSeq; NP_031672.2; NM_007646.4. 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; 50-283. DR BioGrid; 198590; 1. DR DIP; DIP-59864N; -. DR IntAct; P56528; 1. DR MINT; MINT-4090243; -. DR PhosphoSite; P56528; -. DR MaxQB; P56528; -. DR PaxDb; 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; NOG42596; -. DR HOGENOM; HOG000293141; -. DR HOVERGEN; HBG005277; -. DR InParanoid; P56528; -. DR KO; K01242; -. DR OMA; KNPCNIT; -. DR OrthoDB; EOG7RBZ9B; -. DR PhylomeDB; P56528; -. DR TreeFam; TF332530; -. DR ChiTaRS; CD38; mouse. DR EvolutionaryTrace; P56528; -. DR NextBio; 281424; -. DR PRO; PR:P56528; -. DR ArrayExpress; P56528; -. DR Bgee; P56528; -. DR CleanEx; MM_CD38; -. DR Genevestigator; P56528; -. DR GO; GO:0009986; C:cell surface; IDA:MGI. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016020; C:membrane; IDA:MGI. DR GO; GO:0005634; C:nucleus; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl. DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IMP:MGI. DR GO; GO:0050135; F:NAD(P)+ nucleosidase activity; IEA:UniProtKB-EC. DR GO; GO:0003953; F:NAD+ nucleosidase activity; IEA:Ensembl. DR GO; GO:0016849; F:phosphorus-oxygen lyase activity; IMP:MGI. DR GO; GO:0050853; P:B cell receptor signaling pathway; IEA:Ensembl. DR GO; GO:0007565; P:female pregnancy; IEA:Ensembl. DR GO; GO:0060292; P:long term synaptic depression; IEA:Ensembl. DR GO; GO:0008152; P:metabolic process; IMP:GOC. DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl. DR GO; GO:0045779; P:negative regulation of bone resorption; 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; IDA:MGI. DR GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl. DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl. DR GO; GO:0032024; P:positive regulation of insulin secretion; IEA:Ensembl. DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl. DR GO; GO:0045907; P:positive regulation of vasoconstriction; IEA:Ensembl. DR GO; GO:0042493; P:response to drug; IEA:Ensembl. DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl. DR GO; GO:0033194; P:response to hydroperoxide; IEA:Ensembl. DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl. 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 Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR003193; ADP-ribosyl_cyclase. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR10912; PTHR10912; 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 (Potential). FT TRANSMEM 22 44 Helical; Signal-anchor for type II FT membrane protein; (Potential). FT TOPO_DOM 45 304 Extracellular (Potential). FT ACT_SITE 123 123 By similarity. FT ACT_SITE 205 205 By similarity. FT CARBOHYD 104 104 N-linked (GlcNAc...) (Potential). FT CARBOHYD 124 124 N-linked (GlcNAc...) (Potential). FT CARBOHYD 213 213 N-linked (GlcNAc...) (Potential). FT CARBOHYD 223 223 N-linked (GlcNAc...) (Potential). FT DISULFID 70 86 FT DISULFID 103 184 FT DISULFID 164 177 FT DISULFID 258 279 FT DISULFID 291 300 FT CONFLICT 191 191 V -> M (in Ref. 1; AAA03163). FT CONFLICT 229 229 V -> L (in Ref. 1; AAA03163). FT HELIX 62 75 FT HELIX 79 81 FT HELIX 86 97 FT HELIX 107 110 FT HELIX 111 116 FT HELIX 149 151 FT HELIX 153 158 FT HELIX 188 203 FT STRAND 206 219 FT HELIX 225 228 FT HELIX 230 233 FT TURN 236 238 FT STRAND 239 247 FT STRAND 250 252 FT HELIX 257 259 FT HELIX 261 271 FT TURN 272 274 FT STRAND 276 282 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 //