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   27-MAR-2024, entry version 175.
DE   RecName: Full=ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1;
DE            EC=3.2.2.- {ECO:0000269|PubMed:11829748};
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 {ECO:0000269|PubMed:11829748};
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 {ECO:0000303|PubMed:8376770};
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 CYCLIC ADP-RIBOSE AND NICOTINIC ACID-ADENINE
RP   DINUCLEOTIDE PHOSPHATE, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
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 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 (cADPR)
CC       and nicotinate-adenine dinucleotide phosphate (NAADP), the former a
CC       second messenger for glucose-induced insulin secretion, the latter a
CC       Ca(2+) mobilizer (PubMed:11829748). Also has cADPR hydrolase activity
CC       (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P28907,
CC       ECO:0000269|PubMed:11829748}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) = cyclic ADP-beta-D-ribose + H(+) + nicotinamide;
CC         Xref=Rhea:RHEA:38611, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:73672;
CC         Evidence={ECO:0000269|PubMed:11829748};
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; Evidence={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   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P28907}.
CC   -!- INTERACTION:
CC       P56528; P56528: Cd38; NbExp=5; IntAct=EBI-8401721, EBI-8401721;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:11829748,
CC       ECO:0000305|PubMed:8376770}; Single-pass type II membrane protein
CC       {ECO:0000305|PubMed:8376770}.
CC   -!- DISRUPTION PHENOTYPE: Loss of cADPR and NAADP synthesis.
CC       {ECO:0000269|PubMed:11829748}.
CC   -!- SIMILARITY: Belongs to the ADP-ribosyl cyclase family. {ECO:0000305}.
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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   AlphaFoldDB; P56528; -.
DR   SMR; P56528; -.
DR   BioGRID; 198590; 1.
DR   DIP; DIP-59864N; -.
DR   STRING; 10090.ENSMUSP00000030964; -.
DR   BindingDB; P56528; -.
DR   ChEMBL; CHEMBL3425388; -.
DR   GlyConnect; 2113; 9 N-Linked glycans (3 sites).
DR   GlyCosmos; P56528; 4 sites, 8 glycans.
DR   GlyGen; P56528; 4 sites, 8 N-linked glycans (3 sites).
DR   iPTMnet; P56528; -.
DR   PhosphoSitePlus; P56528; -.
DR   SwissPalm; P56528; -.
DR   jPOST; P56528; -.
DR   PaxDb; 10090-ENSMUSP00000030964; -.
DR   PeptideAtlas; P56528; -.
DR   ProteomicsDB; 280023; -.
DR   Antibodypedia; 9844; 3057 antibodies from 56 providers.
DR   DNASU; 12494; -.
DR   Ensembl; ENSMUST00000030964.6; ENSMUSP00000030964.5; ENSMUSG00000029084.6.
DR   GeneID; 12494; -.
DR   KEGG; mmu:12494; -.
DR   UCSC; uc008xic.2; mouse.
DR   AGR; MGI:107474; -.
DR   CTD; 952; -.
DR   MGI; MGI:107474; Cd38.
DR   VEuPathDB; HostDB:ENSMUSG00000029084; -.
DR   eggNOG; ENOG502S1HV; Eukaryota.
DR   GeneTree; ENSGT00390000017291; -.
DR   HOGENOM; CLU_067834_0_1_1; -.
DR   InParanoid; P56528; -.
DR   OMA; FWKVISQ; -.
DR   OrthoDB; 4265952at2759; -.
DR   PhylomeDB; P56528; -.
DR   TreeFam; TF332530; -.
DR   BRENDA; 2.4.99.20; 3474.
DR   BRENDA; 3.2.2.6; 3474.
DR   Reactome; R-MMU-196807; Nicotinate metabolism.
DR   BioGRID-ORCS; 12494; 1 hit in 80 CRISPR screens.
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 210 other cell types or tissues.
DR   ExpressionAtlas; P56528; baseline and differential.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR   GO; GO:0009986; C:cell surface; IDA:MGI.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0005886; C:plasma 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:0042100; P:B cell proliferation; IDA: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:0045892; P:negative regulation of DNA-templated transcription; ISO:MGI.
DR   GO; GO:0010977; P:negative regulation of neuron projection development; 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:0045893; P:positive regulation of DNA-templated transcription; ISO:MGI.
DR   GO; GO:0032024; P:positive regulation of insulin secretion; ISO:MGI.
DR   GO; GO:0045907; P:positive regulation of vasoconstriction; 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   GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
DR   CDD; cd04759; Rib_hydrolase; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR003193; ADP-ribosyl_cyclase.
DR   PANTHER; PTHR10912; ADP-RIBOSYL CYCLASE; 1.
DR   PANTHER; PTHR10912:SF5; ADP-RIBOSYL CYCLASE_CYCLIC ADP-RIBOSE HYDROLASE 1; 1.
DR   Pfam; PF02267; Rib_hydrolayse; 1.
DR   SUPFAM; SSF52309; N-(deoxy)ribosyltransferase-like; 1.
DR   Genevisible; P56528; MM.
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:0007829|PDB:2EG9"
FT   HELIX           79..81
FT                   /evidence="ECO:0007829|PDB:2EG9"
FT   HELIX           86..97
FT                   /evidence="ECO:0007829|PDB:2EG9"
FT   HELIX           107..110
FT                   /evidence="ECO:0007829|PDB:2EG9"
FT   HELIX           111..116
FT                   /evidence="ECO:0007829|PDB:2EG9"
FT   HELIX           149..151
FT                   /evidence="ECO:0007829|PDB:2EG9"
FT   HELIX           153..158
FT                   /evidence="ECO:0007829|PDB:2EG9"
FT   HELIX           188..203
FT                   /evidence="ECO:0007829|PDB:2EG9"
FT   STRAND          206..219
FT                   /evidence="ECO:0007829|PDB:2EG9"
FT   HELIX           225..228
FT                   /evidence="ECO:0007829|PDB:2EG9"
FT   HELIX           230..233
FT                   /evidence="ECO:0007829|PDB:2EG9"
FT   TURN            236..238
FT                   /evidence="ECO:0007829|PDB:2EG9"
FT   STRAND          239..247
FT                   /evidence="ECO:0007829|PDB:2EG9"
FT   STRAND          250..252
FT                   /evidence="ECO:0007829|PDB:2EG9"
FT   HELIX           257..259
FT                   /evidence="ECO:0007829|PDB:2EG9"
FT   HELIX           261..271
FT                   /evidence="ECO:0007829|PDB:2EG9"
FT   TURN            272..274
FT                   /evidence="ECO:0007829|PDB:2EG9"
FT   STRAND          276..282
FT                   /evidence="ECO:0007829|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
//