CD38_MOUSE
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 03-AUG-2022, entry version 166.
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 P56528; P56528: Cd38; 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}.
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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 GlyGen; P56528; 4 sites, 8 N-linked glycans (3 sites).
DR iPTMnet; P56528; -.
DR PhosphoSitePlus; P56528; -.
DR SwissPalm; P56528; -.
DR jPOST; P56528; -.
DR PaxDb; P56528; -.
DR PeptideAtlas; P56528; -.
DR PRIDE; P56528; -.
DR ProteomicsDB; 280023; -.
DR Antibodypedia; 9844; 2499 antibodies from 55 providers.
DR DNASU; 12494; -.
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 VEuPathDB; HostDB:ENSMUSG00000029084; -.
DR eggNOG; ENOG502S1HV; Eukaryota.
DR GeneTree; ENSGT00390000017291; -.
DR HOGENOM; CLU_067834_0_1_1; -.
DR InParanoid; P56528; -.
DR OMA; MNYDSCP; -.
DR OrthoDB; 1460460at2759; -.
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 75 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 209 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: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: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: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: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 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: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
