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ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1 (EC 3.2.2.6) (2'-phospho-ADP-ribosyl cyclase) (2'-phospho-ADP-ribosyl cyclase/2'-phospho-cyclic-ADP-ribose transferase) (EC 2.4.99.20) (2'-phospho-cyclic-ADP-ribose transferase) (ADP-ribosyl cyclase 1) (ADPRC 1) (Cyclic ADP-ribose hydrolase 1) (cADPr hydrolase 1) (T10) (CD antigen CD38)

 CD38_HUMAN              Reviewed;         300 AA.
P28907; O00121; O00122; Q96HY4;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
23-NOV-2004, sequence version 2.
12-SEP-2018, entry version 188.
RecName: Full=ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1;
EC=3.2.2.6;
AltName: Full=2'-phospho-ADP-ribosyl cyclase;
AltName: Full=2'-phospho-ADP-ribosyl cyclase/2'-phospho-cyclic-ADP-ribose transferase;
EC=2.4.99.20;
AltName: Full=2'-phospho-cyclic-ADP-ribose transferase;
AltName: Full=ADP-ribosyl cyclase 1;
Short=ADPRC 1;
AltName: Full=Cyclic ADP-ribose hydrolase 1;
Short=cADPr hydrolase 1;
AltName: Full=T10;
AltName: CD_antigen=CD38;
Name=CD38;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2319135;
Jackson D.G., Bell J.I.;
"Isolation of a cDNA encoding the human CD38 (T10) molecule, a cell
surface glycoprotein with an unusual discontinuous pattern of
expression during lymphocyte differentiation.";
J. Immunol. 144:2811-2815(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], NUCLEOTIDE SEQUENCE [MRNA]
(ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
TISSUE=Esophageal carcinoma, and Pancreas;
PubMed=9074508; DOI=10.1016/S0378-1119(96)00723-8;
Nata K., Takamura T., Karasawa T., Kumagai T., Hashioka W., Tohgo A.,
Yonekura H., Takasawa S., Nakamura S., Okamoto H.;
"Human gene encoding CD38 (ADP-ribosyl cyclase/cyclic ADP-ribose
hydrolase): organization, nucleotide sequence and alternative
splicing.";
Gene 186:285-292(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=B-cell;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
SIMILARITY TO NADASE.
PubMed=1471258; DOI=10.1016/0968-0004(92)90337-9;
States D.J., Walseth T.F., Lee H.C.;
"Similarities in amino acid sequences of Aplysia ADP-ribosyl cyclase
and human lymphocyte antigen CD38.";
Trends Biochem. Sci. 17:495-495(1992).
[5]
CHARACTERIZATION.
PubMed=8253715;
Takasawa S., Tohgo A., Noguchi N., Koguma T., Nata K., Sugimoto T.,
Yonekura H., Okamoto H.;
"Synthesis and hydrolysis of cyclic ADP-ribose by human leukocyte
antigen CD38 and inhibition of the hydrolysis by ATP.";
J. Biol. Chem. 268:26052-26054(1993).
[6]
ACTIVE SITE, AND MUTAGENESIS OF CYS-119; CYS-160; CYS-173 AND CYS-201.
PubMed=7961800;
Tohgo A., Takasawa S., Noguchi N., Koguma T., Nata K., Sugimoto T.,
Furuya Y., Yonekura H., Okamoto H.;
"Essential cysteine residues for cyclic ADP-ribose synthesis and
hydrolysis by CD38.";
J. Biol. Chem. 269:28555-28557(1994).
[7]
SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
Hillman R.T., Green R.E., Brenner S.E.;
"An unappreciated role for RNA surveillance.";
Genome Biol. 5:R8.1-R8.16(2004).
[8]
CATALYTIC ACTIVITY.
PubMed=16690024; DOI=10.1016/j.bbrc.2006.04.096;
Moreschi I., Bruzzone S., Melone L., De Flora A., Zocchi E.;
"NAADP+ synthesis from cADPRP and nicotinic acid by ADP-ribosyl
cyclases.";
Biochem. Biophys. Res. Commun. 345:573-580(2006).
[9]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-100; ASN-209 AND ASN-219.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[10]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-219.
TISSUE=Leukemic T-cell;
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[13]
X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 45-300, AND DISULFIDE BONDS.
PubMed=16154090; DOI=10.1016/j.str.2005.05.012;
Liu Q., Kriksunov I.A., Graeff R., Munshi C., Lee H.C., Hao Q.;
"Crystal structure of human CD38 extracellular domain.";
Structure 13:1331-1339(2005).
[14]
VARIANT TRP-140.
PubMed=9754820; DOI=10.1007/s001250051026;
Yagui K., Shimada F., Mimura M., Hashimoto N., Suzuki Y., Tokuyama Y.,
Nata K., Tohgo A., Ikehata F., Takasawa S., Okamoto H., Makino H.,
Saito Y., Kanatsuka A.;
"A missense mutation in the CD38 gene, a novel factor for insulin
secretion: association with Type II diabetes mellitus in Japanese
subjects and evidence of abnormal function when expressed in vitro.";
Diabetologia 41:1024-1028(1998).
-!- FUNCTION: Synthesizes the second messagers cyclic ADP-ribose and
nicotinate-adenine dinucleotide phosphate, the former a second
messenger for glucose-induced insulin secretion. Also has cADPr
hydrolase activity. Also moonlights as a receptor in cells of the
immune system.
-!- CATALYTIC ACTIVITY: NAD(+) + H(2)O = ADP-D-ribose + nicotinamide.
{ECO:0000269|PubMed:16690024}.
-!- CATALYTIC ACTIVITY: NADP(+) + nicotinate = nicotinate-adenine
dinucleotide phosphate + nicotinamide.
{ECO:0000269|PubMed:16690024}.
-!- ACTIVITY REGULATION: ATP inhibits the hydrolyzing activity.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane
protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P28907-1; Sequence=Displayed;
Name=2;
IsoId=P28907-2; Sequence=VSP_000707, VSP_000708;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
-!- TISSUE SPECIFICITY: Expressed at high levels in pancreas, liver,
kidney, brain, testis, ovary, placenta, malignant lymphoma and
neuroblastoma. {ECO:0000269|PubMed:9074508}.
-!- DEVELOPMENTAL STAGE: Preferentially expressed at both early and
late stages of the B and T-cell maturation. It is also detected on
erythroid and myeloid progenitors in bone marrow, where the level
of surface expression was shown to decrease during differentiation
of blast-forming unit E to colony-forming unit E.
-!- SIMILARITY: Belongs to the ADP-ribosyl cyclase family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=CD38 entry;
URL="https://en.wikipedia.org/wiki/CD38";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CD38ID978ch4p15.html";
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EMBL; M34461; AAA68482.1; -; mRNA.
EMBL; D84276; BAA18964.1; -; mRNA.
EMBL; D84277; BAA18965.1; -; mRNA.
EMBL; D84284; BAA18966.1; -; Genomic_DNA.
EMBL; BC007964; AAH07964.1; -; mRNA.
CCDS; CCDS3417.1; -. [P28907-1]
PIR; A43521; A43521.
RefSeq; NP_001766.2; NM_001775.3. [P28907-1]
UniGene; Hs.479214; -.
PDB; 1YH3; X-ray; 1.91 A; A/B=45-300.
PDB; 1ZVM; X-ray; 2.20 A; A/B/C/D=45-300.
PDB; 2EF1; X-ray; 2.40 A; A/B=45-300.
PDB; 2HCT; X-ray; 1.95 A; A/B=45-300.
PDB; 2I65; X-ray; 1.90 A; A/B=45-300.
PDB; 2I66; X-ray; 1.70 A; A/B=45-300.
PDB; 2I67; X-ray; 1.71 A; A/B=45-300.
PDB; 2O3Q; X-ray; 1.98 A; A/B=45-300.
PDB; 2O3R; X-ray; 1.75 A; A/B=45-300.
PDB; 2O3S; X-ray; 1.50 A; A/B=45-300.
PDB; 2O3T; X-ray; 1.68 A; A/B=45-300.
PDB; 2O3U; X-ray; 2.11 A; A/B=45-300.
PDB; 2PGJ; X-ray; 1.71 A; A/B=45-300.
PDB; 2PGL; X-ray; 1.76 A; A/B=45-300.
PDB; 3DZF; X-ray; 2.01 A; A/B/C/D/E/F=45-300.
PDB; 3DZG; X-ray; 1.65 A; A/B=45-300.
PDB; 3DZH; X-ray; 1.60 A; A/B=45-300.
PDB; 3DZI; X-ray; 1.73 A; A/B=45-300.
PDB; 3DZJ; X-ray; 1.90 A; A/B=45-300.
PDB; 3DZK; X-ray; 1.81 A; A/B=45-300.
PDB; 3F6Y; X-ray; 1.45 A; A=45-300.
PDB; 3I9M; X-ray; 1.75 A; A/B=45-300.
PDB; 3I9N; X-ray; 2.01 A; A/B=45-300.
PDB; 3OFS; X-ray; 2.20 A; A/B/C/D/E/F=46-300.
PDB; 3RAJ; X-ray; 3.04 A; A=46-300.
PDB; 3ROK; X-ray; 1.65 A; A/B=45-296.
PDB; 3ROM; X-ray; 2.04 A; A/B=45-296.
PDB; 3ROP; X-ray; 1.94 A; A/B=45-296.
PDB; 3ROQ; X-ray; 2.10 A; A/B=45-296.
PDB; 3U4H; X-ray; 1.88 A; A/B=45-300.
PDB; 3U4I; X-ray; 2.12 A; A/B=45-300.
PDB; 4CMH; X-ray; 1.53 A; A=45-300.
PDB; 4F45; X-ray; 2.10 A; A/B=46-300.
PDB; 4F46; X-ray; 1.69 A; A/B=46-300.
PDB; 4OGW; X-ray; 2.05 A; A=46-300.
PDB; 4TMF; X-ray; 2.05 A; A/B=50-300.
PDB; 4XJS; X-ray; 2.80 A; A=46-300.
PDB; 4XJT; X-ray; 2.60 A; A=46-300.
PDB; 5F1K; X-ray; 2.30 A; A/B=45-300.
PDB; 5F1O; X-ray; 2.20 A; A=46-300.
PDB; 5F21; X-ray; 1.90 A; A=46-300.
PDBsum; 1YH3; -.
PDBsum; 1ZVM; -.
PDBsum; 2EF1; -.
PDBsum; 2HCT; -.
PDBsum; 2I65; -.
PDBsum; 2I66; -.
PDBsum; 2I67; -.
PDBsum; 2O3Q; -.
PDBsum; 2O3R; -.
PDBsum; 2O3S; -.
PDBsum; 2O3T; -.
PDBsum; 2O3U; -.
PDBsum; 2PGJ; -.
PDBsum; 2PGL; -.
PDBsum; 3DZF; -.
PDBsum; 3DZG; -.
PDBsum; 3DZH; -.
PDBsum; 3DZI; -.
PDBsum; 3DZJ; -.
PDBsum; 3DZK; -.
PDBsum; 3F6Y; -.
PDBsum; 3I9M; -.
PDBsum; 3I9N; -.
PDBsum; 3OFS; -.
PDBsum; 3RAJ; -.
PDBsum; 3ROK; -.
PDBsum; 3ROM; -.
PDBsum; 3ROP; -.
PDBsum; 3ROQ; -.
PDBsum; 3U4H; -.
PDBsum; 3U4I; -.
PDBsum; 4CMH; -.
PDBsum; 4F45; -.
PDBsum; 4F46; -.
PDBsum; 4OGW; -.
PDBsum; 4TMF; -.
PDBsum; 4XJS; -.
PDBsum; 4XJT; -.
PDBsum; 5F1K; -.
PDBsum; 5F1O; -.
PDBsum; 5F21; -.
ProteinModelPortal; P28907; -.
SMR; P28907; -.
BioGrid; 107390; 6.
STRING; 9606.ENSP00000226279; -.
BindingDB; P28907; -.
ChEMBL; CHEMBL4660; -.
DrugBank; DB09331; Daratumumab.
GuidetoPHARMACOLOGY; 2766; -.
iPTMnet; P28907; -.
PhosphoSitePlus; P28907; -.
SwissPalm; P28907; -.
BioMuta; CD38; -.
DMDM; 55977782; -.
EPD; P28907; -.
MaxQB; P28907; -.
PaxDb; P28907; -.
PeptideAtlas; P28907; -.
PRIDE; P28907; -.
ProteomicsDB; 54507; -.
ProteomicsDB; 54508; -. [P28907-2]
DNASU; 952; -.
Ensembl; ENST00000226279; ENSP00000226279; ENSG00000004468. [P28907-1]
Ensembl; ENST00000502843; ENSP00000427277; ENSG00000004468. [P28907-2]
GeneID; 952; -.
KEGG; hsa:952; -.
UCSC; uc003gol.2; human. [P28907-1]
CTD; 952; -.
DisGeNET; 952; -.
EuPathDB; HostDB:ENSG00000004468.12; -.
GeneCards; CD38; -.
HGNC; HGNC:1667; CD38.
HPA; CAB002493; -.
HPA; CAB025255; -.
HPA; HPA022132; -.
HPA; HPA052381; -.
MIM; 107270; gene.
neXtProt; NX_P28907; -.
OpenTargets; ENSG00000004468; -.
PharmGKB; PA26214; -.
eggNOG; ENOG410IH8E; Eukaryota.
eggNOG; ENOG4111W33; LUCA.
GeneTree; ENSGT00390000017291; -.
HOGENOM; HOG000293141; -.
HOVERGEN; HBG005277; -.
InParanoid; P28907; -.
KO; K01242; -.
OMA; QCVKNPE; -.
OrthoDB; EOG091G0GI3; -.
PhylomeDB; P28907; -.
TreeFam; TF332530; -.
BioCyc; MetaCyc:HS00103-MONOMER; -.
BRENDA; 2.4.99.20; 2681.
BRENDA; 3.2.2.5; 2681.
Reactome; R-HSA-196807; Nicotinate metabolism.
SABIO-RK; P28907; -.
ChiTaRS; CD38; human.
EvolutionaryTrace; P28907; -.
GeneWiki; CD38; -.
GenomeRNAi; 952; -.
PRO; PR:P28907; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000004468; Expressed in 143 organ(s), highest expression level in epithelium of bronchus.
CleanEx; HS_CD38; -.
ExpressionAtlas; P28907; baseline and differential.
Genevisible; P28907; HS.
GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; TAS:ProtInc.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0030667; C:secretory granule membrane; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0050135; F:NAD(P)+ nucleosidase activity; IEA:UniProtKB-EC.
GO; GO:0003953; F:NAD+ nucleosidase activity; IBA:GO_Central.
GO; GO:0061809; F:NAD+ nucleotidase, cyclic ADP-ribose generating; IEA:UniProtKB-EC.
GO; GO:0016849; F:phosphorus-oxygen lyase activity; IBA:GO_Central.
GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
GO; GO:0097190; P:apoptotic signaling pathway; TAS:ProtInc.
GO; GO:0014824; P:artery smooth muscle contraction; IEA:Ensembl.
GO; GO:0050853; P:B cell receptor signaling pathway; IMP:UniProtKB.
GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
GO; GO:0060292; P:long term synaptic depression; IEA:Ensembl.
GO; GO:0019674; P:NAD metabolic process; TAS:Reactome.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0045779; P:negative regulation of bone resorption; IEA:Ensembl.
GO; GO:0010977; P:negative regulation of neuron projection development; IEA:Ensembl.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0030890; P:positive regulation of B cell proliferation; IMP:UniProtKB.
GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
GO; GO:0032024; P:positive regulation of insulin secretion; IEA:Ensembl.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0045907; P:positive regulation of vasoconstriction; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IMP:UniProtKB.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0033194; P:response to hydroperoxide; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0070555; P:response to interleukin-1; IEA:Ensembl.
GO; GO:0032570; P:response to progesterone; IEA:Ensembl.
GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; NAS:ProtInc.
CDD; cd04759; Rib_hydrolase; 1.
InterPro; IPR003193; ADP-ribosyl_cyclase.
InterPro; IPR033567; CD38.
PANTHER; PTHR10912; PTHR10912; 1.
PANTHER; PTHR10912:SF5; PTHR10912:SF5; 1.
Pfam; PF02267; Rib_hydrolayse; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Diabetes mellitus; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
NAD; NADP; Polymorphism; Receptor; Reference proteome; Signal-anchor;
Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 300 ADP-ribosyl cyclase/cyclic ADP-ribose
hydrolase 1.
/FTId=PRO_0000144066.
TOPO_DOM 1 21 Cytoplasmic. {ECO:0000255}.
TRANSMEM 22 42 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 43 300 Extracellular. {ECO:0000255}.
ACT_SITE 119 119 {ECO:0000269|PubMed:7961800}.
ACT_SITE 201 201 {ECO:0000269|PubMed:7961800}.
CARBOHYD 100 100 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 164 164 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 209 209 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 219 219 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19349973}.
DISULFID 67 82 {ECO:0000269|PubMed:16154090}.
DISULFID 99 180 {ECO:0000269|PubMed:16154090}.
DISULFID 160 173 {ECO:0000269|PubMed:16154090}.
DISULFID 254 275 {ECO:0000269|PubMed:16154090}.
DISULFID 287 296 {ECO:0000269|PubMed:16154090}.
VAR_SEQ 122 122 I -> K (in isoform 2).
{ECO:0000303|PubMed:9074508}.
/FTId=VSP_000707.
VAR_SEQ 123 300 Missing (in isoform 2).
{ECO:0000303|PubMed:9074508}.
/FTId=VSP_000708.
VARIANT 140 140 R -> W (seems to contribute to the
development of type II diabetes; 50%
reduction in activity; dbSNP:rs1800561).
{ECO:0000269|PubMed:9754820}.
/FTId=VAR_001323.
MUTAGEN 119 119 C->K: Loss of cADPr hydrolase activity.
{ECO:0000269|PubMed:7961800}.
MUTAGEN 119 119 C->R,E,A: Loss of cADPr hydrolase and
ADP-ribosyl cyclase activity.
{ECO:0000269|PubMed:7961800}.
MUTAGEN 160 160 C->A: Loss of cADPr hydrolase and ADP-
ribosyl cyclase activity.
{ECO:0000269|PubMed:7961800}.
MUTAGEN 173 173 C->A: Loss of cADPr hydrolase and ADP-
ribosyl cyclase activity.
{ECO:0000269|PubMed:7961800}.
MUTAGEN 201 201 C->D,K,A: Loss of cADPr hydrolase and
ADP-ribosyl cyclase activity.
{ECO:0000269|PubMed:7961800}.
MUTAGEN 201 201 C->E: Loss of cADPr hydrolase activity.
{ECO:0000269|PubMed:7961800}.
CONFLICT 49 49 Q -> T (in Ref. 1; AAA68482).
{ECO:0000305}.
STRAND 51 53 {ECO:0000244|PDB:3F6Y}.
HELIX 59 73 {ECO:0000244|PDB:3F6Y}.
HELIX 75 77 {ECO:0000244|PDB:2O3S}.
HELIX 82 93 {ECO:0000244|PDB:3F6Y}.
STRAND 94 96 {ECO:0000244|PDB:3RAJ}.
HELIX 98 100 {ECO:0000244|PDB:3F6Y}.
HELIX 103 106 {ECO:0000244|PDB:3F6Y}.
HELIX 107 112 {ECO:0000244|PDB:3F6Y}.
HELIX 119 121 {ECO:0000244|PDB:3F6Y}.
STRAND 122 127 {ECO:0000244|PDB:2O3S}.
STRAND 132 134 {ECO:0000244|PDB:3F6Y}.
HELIX 136 141 {ECO:0000244|PDB:3F6Y}.
STRAND 142 144 {ECO:0000244|PDB:3RAJ}.
HELIX 145 147 {ECO:0000244|PDB:3F6Y}.
HELIX 149 154 {ECO:0000244|PDB:3F6Y}.
STRAND 165 167 {ECO:0000244|PDB:3F6Y}.
STRAND 171 173 {ECO:0000244|PDB:3F6Y}.
TURN 176 179 {ECO:0000244|PDB:3F6Y}.
STRAND 181 183 {ECO:0000244|PDB:3F6Y}.
HELIX 184 199 {ECO:0000244|PDB:3F6Y}.
STRAND 202 209 {ECO:0000244|PDB:3F6Y}.
STRAND 212 216 {ECO:0000244|PDB:3F6Y}.
STRAND 218 220 {ECO:0000244|PDB:2EF1}.
HELIX 221 224 {ECO:0000244|PDB:3F6Y}.
HELIX 227 229 {ECO:0000244|PDB:3F6Y}.
TURN 232 234 {ECO:0000244|PDB:3F6Y}.
STRAND 235 243 {ECO:0000244|PDB:3F6Y}.
STRAND 246 249 {ECO:0000244|PDB:3F6Y}.
HELIX 253 255 {ECO:0000244|PDB:3F6Y}.
HELIX 257 268 {ECO:0000244|PDB:3F6Y}.
STRAND 272 278 {ECO:0000244|PDB:3F6Y}.
HELIX 281 289 {ECO:0000244|PDB:2O3S}.
TURN 291 293 {ECO:0000244|PDB:3DZG}.
HELIX 294 296 {ECO:0000244|PDB:5F21}.
SEQUENCE 300 AA; 34328 MW; 47BBE38C3DE3E6AA CRC64;
MANCEFSPVS GDKPCCRLSR RAQLCLGVSI LVLILVVVLA VVVPRWRQQW SGPGTTKRFP
ETVLARCVKY TEIHPEMRHV DCQSVWDAFK GAFISKHPCN ITEEDYQPLM KLGTQTVPCN
KILLWSRIKD LAHQFTQVQR DMFTLEDTLL GYLADDLTWC GEFNTSKINY QSCPDWRKDC
SNNPVSVFWK TVSRRFAEAA CDVVHVMLNG SRSKIFDKNS TFGSVEVHNL QPEKVQTLEA
WVIHGGREDS RDLCQDPTIK ELESIISKRN IQFSCKNIYR PDKFLQCVKN PEDSSCTSEI


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