CD38_HUMAN
ID CD38_HUMAN Reviewed; 300 AA.
AC P28907; O00121; O00122; Q96HY4;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 213.
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=T10;
DE AltName: CD_antigen=CD38;
GN Name=CD38;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2319135;
RA Jackson D.G., Bell J.I.;
RT "Isolation of a cDNA encoding the human CD38 (T10) molecule, a cell surface
RT glycoprotein with an unusual discontinuous pattern of expression during
RT lymphocyte differentiation.";
RL J. Immunol. 144:2811-2815(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1
RP AND 2), AND TISSUE SPECIFICITY.
RC TISSUE=Esophageal carcinoma, and Pancreas;
RX PubMed=9074508; DOI=10.1016/s0378-1119(96)00723-8;
RA Nata K., Takamura T., Karasawa T., Kumagai T., Hashioka W., Tohgo A.,
RA Yonekura H., Takasawa S., Nakamura S., Okamoto H.;
RT "Human gene encoding CD38 (ADP-ribosyl cyclase/cyclic ADP-ribose
RT hydrolase): organization, nucleotide sequence and alternative splicing.";
RL Gene 186:285-292(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=B-cell;
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 SIMILARITY TO NADASE.
RX PubMed=1471258; DOI=10.1016/0968-0004(92)90337-9;
RA States D.J., Walseth T.F., Lee H.C.;
RT "Similarities in amino acid sequences of Aplysia ADP-ribosyl cyclase and
RT human lymphocyte antigen CD38.";
RL Trends Biochem. Sci. 17:495-495(1992).
RN [5]
RP CHARACTERIZATION.
RX PubMed=8253715; DOI=10.1016/s0021-9258(19)74275-6;
RA Takasawa S., Tohgo A., Noguchi N., Koguma T., Nata K., Sugimoto T.,
RA Yonekura H., Okamoto H.;
RT "Synthesis and hydrolysis of cyclic ADP-ribose by human leukocyte antigen
RT CD38 and inhibition of the hydrolysis by ATP.";
RL J. Biol. Chem. 268:26052-26054(1993).
RN [6]
RP ACTIVE SITE, AND MUTAGENESIS OF CYS-119; CYS-160; CYS-173 AND CYS-201.
RX PubMed=7961800; DOI=10.1016/s0021-9258(19)61940-x;
RA Tohgo A., Takasawa S., Noguchi N., Koguma T., Nata K., Sugimoto T.,
RA Furuya Y., Yonekura H., Okamoto H.;
RT "Essential cysteine residues for cyclic ADP-ribose synthesis and hydrolysis
RT by CD38.";
RL J. Biol. Chem. 269:28555-28557(1994).
RN [7]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [8]
RP CATALYTIC ACTIVITY.
RX PubMed=16690024; DOI=10.1016/j.bbrc.2006.04.096;
RA Moreschi I., Bruzzone S., Melone L., De Flora A., Zocchi E.;
RT "NAADP+ synthesis from cADPRP and nicotinic acid by ADP-ribosyl cyclases.";
RL Biochem. Biophys. Res. Commun. 345:573-580(2006).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-100; ASN-209 AND ASN-219.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-219.
RC TISSUE=Leukemic T-cell;
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 45-300, AND DISULFIDE BONDS.
RX PubMed=16154090; DOI=10.1016/j.str.2005.05.012;
RA Liu Q., Kriksunov I.A., Graeff R., Munshi C., Lee H.C., Hao Q.;
RT "Crystal structure of human CD38 extracellular domain.";
RL Structure 13:1331-1339(2005).
RN [14]
RP VARIANT TRP-140.
RX PubMed=9754820; DOI=10.1007/s001250051026;
RA Yagui K., Shimada F., Mimura M., Hashimoto N., Suzuki Y., Tokuyama Y.,
RA Nata K., Tohgo A., Ikehata F., Takasawa S., Okamoto H., Makino H.,
RA Saito Y., Kanatsuka A.;
RT "A missense mutation in the CD38 gene, a novel factor for insulin
RT secretion: association with Type II diabetes mellitus in Japanese subjects
RT and evidence of abnormal function when expressed in vitro.";
RL Diabetologia 41:1024-1028(1998).
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. Also moonlights as a receptor in cells of the
CC immune system.
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 Evidence={ECO:0000269|PubMed:16690024};
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:16690024};
CC -!- ACTIVITY REGULATION: ATP inhibits the hydrolyzing activity.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P28907-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P28907-2; Sequence=VSP_000707, VSP_000708;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in pancreas, liver,
CC kidney, brain, testis, ovary, placenta, malignant lymphoma and
CC neuroblastoma. {ECO:0000269|PubMed:9074508}.
CC -!- DEVELOPMENTAL STAGE: Preferentially expressed at both early and late
CC stages of the B and T-cell maturation. It is also detected on erythroid
CC and myeloid progenitors in bone marrow, where the level of surface
CC expression was shown to decrease during differentiation of blast-
CC forming unit E to colony-forming unit E.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ADP-ribosyl cyclase family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=CD38 entry;
CC URL="https://en.wikipedia.org/wiki/CD38";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CD38ID978ch4p15.html";
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DR EMBL; M34461; AAA68482.1; -; mRNA.
DR EMBL; D84276; BAA18964.1; -; mRNA.
DR EMBL; D84277; BAA18965.1; -; mRNA.
DR EMBL; D84284; BAA18966.1; -; Genomic_DNA.
DR EMBL; BC007964; AAH07964.1; -; mRNA.
DR CCDS; CCDS3417.1; -. [P28907-1]
DR PIR; A43521; A43521.
DR RefSeq; NP_001766.2; NM_001775.3. [P28907-1]
DR PDB; 1YH3; X-ray; 1.91 A; A/B=45-300.
DR PDB; 1ZVM; X-ray; 2.20 A; A/B/C/D=45-300.
DR PDB; 2EF1; X-ray; 2.40 A; A/B=45-300.
DR PDB; 2HCT; X-ray; 1.95 A; A/B=45-300.
DR PDB; 2I65; X-ray; 1.90 A; A/B=45-300.
DR PDB; 2I66; X-ray; 1.70 A; A/B=45-300.
DR PDB; 2I67; X-ray; 1.71 A; A/B=45-300.
DR PDB; 2O3Q; X-ray; 1.98 A; A/B=45-300.
DR PDB; 2O3R; X-ray; 1.75 A; A/B=45-300.
DR PDB; 2O3S; X-ray; 1.50 A; A/B=45-300.
DR PDB; 2O3T; X-ray; 1.68 A; A/B=45-300.
DR PDB; 2O3U; X-ray; 2.11 A; A/B=45-300.
DR PDB; 2PGJ; X-ray; 1.71 A; A/B=45-300.
DR PDB; 2PGL; X-ray; 1.76 A; A/B=45-300.
DR PDB; 3DZF; X-ray; 2.01 A; A/B/C/D/E/F=45-300.
DR PDB; 3DZG; X-ray; 1.65 A; A/B=45-300.
DR PDB; 3DZH; X-ray; 1.60 A; A/B=45-300.
DR PDB; 3DZI; X-ray; 1.73 A; A/B=45-300.
DR PDB; 3DZJ; X-ray; 1.90 A; A/B=45-300.
DR PDB; 3DZK; X-ray; 1.81 A; A/B=45-300.
DR PDB; 3F6Y; X-ray; 1.45 A; A=45-300.
DR PDB; 3I9M; X-ray; 1.75 A; A/B=45-300.
DR PDB; 3I9N; X-ray; 2.01 A; A/B=45-300.
DR PDB; 3OFS; X-ray; 2.20 A; A/B/C/D/E/F=46-300.
DR PDB; 3RAJ; X-ray; 3.04 A; A=46-300.
DR PDB; 3ROK; X-ray; 1.65 A; A/B=45-296.
DR PDB; 3ROM; X-ray; 2.04 A; A/B=45-296.
DR PDB; 3ROP; X-ray; 1.94 A; A/B=45-296.
DR PDB; 3ROQ; X-ray; 2.10 A; A/B=45-296.
DR PDB; 3U4H; X-ray; 1.88 A; A/B=45-300.
DR PDB; 3U4I; X-ray; 2.12 A; A/B=45-300.
DR PDB; 4CMH; X-ray; 1.53 A; A=45-300.
DR PDB; 4F45; X-ray; 2.10 A; A/B=46-300.
DR PDB; 4F46; X-ray; 1.69 A; A/B=46-300.
DR PDB; 4OGW; X-ray; 2.05 A; A=46-300.
DR PDB; 4TMF; X-ray; 2.05 A; A/B=50-300.
DR PDB; 4XJS; X-ray; 2.80 A; A=46-300.
DR PDB; 4XJT; X-ray; 2.60 A; A=46-300.
DR PDB; 5F1K; X-ray; 2.30 A; A/B=45-300.
DR PDB; 5F1O; X-ray; 2.20 A; A=46-300.
DR PDB; 5F21; X-ray; 1.90 A; A=46-300.
DR PDB; 6EDR; X-ray; 2.40 A; A/B=45-300.
DR PDB; 6VUA; X-ray; 1.50 A; A/B=45-300.
DR PDB; 7DHA; X-ray; 2.55 A; A=45-300.
DR PDB; 7DUO; X-ray; 2.81 A; B=57-285.
DR PDBsum; 1YH3; -.
DR PDBsum; 1ZVM; -.
DR PDBsum; 2EF1; -.
DR PDBsum; 2HCT; -.
DR PDBsum; 2I65; -.
DR PDBsum; 2I66; -.
DR PDBsum; 2I67; -.
DR PDBsum; 2O3Q; -.
DR PDBsum; 2O3R; -.
DR PDBsum; 2O3S; -.
DR PDBsum; 2O3T; -.
DR PDBsum; 2O3U; -.
DR PDBsum; 2PGJ; -.
DR PDBsum; 2PGL; -.
DR PDBsum; 3DZF; -.
DR PDBsum; 3DZG; -.
DR PDBsum; 3DZH; -.
DR PDBsum; 3DZI; -.
DR PDBsum; 3DZJ; -.
DR PDBsum; 3DZK; -.
DR PDBsum; 3F6Y; -.
DR PDBsum; 3I9M; -.
DR PDBsum; 3I9N; -.
DR PDBsum; 3OFS; -.
DR PDBsum; 3RAJ; -.
DR PDBsum; 3ROK; -.
DR PDBsum; 3ROM; -.
DR PDBsum; 3ROP; -.
DR PDBsum; 3ROQ; -.
DR PDBsum; 3U4H; -.
DR PDBsum; 3U4I; -.
DR PDBsum; 4CMH; -.
DR PDBsum; 4F45; -.
DR PDBsum; 4F46; -.
DR PDBsum; 4OGW; -.
DR PDBsum; 4TMF; -.
DR PDBsum; 4XJS; -.
DR PDBsum; 4XJT; -.
DR PDBsum; 5F1K; -.
DR PDBsum; 5F1O; -.
DR PDBsum; 5F21; -.
DR PDBsum; 6EDR; -.
DR PDBsum; 6VUA; -.
DR PDBsum; 7DHA; -.
DR PDBsum; 7DUO; -.
DR AlphaFoldDB; P28907; -.
DR SMR; P28907; -.
DR BioGRID; 107390; 10.
DR IntAct; P28907; 5.
DR STRING; 9606.ENSP00000226279; -.
DR BindingDB; P28907; -.
DR ChEMBL; CHEMBL4660; -.
DR DrugBank; DB09331; Daratumumab.
DR DrugBank; DB14811; Isatuximab.
DR DrugBank; DB16370; Mezagitamab.
DR DrugCentral; P28907; -.
DR GuidetoPHARMACOLOGY; 2766; -.
DR GlyConnect; 997; 1 N-Linked glycan (1 site).
DR GlyGen; P28907; 5 sites, 1 N-linked glycan (1 site).
DR iPTMnet; P28907; -.
DR PhosphoSitePlus; P28907; -.
DR SwissPalm; P28907; -.
DR BioMuta; CD38; -.
DR DMDM; 55977782; -.
DR EPD; P28907; -.
DR jPOST; P28907; -.
DR MassIVE; P28907; -.
DR MaxQB; P28907; -.
DR PaxDb; P28907; -.
DR PeptideAtlas; P28907; -.
DR PRIDE; P28907; -.
DR ProteomicsDB; 54507; -. [P28907-1]
DR ProteomicsDB; 54508; -. [P28907-2]
DR ABCD; P28907; 65 sequenced antibodies.
DR Antibodypedia; 9844; 2499 antibodies from 55 providers.
DR CPTC; P28907; 1 antibody.
DR DNASU; 952; -.
DR Ensembl; ENST00000226279.8; ENSP00000226279.2; ENSG00000004468.13. [P28907-1]
DR Ensembl; ENST00000502843.5; ENSP00000427277.1; ENSG00000004468.13. [P28907-2]
DR GeneID; 952; -.
DR KEGG; hsa:952; -.
DR MANE-Select; ENST00000226279.8; ENSP00000226279.2; NM_001775.4; NP_001766.2.
DR UCSC; uc003gol.2; human. [P28907-1]
DR CTD; 952; -.
DR DisGeNET; 952; -.
DR GeneCards; CD38; -.
DR HGNC; HGNC:1667; CD38.
DR HPA; ENSG00000004468; Tissue enhanced (lymphoid).
DR MIM; 107270; gene.
DR neXtProt; NX_P28907; -.
DR OpenTargets; ENSG00000004468; -.
DR PharmGKB; PA26214; -.
DR VEuPathDB; HostDB:ENSG00000004468; -.
DR eggNOG; ENOG502S1HV; Eukaryota.
DR GeneTree; ENSGT00390000017291; -.
DR HOGENOM; CLU_2025937_0_0_1; -.
DR InParanoid; P28907; -.
DR OMA; MNYDSCP; -.
DR PhylomeDB; P28907; -.
DR TreeFam; TF332530; -.
DR BioCyc; MetaCyc:HS00103-MON; -.
DR BRENDA; 2.4.99.20; 2681.
DR BRENDA; 3.2.2.5; 2681.
DR BRENDA; 3.2.2.6; 2681.
DR PathwayCommons; P28907; -.
DR Reactome; R-HSA-196807; Nicotinate metabolism.
DR SABIO-RK; P28907; -.
DR SignaLink; P28907; -.
DR SIGNOR; P28907; -.
DR BioGRID-ORCS; 952; 8 hits in 1077 CRISPR screens.
DR ChiTaRS; CD38; human.
DR EvolutionaryTrace; P28907; -.
DR GeneWiki; CD38; -.
DR GenomeRNAi; 952; -.
DR Pharos; P28907; Tclin.
DR PRO; PR:P28907; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P28907; protein.
DR Bgee; ENSG00000004468; Expressed in seminal vesicle and 129 other tissues.
DR ExpressionAtlas; P28907; baseline and differential.
DR Genevisible; P28907; HS.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0030667; C:secretory granule membrane; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0050135; F:NAD(P)+ nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0003953; F:NAD+ nucleosidase activity; IBA:GO_Central.
DR GO; GO:0061809; F:NAD+ nucleotidase, cyclic ADP-ribose generating; IEA:UniProtKB-EC.
DR GO; GO:0016849; F:phosphorus-oxygen lyase activity; IBA:GO_Central.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0097190; P:apoptotic signaling pathway; TAS:ProtInc.
DR GO; GO:0014824; P:artery smooth muscle contraction; IEA:Ensembl.
DR GO; GO:0042100; P:B cell proliferation; IEA:Ensembl.
DR GO; GO:0050853; P:B cell receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
DR GO; GO:0060292; P:long-term synaptic depression; IEA:Ensembl.
DR GO; GO:0019674; P:NAD metabolic process; TAS:Reactome.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0045779; P:negative regulation of bone resorption; IEA:Ensembl.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; IMP:UniProtKB.
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; IMP:UniProtKB.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; 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 GO; GO:0009410; P:response to xenobiotic stimulus; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; NAS:ProtInc.
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; Alternative splicing; Diabetes mellitus; Disulfide bond;
KW Glycoprotein; Hydrolase; Membrane; NAD; NADP; Receptor; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..300
FT /note="ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1"
FT /id="PRO_0000144066"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..42
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..300
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT ACT_SITE 119
FT /evidence="ECO:0000269|PubMed:7961800"
FT ACT_SITE 201
FT /evidence="ECO:0000269|PubMed:7961800"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:19349973"
FT DISULFID 67..82
FT /evidence="ECO:0000269|PubMed:16154090"
FT DISULFID 99..180
FT /evidence="ECO:0000269|PubMed:16154090"
FT DISULFID 160..173
FT /evidence="ECO:0000269|PubMed:16154090"
FT DISULFID 254..275
FT /evidence="ECO:0000269|PubMed:16154090"
FT DISULFID 287..296
FT /evidence="ECO:0000269|PubMed:16154090"
FT VAR_SEQ 122
FT /note="I -> K (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9074508"
FT /id="VSP_000707"
FT VAR_SEQ 123..300
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9074508"
FT /id="VSP_000708"
FT VARIANT 140
FT /note="R -> W (seems to contribute to the development of
FT type II diabetes; 50% reduction in activity;
FT dbSNP:rs1800561)"
FT /evidence="ECO:0000269|PubMed:9754820"
FT /id="VAR_001323"
FT MUTAGEN 119
FT /note="C->K: Loss of cADPr hydrolase activity."
FT /evidence="ECO:0000269|PubMed:7961800"
FT MUTAGEN 119
FT /note="C->R,E,A: Loss of cADPr hydrolase and ADP-ribosyl
FT cyclase activity."
FT /evidence="ECO:0000269|PubMed:7961800"
FT MUTAGEN 160
FT /note="C->A: Loss of cADPr hydrolase and ADP-ribosyl
FT cyclase activity."
FT /evidence="ECO:0000269|PubMed:7961800"
FT MUTAGEN 173
FT /note="C->A: Loss of cADPr hydrolase and ADP-ribosyl
FT cyclase activity."
FT /evidence="ECO:0000269|PubMed:7961800"
FT MUTAGEN 201
FT /note="C->D,K,A: Loss of cADPr hydrolase and ADP-ribosyl
FT cyclase activity."
FT /evidence="ECO:0000269|PubMed:7961800"
FT MUTAGEN 201
FT /note="C->E: Loss of cADPr hydrolase activity."
FT /evidence="ECO:0000269|PubMed:7961800"
FT CONFLICT 49
FT /note="Q -> T (in Ref. 1; AAA68482)"
FT /evidence="ECO:0000305"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:3F6Y"
FT HELIX 59..73
FT /evidence="ECO:0007829|PDB:3F6Y"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:2O3S"
FT HELIX 82..93
FT /evidence="ECO:0007829|PDB:3F6Y"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:3RAJ"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:3F6Y"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:3F6Y"
FT HELIX 107..112
FT /evidence="ECO:0007829|PDB:3F6Y"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:3F6Y"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:2O3S"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:3F6Y"
FT HELIX 136..141
FT /evidence="ECO:0007829|PDB:3F6Y"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:3RAJ"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:3F6Y"
FT HELIX 149..154
FT /evidence="ECO:0007829|PDB:3F6Y"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:3F6Y"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:3F6Y"
FT TURN 176..179
FT /evidence="ECO:0007829|PDB:3F6Y"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:3F6Y"
FT HELIX 184..199
FT /evidence="ECO:0007829|PDB:3F6Y"
FT STRAND 202..209
FT /evidence="ECO:0007829|PDB:3F6Y"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:3F6Y"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:2EF1"
FT HELIX 221..224
FT /evidence="ECO:0007829|PDB:3F6Y"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:3F6Y"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:3F6Y"
FT STRAND 235..243
FT /evidence="ECO:0007829|PDB:3F6Y"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:3F6Y"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:3F6Y"
FT HELIX 257..268
FT /evidence="ECO:0007829|PDB:3F6Y"
FT STRAND 272..278
FT /evidence="ECO:0007829|PDB:3F6Y"
FT HELIX 281..289
FT /evidence="ECO:0007829|PDB:2O3S"
FT TURN 291..293
FT /evidence="ECO:0007829|PDB:3DZG"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:5F21"
SQ 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
