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Protein

ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1

Gene

CD38

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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 activityi

NAD+ + H2O = ADP-D-ribose + nicotinamide.1 Publication
NADP+ + nicotinate = nicotinate-adenine dinucleotide phosphate + nicotinamide.1 Publication

Activity regulationi

ATP inhibits the hydrolyzing activity.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei1191 Publication1
Active sitei2011 Publication1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Receptor, Transferase
LigandNAD, NADP

Enzyme and pathway databases

BioCyciMetaCyc:HS00103-MONOMER
BRENDAi2.4.99.20 2681
3.2.2.5 2681
ReactomeiR-HSA-196807 Nicotinate metabolism
SABIO-RKiP28907

Names & Taxonomyi

Protein namesi
Recommended name:
ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1 (EC:3.2.2.6)
Alternative name(s):
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
Short name:
ADPRC 1
Cyclic ADP-ribose hydrolase 1
Short name:
cADPr hydrolase 1
T10
CD_antigen: CD38
Gene namesi
Name:CD38
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

EuPathDBiHostDB:ENSG00000004468.12
HGNCiHGNC:1667 CD38
MIMi107270 gene
neXtProtiNX_P28907

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 21CytoplasmicSequence analysisAdd BLAST21
Transmembranei22 – 42Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini43 – 300ExtracellularSequence analysisAdd BLAST258

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi119C → K: Loss of cADPr hydrolase activity. 1 Publication1
Mutagenesisi119C → R, E or A: Loss of cADPr hydrolase and ADP-ribosyl cyclase activity. 1 Publication1
Mutagenesisi160C → A: Loss of cADPr hydrolase and ADP-ribosyl cyclase activity. 1 Publication1
Mutagenesisi173C → A: Loss of cADPr hydrolase and ADP-ribosyl cyclase activity. 1 Publication1
Mutagenesisi201C → D, K or A: Loss of cADPr hydrolase and ADP-ribosyl cyclase activity. 1 Publication1
Mutagenesisi201C → E: Loss of cADPr hydrolase activity. 1 Publication1

Keywords - Diseasei

Diabetes mellitus

Organism-specific databases

DisGeNETi952
OpenTargetsiENSG00000004468
PharmGKBiPA26214

Chemistry databases

ChEMBLiCHEMBL4660
DrugBankiDB09331 Daratumumab
GuidetoPHARMACOLOGYi2766

Polymorphism and mutation databases

BioMutaiCD38
DMDMi55977782

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001440661 – 300ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1Add BLAST300

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi67 ↔ 821 Publication
Disulfide bondi99 ↔ 1801 Publication
Glycosylationi100N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi160 ↔ 1731 Publication
Glycosylationi164N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi209N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi219N-linked (GlcNAc...) asparagine2 Publications1
Disulfide bondi254 ↔ 2751 Publication
Disulfide bondi287 ↔ 2961 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiP28907
MaxQBiP28907
PaxDbiP28907
PeptideAtlasiP28907
PRIDEiP28907
ProteomicsDBi54507
54508 [P28907-2]

PTM databases

iPTMnetiP28907
PhosphoSitePlusiP28907
SwissPalmiP28907

Expressioni

Tissue specificityi

Expressed at high levels in pancreas, liver, kidney, brain, testis, ovary, placenta, malignant lymphoma and neuroblastoma.1 Publication

Developmental stagei

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.

Gene expression databases

BgeeiENSG00000004468 Expressed in 143 organ(s), highest expression level in epithelium of bronchus
CleanExiHS_CD38
ExpressionAtlasiP28907 baseline and differential
GenevisibleiP28907 HS

Organism-specific databases

HPAiCAB002493
CAB025255
HPA022132
HPA052381

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

BioGridi107390, 6 interactors
STRINGi9606.ENSP00000226279

Chemistry databases

BindingDBiP28907

Structurei

Secondary structure

1300
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP28907
SMRiP28907
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28907

Family & Domainsi

Sequence similaritiesi

Belongs to the ADP-ribosyl cyclase family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IH8E Eukaryota
ENOG4111W33 LUCA
GeneTreeiENSGT00390000017291
HOGENOMiHOG000293141
HOVERGENiHBG005277
InParanoidiP28907
KOiK01242
OMAiQCVKNPE
OrthoDBiEOG091G0GI3
PhylomeDBiP28907
TreeFamiTF332530

Family and domain databases

CDDicd04759 Rib_hydrolase, 1 hit
InterProiView protein in InterPro
IPR003193 ADP-ribosyl_cyclase
IPR033567 CD38
PANTHERiPTHR10912 PTHR10912, 1 hit
PTHR10912:SF5 PTHR10912:SF5, 1 hit
PfamiView protein in Pfam
PF02267 Rib_hydrolayse, 1 hit

Sequences (2+)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.iShow all

Isoform 1 (identifier: P28907-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MANCEFSPVS GDKPCCRLSR RAQLCLGVSI LVLILVVVLA VVVPRWRQQW
60 70 80 90 100
SGPGTTKRFP ETVLARCVKY TEIHPEMRHV DCQSVWDAFK GAFISKHPCN
110 120 130 140 150
ITEEDYQPLM KLGTQTVPCN KILLWSRIKD LAHQFTQVQR DMFTLEDTLL
160 170 180 190 200
GYLADDLTWC GEFNTSKINY QSCPDWRKDC SNNPVSVFWK TVSRRFAEAA
210 220 230 240 250
CDVVHVMLNG SRSKIFDKNS TFGSVEVHNL QPEKVQTLEA WVIHGGREDS
260 270 280 290 300
RDLCQDPTIK ELESIISKRN IQFSCKNIYR PDKFLQCVKN PEDSSCTSEI
Length:300
Mass (Da):34,328
Last modified:November 23, 2004 - v2
Checksum:i47BBE38C3DE3E6AA
GO
Isoform 2 (identifier: P28907-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     122-122: I → K
     123-300: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Show »
Length:122
Mass (Da):13,788
Checksum:i06312C3A52C6ED5C
GO

Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H0Y950H0Y950_HUMAN
ADP-ribosyl cyclase/cyclic ADP-ribo...
CD38
151Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti49Q → T in AAA68482 (PubMed:2319135).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_001323140R → W Seems to contribute to the development of type II diabetes; 50% reduction in activity. 1 PublicationCorresponds to variant dbSNP:rs1800561Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_000707122I → K in isoform 2. 1 Publication1
Alternative sequenceiVSP_000708123 – 300Missing in isoform 2. 1 PublicationAdd BLAST178

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34461 mRNA Translation: AAA68482.1
D84276 mRNA Translation: BAA18964.1
D84277 mRNA Translation: BAA18965.1
D84284 Genomic DNA Translation: BAA18966.1
BC007964 mRNA Translation: AAH07964.1
CCDSiCCDS3417.1 [P28907-1]
PIRiA43521
RefSeqiNP_001766.2, NM_001775.3 [P28907-1]
UniGeneiHs.479214

Genome annotation databases

EnsembliENST00000226279; ENSP00000226279; ENSG00000004468 [P28907-1]
ENST00000502843; ENSP00000427277; ENSG00000004468 [P28907-2]
GeneIDi952
KEGGihsa:952
UCSCiuc003gol.2 human [P28907-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Cross-referencesi

Web resourcesi

Wikipedia

CD38 entry

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34461 mRNA Translation: AAA68482.1
D84276 mRNA Translation: BAA18964.1
D84277 mRNA Translation: BAA18965.1
D84284 Genomic DNA Translation: BAA18966.1
BC007964 mRNA Translation: AAH07964.1
CCDSiCCDS3417.1 [P28907-1]
PIRiA43521
RefSeqiNP_001766.2, NM_001775.3 [P28907-1]
UniGeneiHs.479214

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YH3X-ray1.91A/B45-300[»]
1ZVMX-ray2.20A/B/C/D45-300[»]
2EF1X-ray2.40A/B45-300[»]
2HCTX-ray1.95A/B45-300[»]
2I65X-ray1.90A/B45-300[»]
2I66X-ray1.70A/B45-300[»]
2I67X-ray1.71A/B45-300[»]
2O3QX-ray1.98A/B45-300[»]
2O3RX-ray1.75A/B45-300[»]
2O3SX-ray1.50A/B45-300[»]
2O3TX-ray1.68A/B45-300[»]
2O3UX-ray2.11A/B45-300[»]
2PGJX-ray1.71A/B45-300[»]
2PGLX-ray1.76A/B45-300[»]
3DZFX-ray2.01A/B/C/D/E/F45-300[»]
3DZGX-ray1.65A/B45-300[»]
3DZHX-ray1.60A/B45-300[»]
3DZIX-ray1.73A/B45-300[»]
3DZJX-ray1.90A/B45-300[»]
3DZKX-ray1.81A/B45-300[»]
3F6YX-ray1.45A45-300[»]
3I9MX-ray1.75A/B45-300[»]
3I9NX-ray2.01A/B45-300[»]
3OFSX-ray2.20A/B/C/D/E/F46-300[»]
3RAJX-ray3.04A46-300[»]
3ROKX-ray1.65A/B45-296[»]
3ROMX-ray2.04A/B45-296[»]
3ROPX-ray1.94A/B45-296[»]
3ROQX-ray2.10A/B45-296[»]
3U4HX-ray1.88A/B45-300[»]
3U4IX-ray2.12A/B45-300[»]
4CMHX-ray1.53A45-300[»]
4F45X-ray2.10A/B46-300[»]
4F46X-ray1.69A/B46-300[»]
4OGWX-ray2.05A46-300[»]
4TMFX-ray2.05A/B50-300[»]
4XJSX-ray2.80A46-300[»]
4XJTX-ray2.60A46-300[»]
5F1KX-ray2.30A/B45-300[»]
5F1OX-ray2.20A46-300[»]
5F21X-ray1.90A46-300[»]
ProteinModelPortaliP28907
SMRiP28907
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107390, 6 interactors
STRINGi9606.ENSP00000226279

Chemistry databases

BindingDBiP28907
ChEMBLiCHEMBL4660
DrugBankiDB09331 Daratumumab
GuidetoPHARMACOLOGYi2766

PTM databases

iPTMnetiP28907
PhosphoSitePlusiP28907
SwissPalmiP28907

Polymorphism and mutation databases

BioMutaiCD38
DMDMi55977782

Proteomic databases

EPDiP28907
MaxQBiP28907
PaxDbiP28907
PeptideAtlasiP28907
PRIDEiP28907
ProteomicsDBi54507
54508 [P28907-2]

Protocols and materials databases

DNASUi952
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000226279; ENSP00000226279; ENSG00000004468 [P28907-1]
ENST00000502843; ENSP00000427277; ENSG00000004468 [P28907-2]
GeneIDi952
KEGGihsa:952
UCSCiuc003gol.2 human [P28907-1]

Organism-specific databases

CTDi952
DisGeNETi952
EuPathDBiHostDB:ENSG00000004468.12
GeneCardsiCD38
HGNCiHGNC:1667 CD38
HPAiCAB002493
CAB025255
HPA022132
HPA052381
MIMi107270 gene
neXtProtiNX_P28907
OpenTargetsiENSG00000004468
PharmGKBiPA26214
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IH8E Eukaryota
ENOG4111W33 LUCA
GeneTreeiENSGT00390000017291
HOGENOMiHOG000293141
HOVERGENiHBG005277
InParanoidiP28907
KOiK01242
OMAiQCVKNPE
OrthoDBiEOG091G0GI3
PhylomeDBiP28907
TreeFamiTF332530

Enzyme and pathway databases

BioCyciMetaCyc:HS00103-MONOMER
BRENDAi2.4.99.20 2681
3.2.2.5 2681
ReactomeiR-HSA-196807 Nicotinate metabolism
SABIO-RKiP28907

Miscellaneous databases

ChiTaRSiCD38 human
EvolutionaryTraceiP28907
GeneWikiiCD38
GenomeRNAii952
PROiPR:P28907
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000004468 Expressed in 143 organ(s), highest expression level in epithelium of bronchus
CleanExiHS_CD38
ExpressionAtlasiP28907 baseline and differential
GenevisibleiP28907 HS

Family and domain databases

CDDicd04759 Rib_hydrolase, 1 hit
InterProiView protein in InterPro
IPR003193 ADP-ribosyl_cyclase
IPR033567 CD38
PANTHERiPTHR10912 PTHR10912, 1 hit
PTHR10912:SF5 PTHR10912:SF5, 1 hit
PfamiView protein in Pfam
PF02267 Rib_hydrolayse, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiCD38_HUMAN
AccessioniPrimary (citable) accession number: P28907
Secondary accession number(s): O00121, O00122, Q96HY4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: November 23, 2004
Last modified: September 12, 2018
This is version 188 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health

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