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Protein

ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1

Gene

Cd38

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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 (By similarity).By similarity1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei123By similarity1
Active sitei205By similarity1

GO - Molecular functioni

  • hydrolase activity, acting on glycosyl bonds Source: MGI
  • NAD(P)+ nucleosidase activity Source: UniProtKB-EC
  • NAD+ nucleosidase activity Source: GO_Central
  • phosphorus-oxygen lyase activity Source: MGI
  • transferase activity Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transferase

Keywords - Ligandi

NAD, NADP

Enzyme and pathway databases

BRENDAi2.4.99.20. 3474.

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
I-19
NIM-R5 antigen
CD_antigen: CD38
Gene namesi
Name:Cd38
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:107474. Cd38.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 21CytoplasmicSequence analysisAdd BLAST21
Transmembranei22 – 44Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST23
Topological domaini45 – 304ExtracellularSequence analysisAdd BLAST260

GO - Cellular componenti

  • cell surface Source: MGI
  • extracellular exosome Source: MGI
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: MGI
  • nucleus Source: Ensembl
  • plasma membrane Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3425388.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001440681 – 304ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1Add BLAST304

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi70 ↔ 861 Publication
Disulfide bondi103 ↔ 1841 Publication
Glycosylationi104N-linked (GlcNAc...)Sequence analysis1
Glycosylationi124N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi164 ↔ 1771 Publication
Glycosylationi213N-linked (GlcNAc...)Sequence analysis1
Glycosylationi223N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi258 ↔ 2791 Publication
Disulfide bondi291 ↔ 3001 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP56528.
PeptideAtlasiP56528.
PRIDEiP56528.

PTM databases

iPTMnetiP56528.
PhosphoSitePlusiP56528.
SwissPalmiP56528.

Expressioni

Gene expression databases

BgeeiENSMUSG00000029084.
CleanExiMM_CD38.
ExpressionAtlasiP56528. baseline and differential.
GenevisibleiP56528. MM.

Interactioni

Protein-protein interaction databases

BioGridi198590. 1 interactor.
DIPiDIP-59864N.
IntActiP56528. 1 interactor.
MINTiMINT-4090243.
STRINGi10090.ENSMUSP00000030964.

Chemistry databases

BindingDBiP56528.

Structurei

Secondary structure

1304
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi62 – 75Combined sources14
Helixi79 – 81Combined sources3
Helixi86 – 97Combined sources12
Helixi107 – 110Combined sources4
Helixi111 – 116Combined sources6
Helixi149 – 151Combined sources3
Helixi153 – 158Combined sources6
Helixi188 – 203Combined sources16
Beta strandi206 – 219Combined sources14
Helixi225 – 228Combined sources4
Helixi230 – 233Combined sources4
Turni236 – 238Combined sources3
Beta strandi239 – 247Combined sources9
Beta strandi250 – 252Combined sources3
Helixi257 – 259Combined sources3
Helixi261 – 271Combined sources11
Turni272 – 274Combined sources3
Beta strandi276 – 282Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2EG9X-ray2.80A/B48-288[»]
ProteinModelPortaliP56528.
SMRiP56528.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56528.

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.
InParanoidiP56528.
KOiK01242.
OMAiCKNIYRP.
OrthoDBiEOG091G0GI3.
PhylomeDBiP56528.
TreeFamiTF332530.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR003193. ADP-ribosyl_cyclase.
IPR033567. CD38.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR10912. PTHR10912. 1 hit.
PTHR10912:SF5. PTHR10912:SF5. 1 hit.
PfamiPF02267. Rib_hydrolayse. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P56528-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANYEFSQVS GDRPGCRLSR KAQIGLGVGL LVLIALVVGI VVILLRPRSL
60 70 80 90 100
LVWTGEPTTK HFSDIFLGRC LIYTQILRPE MRDQNCQEIL STFKGAFVSK
110 120 130 140 150
NPCNITREDY APLVKLVTQT IPCNKTLFWS KSKHLAHQYT WIQGKMFTLE
160 170 180 190 200
DTLLGYIADD LRWCGDPSTS DMNYVSCPHW SENCPNNPIT VFWKVISQKF
210 220 230 240 250
AEDACGVVQV MLNGSLREPF YKNSTFGSVE VFSLDPNKVH KLQAWVMHDI
260 270 280 290 300
EGASSNACSS SSLNELKMIV QKRNMIFACV DNYRPARFLQ CVKNPEHPSC

RLNT
Length:304
Mass (Da):34,408
Last modified:November 23, 2004 - v2
Checksum:iDD0A7747C5F67D6F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti191V → M in AAA03163 (PubMed:8376770).Curated1
Sequence conflicti229V → L in AAA03163 (PubMed:8376770).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L11332 mRNA. Translation: AAA03163.1.
AK038439 mRNA. Translation: BAC30000.1.
AK040498 mRNA. Translation: BAC30607.1.
AK042970 mRNA. Translation: BAC31423.1.
BC046312 mRNA. Translation: AAH46312.1.
CCDSiCCDS19265.1.
PIRiI49586.
RefSeqiNP_031672.2. NM_007646.5.
UniGeneiMm.249873.

Genome annotation databases

EnsembliENSMUST00000030964; ENSMUSP00000030964; ENSMUSG00000029084.
GeneIDi12494.
KEGGimmu:12494.
UCSCiuc008xic.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L11332 mRNA. Translation: AAA03163.1.
AK038439 mRNA. Translation: BAC30000.1.
AK040498 mRNA. Translation: BAC30607.1.
AK042970 mRNA. Translation: BAC31423.1.
BC046312 mRNA. Translation: AAH46312.1.
CCDSiCCDS19265.1.
PIRiI49586.
RefSeqiNP_031672.2. NM_007646.5.
UniGeneiMm.249873.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2EG9X-ray2.80A/B48-288[»]
ProteinModelPortaliP56528.
SMRiP56528.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198590. 1 interactor.
DIPiDIP-59864N.
IntActiP56528. 1 interactor.
MINTiMINT-4090243.
STRINGi10090.ENSMUSP00000030964.

Chemistry databases

BindingDBiP56528.
ChEMBLiCHEMBL3425388.

PTM databases

iPTMnetiP56528.
PhosphoSitePlusiP56528.
SwissPalmiP56528.

Proteomic databases

PaxDbiP56528.
PeptideAtlasiP56528.
PRIDEiP56528.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030964; ENSMUSP00000030964; ENSMUSG00000029084.
GeneIDi12494.
KEGGimmu:12494.
UCSCiuc008xic.2. mouse.

Organism-specific databases

CTDi952.
MGIiMGI:107474. Cd38.

Phylogenomic databases

eggNOGiENOG410IH8E. Eukaryota.
ENOG4111W33. LUCA.
GeneTreeiENSGT00390000017291.
HOGENOMiHOG000293141.
HOVERGENiHBG005277.
InParanoidiP56528.
KOiK01242.
OMAiCKNIYRP.
OrthoDBiEOG091G0GI3.
PhylomeDBiP56528.
TreeFamiTF332530.

Enzyme and pathway databases

BRENDAi2.4.99.20. 3474.

Miscellaneous databases

ChiTaRSiCd38. mouse.
EvolutionaryTraceiP56528.
PROiP56528.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000029084.
CleanExiMM_CD38.
ExpressionAtlasiP56528. baseline and differential.
GenevisibleiP56528. MM.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR003193. ADP-ribosyl_cyclase.
IPR033567. CD38.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR10912. PTHR10912. 1 hit.
PTHR10912:SF5. PTHR10912:SF5. 1 hit.
PfamiPF02267. Rib_hydrolayse. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCD38_MOUSE
AccessioniPrimary (citable) accession number: P56528
Secondary accession number(s): Q8BFY8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 23, 2004
Last modified: November 2, 2016
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.