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P56528 (CD38_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Cd38
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length304 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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 By similarity. Ref.4

Catalytic activity

NAD+ + H2O = ADP-D-ribose + nicotinamide.

NADP+ + nicotinate = nicotinate-adenine dinucleotide phosphate + nicotinamide.

Subcellular location

Membrane; Single-pass type II membrane protein.

Sequence similarities

Belongs to the ADP-ribosyl cyclase family.

Ontologies

Keywords
   Cellular componentMembrane
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   LigandNAD
NADP
   Molecular functionHydrolase
Transferase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

female pregnancy

Inferred from electronic annotation. Source: Ensembl

long term synaptic depression

Inferred from electronic annotation. Source: Ensembl

metabolic process

Inferred from mutant phenotype PubMed 12403647. Source: GOC

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of bone resorption

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

positive regulation of B cell proliferation

Inferred from direct assay PubMed 8666928. Source: MGI

positive regulation of cell growth

Inferred from electronic annotation. Source: Ensembl

positive regulation of cytosolic calcium ion concentration

Inferred from electronic annotation. Source: Ensembl

positive regulation of insulin secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

positive regulation of vasoconstriction

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to estradiol

Inferred from electronic annotation. Source: Ensembl

response to hydroperoxide

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to interleukin-1

Inferred from electronic annotation. Source: Ensembl

response to progesterone

Inferred from electronic annotation. Source: Ensembl

response to retinoic acid

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell surface

Inferred from direct assay PubMed 16493007PubMed 9324354. Source: MGI

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

membrane

Inferred from direct assay PubMed 12403647. Source: MGI

nucleus

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionNAD(P)+ nucleosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

NAD+ nucleosidase activity

Inferred from electronic annotation. Source: Ensembl

hydrolase activity, acting on glycosyl bonds

Inferred from mutant phenotype PubMed 12403647. Source: MGI

phosphorus-oxygen lyase activity

Inferred from mutant phenotype PubMed 12403647. Source: MGI

transferase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 304304ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1
PRO_0000144068

Regions

Topological domain1 – 2121Cytoplasmic Potential
Transmembrane22 – 4423Helical; Signal-anchor for type II membrane protein; Potential
Topological domain45 – 304260Extracellular Potential

Sites

Active site1231 By similarity
Active site2051 By similarity

Amino acid modifications

Glycosylation1041N-linked (GlcNAc...) Potential
Glycosylation1241N-linked (GlcNAc...) Potential
Glycosylation2131N-linked (GlcNAc...) Potential
Glycosylation2231N-linked (GlcNAc...) Potential
Disulfide bond70 ↔ 86 Ref.5
Disulfide bond103 ↔ 184 Ref.5
Disulfide bond164 ↔ 177 Ref.5
Disulfide bond258 ↔ 279 Ref.5
Disulfide bond291 ↔ 300 Ref.5

Experimental info

Sequence conflict1911V → M in AAA03163. Ref.1
Sequence conflict2291V → L in AAA03163. Ref.1

Secondary structure

.................................. 304
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P56528 [UniParc].

Last modified November 23, 2004. Version 2.
Checksum: DD0A7747C5F67D6F

FASTA30434,408
        10         20         30         40         50         60 
MANYEFSQVS GDRPGCRLSR KAQIGLGVGL LVLIALVVGI VVILLRPRSL LVWTGEPTTK 

        70         80         90        100        110        120 
HFSDIFLGRC LIYTQILRPE MRDQNCQEIL STFKGAFVSK NPCNITREDY APLVKLVTQT 

       130        140        150        160        170        180 
IPCNKTLFWS KSKHLAHQYT WIQGKMFTLE DTLLGYIADD LRWCGDPSTS DMNYVSCPHW 

       190        200        210        220        230        240 
SENCPNNPIT VFWKVISQKF AEDACGVVQV MLNGSLREPF YKNSTFGSVE VFSLDPNKVH 

       250        260        270        280        290        300 
KLQAWVMHDI EGASSNACSS SSLNELKMIV QKRNMIFACV DNYRPARFLQ CVKNPEHPSC 


RLNT 

« Hide

References

« Hide 'large scale' references
[1]"Expression cloning of a cDNA encoding a novel murine B cell activation marker. Homology to human CD38."
Harada N., Santos-Argumedo L., Chang R., Grimaldi J.C., Lund F.E., Brannan C.I., Copeland N.G., Jenkins N.A., Heath A.W., Parkhouse R.M.E., Howard M.
J. Immunol. 151:3111-3118(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: B-cell.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Cerebellum, Hypothalamus and Thymus.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Olfactory epithelium.
[4]"CD38 is the major enzyme responsible for synthesis of nicotinic acid-adenine dinucleotide phosphate in mammalian tissues."
Chini E.N., Chini C.C., Kato I., Takasawa S., Okamoto H.
Biochem. J. 362:125-130(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN SYNTHESIS OF NICOTINIC ACID-ADENINE DINUCLEOTIDE PHOSPHATE.
[5]"Crystal structure of the truncated extracellular domain of mouse Cd38."
RIKEN structural genomics initiative (RSGI)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 48-288, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS19265.1.
PIRI49586.
RefSeqNP_031672.2. NM_007646.4.
UniGeneMm.249873.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EG9X-ray2.80A/B48-288[»]
ProteinModelPortalP56528.
SMRP56528. Positions 50-283.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198590. 1 interaction.
DIPDIP-59864N.
IntActP56528. 1 interaction.
MINTMINT-4090243.

PTM databases

PhosphoSiteP56528.

Proteomic databases

MaxQBP56528.
PaxDbP56528.
PRIDEP56528.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030964; ENSMUSP00000030964; ENSMUSG00000029084.
GeneID12494.
KEGGmmu:12494.
UCSCuc008xic.2. mouse.

Organism-specific databases

CTD952.
MGIMGI:107474. Cd38.

Phylogenomic databases

eggNOGNOG42596.
HOGENOMHOG000293141.
HOVERGENHBG005277.
InParanoidP56528.
KOK01242.
OMAKNPCNIT.
OrthoDBEOG7RBZ9B.
PhylomeDBP56528.
TreeFamTF332530.

Gene expression databases

ArrayExpressP56528.
BgeeP56528.
CleanExMM_CD38.
GenevestigatorP56528.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR003193. ADP-ribosyl_cyclase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR10912. PTHR10912. 1 hit.
PfamPF02267. Rib_hydrolayse. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCD38. mouse.
EvolutionaryTraceP56528.
NextBio281424.
PROP56528.
SOURCESearch...

Entry information

Entry nameCD38_MOUSE
AccessionPrimary (citable) accession number: P56528
Secondary accession number(s): Q8BFY8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 23, 2004
Last modified: July 9, 2014
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot