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Q64244 (CD38_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 1

EC=3.2.2.5
Alternative name(s):
CD38H
Cyclic ADP-ribose hydrolase 1
Short name=cADPr hydrolase 1
CD_antigen=CD38
Gene names
Name:Cd38
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length303 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Synthesizes cyclic ADP-ribose, a second messenger for glucose-induced insulin secretion. Also has cADPr hydrolase activity. Ref.4

Regulates osteoclastic bone resorption, probably via production of cyclic ADP-ribose and triggering of a cytosolic calcium ion signal through ryanodine receptor activation. Ref.4

Catalytic activity

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

Subcellular location

Membrane; Single-pass type II membrane protein.

Tissue specificity

Spleen, liver, heart, thymus, thyroid gland, ileum, colon, cerebellum, salivary gland, adrenal gland, jejunum, islets of Langerhans and osteoclasts. Ref.4

Sequence similarities

Belongs to the ADP-ribosyl cyclase family.

Ontologies

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

Inferred from electronic annotation. Source: Ensembl

female pregnancy

Inferred from expression pattern PubMed 14998907. Source: RGD

long term synaptic depression

Inferred from mutant phenotype PubMed 10097163. Source: RGD

metabolic process

Inferred from direct assay PubMed 11733184. Source: GOC

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of bone resorption

Inferred from direct assay Ref.4. Source: RGD

negative regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

positive regulation of B cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell growth

Inferred from mutant phenotype PubMed 18719074. Source: RGD

positive regulation of cytosolic calcium ion concentration

Inferred from mutant phenotype PubMed 18719074. Source: RGD

positive regulation of insulin secretion

Inferred from mutant phenotype PubMed 9664081. Source: RGD

positive regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

positive regulation of vasoconstriction

Inferred from mutant phenotype PubMed 18524860. Source: RGD

response to cytokine

Inferred from expression pattern PubMed 11399650. Source: RGD

response to drug

Inferred from electronic annotation. Source: Ensembl

response to estradiol

Inferred from expression pattern PubMed 14998907. Source: RGD

response to hormone

Inferred from direct assay PubMed 9325179. Source: RGD

response to hydroperoxide

Inferred from direct assay PubMed 12893282. Source: RGD

response to hypoxia

Inferred from direct assay PubMed 12111041. Source: RGD

response to interleukin-1

Inferred from expression pattern PubMed 11399650. Source: RGD

response to progesterone

Inferred from expression pattern PubMed 14998907. Source: RGD

response to retinoic acid

Inferred from expression pattern PubMed 11399650. Source: RGD

   Cellular_componentcell surface

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

intracellular membrane-bounded organelle

Inferred from direct assay PubMed 11733184. Source: RGD

nucleus

Inferred from direct assay PubMed 11733184. Source: RGD

plasma membrane

Inferred from direct assay PubMed 17200192. Source: RGD

   Molecular_functionNAD+ nucleosidase activity

Inferred from direct assay PubMed 11733184. Source: RGD

phosphorus-oxygen lyase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 303303ADP-ribosyl cyclase 1
PRO_0000144070

Regions

Topological domain1 – 2121Cytoplasmic Potential
Transmembrane22 – 4423Helical; Signal-anchor for type II membrane protein; Potential
Topological domain45 – 303259Extracellular Potential

Sites

Active site1221 By similarity
Active site2041 By similarity

Amino acid modifications

Glycosylation1031N-linked (GlcNAc...) Potential
Glycosylation1231N-linked (GlcNAc...) Potential
Glycosylation2121N-linked (GlcNAc...) Potential
Glycosylation2221N-linked (GlcNAc...) Potential
Disulfide bond69 ↔ 85 By similarity
Disulfide bond102 ↔ 183 By similarity
Disulfide bond163 ↔ 176 By similarity
Disulfide bond257 ↔ 278 By similarity
Disulfide bond290 ↔ 299 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q64244 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 84F23AD3094871C5

FASTA30334,436
        10         20         30         40         50         60 
MANYEFSQVS EDRPGCRLTR KAQIGLGVGL LLLVALVVVV VIVLWPRSPL VWKGKPTTKH 

        70         80         90        100        110        120 
FADIILGRCL IYTQILRPEM RDQDCKKILS TFKRGFISKN PCNITNEDYA PLVKLVTQTI 

       130        140        150        160        170        180 
PCNKTLFWSK SKHLAHQYTW IQGKMFTLED TLLGYIADDL RWCGDPSTSD MNYDSCPHWS 

       190        200        210        220        230        240 
ENCPNNPVAV FWNVISQKFA EDACGVVQVM LNGSLSEPFY RNSTFGSVEV FNLDPNKVHK 

       250        260        270        280        290        300 
LQAWVMHDIK GTSSNACSSP SINELKSIVN KRNMIFACQD NYRPVRFLQC VKNPEHPSCR 


LNV 

« Hide

References

[1]"A cloned rat CD38-homologous protein and its expression in pancreatic islets."
Li Q., Yamada Y., Yasuda K., Ihara Y., Okamoto Y., Kaisaki P.J., Watanabe R., Ikeda H., Tsuda K., Seino Y.
Biochem. Biophys. Res. Commun. 202:629-636(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
Tissue: Brain.
[2]Erratum
Li Q., Yamada Y., Yasuda K., Ihara Y., Okamoto Y., Kaisaki P.J., Watanabe R., Ikeda H., Tsuda K., Seino Y.
Biochem. Biophys. Res. Commun. 204:1001-1001(1994)
[3]"Cloning and characterization of cDNA encoding rat ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase (homologue to human CD38) from islets of Langerhans."
Koguma T., Takasawa S., Tohgo A., Karasawa T., Furuya Y., Yonekura H., Okamoto H.
Biochim. Biophys. Acta 1223:160-162(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
Tissue: Pancreatic islet.
[4]"CD38/ADP-ribosyl cyclase: a new role in the regulation of osteoclastic bone resorption."
Sun L., Adebanjo O.A., Moonga B.S., Corisdeo S., Anandatheerthavarada H.K., Biswas G., Arakawa T., Hakeda Y., Koval A., Sodam B., Bevis P.J.R., Moser A.J., Lai F.A., Epstein S., Troen B.R., Kumegawa M., Zaidi M.
J. Cell Biol. 146:1161-1172(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[5]Erratum
Sun L., Adebanjo O.A., Moonga B.S., Corisdeo S., Anandatheerthavarada H.K., Biswas G., Arakawa T., Hakeda Y., Koval A., Sodam B., Bevis P.J.R., Moser A.J., Lai F.A., Epstein S., Troen B.R., Kumegawa M., Zaidi M.
J. Cell Biol. 146:1391-1392(1999)
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D30795 mRNA. Translation: BAA06457.1.
D29646 mRNA. Translation: BAA06129.1.
PIRJC2410.
RefSeqNP_037259.1. NM_013127.1.
UniGeneRn.11414.

3D structure databases

ProteinModelPortalQ64244.
SMRQ64244. Positions 50-282.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000004121.

Proteomic databases

PRIDEQ64244.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000004121; ENSRNOP00000004121; ENSRNOG00000003069.
GeneID25668.
KEGGrno:25668.

Organism-specific databases

CTD952.
RGD2303. Cd38.

Phylogenomic databases

eggNOGNOG42596.
GeneTreeENSGT00390000017291.
HOGENOMHOG000293141.
HOVERGENHBG005277.
InParanoidQ64244.
KOK01242.
OMAQTVPCNK.
OrthoDBEOG7RBZ9B.
PhylomeDBQ64244.
TreeFamTF332530.

Enzyme and pathway databases

SABIO-RKQ64244.

Gene expression databases

GenevestigatorQ64244.

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

NextBio607593.
PROQ64244.

Entry information

Entry nameCD38_RAT
AccessionPrimary (citable) accession number: Q64244
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 109 of the entry and version 1 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