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Q9MZ03 (CD38_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
ADP-ribosyl cyclase 1
EC=3.2.2.5
Alternative name(s):
Cyclic ADP-ribose hydrolase 1
Short name=cADPr hydrolase 1
CD_antigen=CD38
Gene names
Name:CD38
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length298 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.1 Ref.3

Catalytic activity

NAD+ + H2O = ADP-ribose + nicotinamide.

Subcellular location

Cell membrane; Single-pass type II membrane protein. Microsome membrane; Single-pass type II membrane protein. Endoplasmic reticulum membrane; Single-pass type II membrane protein Ref.1 Ref.3.

Tissue specificity

Osteoclasts. Ref.1

Sequence similarities

Belongs to the ADP-ribosyl cyclase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 298298ADP-ribosyl cyclase 1
PRO_0000144069

Regions

Topological domain1 – 2121Cytoplasmic Potential
Transmembrane22 – 4221Helical; Signal-anchor for type II membrane protein; Potential
Topological domain43 – 298256Extracellular Potential

Sites

Active site1171 By similarity
Active site1991 By similarity

Amino acid modifications

Glycosylation981N-linked (GlcNAc...) Potential
Glycosylation1181N-linked (GlcNAc...) Potential
Glycosylation1771N-linked (GlcNAc...) Potential
Glycosylation2071N-linked (GlcNAc...) Potential
Glycosylation2681N-linked (GlcNAc...) Potential
Disulfide bond64 ↔ 80 By similarity
Disulfide bond97 ↔ 178 By similarity
Disulfide bond158 ↔ 171 By similarity
Disulfide bond252 ↔ 273 By similarity
Disulfide bond285 ↔ 294 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9MZ03 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 7A4942F5A4625B60

FASTA29833,637
        10         20         30         40         50         60 
MPDYEFSPAS GDRPRSWISK QVLIVLGVCL PVILALAIWV GVLTWRQSSM GATDHVSAIV 

        70         80         90        100        110        120 
LGRCLTYTRN MHPELRNQDC KKILNTFTSA FVSKDPCNIT KEDYQPLIDL VTQTVPCNKT 

       130        140        150        160        170        180 
LFWSRSKELA HQYSGIQKEM FTLEDTLLGY IADNLVWCGD PRTSEVKEEF CPYRNENCSS 

       190        200        210        220        230        240 
TATSVFWTVV SQKFAESACG TVYVMLNGSR TTAFSKASTF GSVEVFNLHP DRVHTLHAWV 

       250        260        270        280        290 
MHDIGGVERD SCLGSSIKEL KSIVNQRNIS FFCQDDYRPA RFVQCVRHPE HPSCSVLM

« Hide

References

[1]"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: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION.
Tissue: Osteoclast.
[2]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)
[3]"Molecular cloning, expression, and functional characterization of a novel member of the CD38 family of ADP-ribosyl cyclases."
Adebanjo O.A., Koval A., Moonga B.S., Wu X.B., Yao S., Bevis P.J.R., Kumegawa M., Zaidi M., Sun L.
Biochem. Biophys. Res. Commun. 273:884-889(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION.
Tissue: Osteoclast.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF272974 mRNA. Translation: AAF87715.1.
PIRJC7323.
RefSeqNP_001076152.1. NM_001082683.1.
UniGeneOcu.1561.

3D structure databases

ProteinModelPortalQ9MZ03.
SMRQ9MZ03. Positions 49-277.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100009409.

Organism-specific databases

CTD952.

Phylogenomic databases

eggNOGNOG42596.
HOGENOMHOG000293141.
HOVERGENHBG005277.
OrthoDBEOG4H9XMX.

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...

Entry information

Entry nameCD38_RABIT
AccessionPrimary (citable) accession number: Q9MZ03
Entry history
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: October 1, 2000
Last modified: April 3, 2013
This is version 76 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

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