Reviewed, UniProtKB/Swiss-Prot Q9MZ03 (CD38_RABIT)

Names and origin

Protein names

Recommended 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

Organism

Oryctolagus cuniculus (Rabbit)

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length	298 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Cell membrane Endoplasmic reticulum Membrane Microsome
Domain	Signal-anchor Transmembrane
Ligand	NAD
Molecular function	Hydrolase
PTM	Disulfide bond Glycoprotein
Gene Ontology (GO)
Biological process	intracellular signaling cascade Ref.1 Inferred from direct assay. Source: UniProtKB metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW microsome Ref.3 Inferred from direct assay. Source: UniProtKB plasma membrane Ref.1 Inferred from direct assay. Source: UniProtKB
Molecular function	NAD+ nucleosidase activity Ref.1 Ref.3 Inferred from direct assay. Source: UniProtKB binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 298	298	ADP-ribosyl cyclase 1		PRO_0000144069
Regions
	Topological domain	1 – 21	21	Cytoplasmic Potential
	Transmembrane	22 – 42	21	Signal-anchor for type II membrane protein Potential
	Topological domain	43 – 298	256	Extracellular Potential
Sites
	Active site	117	1	By similarity
	Active site	199	1	By similarity
Amino acid modifications
	Glycosylation	98	1	N-linked (GlcNAc...) Potential
	Glycosylation	118	1	N-linked (GlcNAc...) Potential
	Glycosylation	177	1	N-linked (GlcNAc...) Potential
	Glycosylation	207	1	N-linked (GlcNAc...) Potential
	Glycosylation	268	1	N-linked (GlcNAc...) Potential
	Disulfide bond	64 ↔ 80		By similarity
	Disulfide bond	97 ↔ 178		By similarity
	Disulfide bond	158 ↔ 171		By similarity
	Disulfide bond	252 ↔ 273		By similarity
	Disulfide bond	285 ↔ 294		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9MZ03-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 7A4942F5A4625B60	FASTA	298	33,637
	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

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: 10477767] [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: 10891341] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION. Tissue: Osteoclast.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF272974 mRNA. Translation: AAF87715.1.
PIR	JC7323.
RefSeq	NP_001076152.1.
UniGene	Ocu.6154
3D structure databases
HSSP	HSSP built from PDB template 1ISI based on UniProtKB Q10588.
ModBase	Search...
Genome annotation databases
GeneID	100009409.
Phylogenomic databases
HOVERGEN	Q9MZ03.
Enzyme and pathway databases
BRENDA	3.2.2.5. 255.
Family and domain databases
InterPro	IPR003193. ADP-ribosyl_cyclase. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 2 hits.
PANTHER	PTHR10912. Rib_hydrolayse. 1 hit.
Pfam	PF02267. Rib_hydrolayse. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CD38_RABIT

Accession

Primary (citable) accession number: Q9MZ03

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 27, 2002
Last sequence update:	October 1, 2000
Last modified:	June 16, 2009
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)