Reviewed, UniProtKB/Swiss-Prot P56528 (CD38_MOUSE)

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
    NIM-R5 antigen
    I-19
    CD_antigen=CD38

Gene names

Name:

Cd38

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	304 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Synthesizes cyclic ADP-ribose, a second messenger for glucose-induced insulin secretion. Also has cADPr hydrolase activity By similarity.
Catalytic activity	NAD+ + H2O = ADP-ribose + nicotinamide.
Subcellular location	Membrane; Single-pass type II membrane protein.
Sequence similarities	Belongs to the ADP-ribosyl cyclase family.

Ontologies

Keywords
Cellular component	Membrane
Domain	Signal-anchor Transmembrane
Ligand	NAD
Molecular function	Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	metabolic process Inferred from electronic annotation. Source: InterPro positive regulation of B cell proliferation Inferred from direct assay. Source: MGI
Cellular component	cell surface Inferred from direct assay. Source: MGI integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell membrane fraction Inferred from direct assay. Source: MGI
Molecular function	NAD+ nucleosidase activity Inferred from electronic annotation. Source: EC binding Inferred from electronic annotation. Source: InterPro phosphorus-oxygen lyase activity Inferred from mutant phenotype. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 304

304

ADP-ribosyl cyclase 1

PRO_0000144068

Regions

Topological domain

1 – 21

21

Cytoplasmic Potential

Transmembrane

22 – 44

23

Signal-anchor for type II membrane protein Potential

Topological domain

45 – 304

260

Extracellular Potential

Sites

Active site

123

1

By similarity

Active site

205

1

By similarity

Amino acid modifications

Glycosylation

104

1

N-linked (GlcNAc...) Potential

Glycosylation

124

1

N-linked (GlcNAc...) Potential

Glycosylation

213

1

N-linked (GlcNAc...) Potential

Glycosylation

223

1

N-linked (GlcNAc...) Potential

Disulfide bond

70 ↔ 86

Ref.4

Disulfide bond

103 ↔ 184

Ref.4

Disulfide bond

164 ↔ 177

Ref.4

Disulfide bond

258 ↔ 279

Ref.4

Disulfide bond

291 ↔ 300

Ref.4

Experimental info

Sequence conflict

191

1

V → M in AAA03163. Ref.1

Sequence conflict

229

1

V → L in AAA03163. Ref.1

Secondary structure

1

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304

Helix Strand Turn

Details...

Helix

62 – 75

14

Helix

79 – 81

3

Helix

86 – 97

12

Helix

107 – 110

4

Helix

111 – 116

6

Helix

149 – 151

3

Helix

153 – 158

6

Helix

188 – 203

16

Beta strand

206 – 219

14

Helix

225 – 228

4

Helix

230 – 233

4

Turn

236 – 238

3

Beta strand

239 – 247

9

Beta strand

250 – 252

3

Helix

257 – 259

3

Helix

261 – 271

11

Turn

272 – 274

3

Beta strand

276 – 282

7

Sequences

	Sequence		Length	Mass (Da)
	P56528-1 [UniParc]. Last modified November 23, 2004. Version 2. Checksum: DD0A7747C5F67D6F	FASTA	304	34,408
	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

References

	« Hide 'large scale' referencesShow '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: 8376770] [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. , 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: 16141072] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Olfactory epithelium.
[4]	"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

EMBLGenBankDDBJ

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.

IPI

IPI00307966.

PIR

I49586.

RefSeq

NP_031672.2.

UniGene

Mm.249873

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2EG9	X-ray	2.80	A/B	48-288	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P56528.

Proteomic databases

PRIDE

P56528.

Genome annotation databases

Ensembl

ENSMUST00000030964; ENSMUSP00000030964; ENSMUSG00000029084; Mus musculus. [Genome view]

GeneID

12494.

KEGG

mmu:12494.

UCSC

uc008xic.1. mouse.

Organism-specific databases

CTD

12494.

MGI

MGI:107474. Cd38.

Phylogenomic databases

HOGENOM

P56528.

HOVERGEN

P56528.

OMA

QCVKNPE.

Enzyme and pathway databases

BRENDA

3.2.2.5. 244.

Gene expression databases

ArrayExpress

P56528.

Bgee

P56528.

CleanEx

MM_CD38.

Genevestigator

P56528.

GermOnline

ENSMUSG00000029084. Mus musculus.

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. 1 hit.

PANTHER

PTHR10912. Rib_hydrolayse. 1 hit.

Pfam

PF02267. Rib_hydrolayse. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

281424.

SOURCE

Search...

Entry information

Entry name

CD38_MOUSE

Accession

Primary (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:	November 3, 2009
This is version 73 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)