P56528 (CD38_MOUSE) Reviewed, UniProtKB/Swiss-Prot

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
I-19
NIM-R5 antigen
CD_antigen=CD38

Gene names

Name:

Cd38

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	304 AA.
Sequence status	Complete.
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 Transmembrane helix
Ligand	NAD
Molecular function	Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	B cell receptor signaling pathway Inferred from electronic annotation. Source: Compara elevation of cytosolic calcium ion concentration Inferred from electronic annotation. Source: Compara female pregnancy Inferred from electronic annotation. Source: Compara long term synaptic depression Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of bone resorption Inferred from electronic annotation. Source: Compara negative regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: Compara positive regulation of B cell proliferation Inferred from direct assay PubMed 8666928. Source: MGI positive regulation of cell growth Inferred from electronic annotation. Source: Compara positive regulation of insulin secretion Inferred from electronic annotation. Source: Compara positive regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: Compara positive regulation of vasoconstriction Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara response to estradiol stimulus Inferred from electronic annotation. Source: Compara response to hydroperoxide Inferred from electronic annotation. Source: Compara response to hypoxia Inferred from electronic annotation. Source: Compara response to interleukin-1 Inferred from electronic annotation. Source: Compara response to progesterone stimulus Inferred from electronic annotation. Source: Compara response to retinoic acid Inferred from electronic annotation. Source: Compara
Cellular_component	cell surface Inferred from direct assay PubMed 16493007PubMed 9324354. Source: MGI integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW membrane Inferred from direct assay PubMed 12403647. Source: MGI nucleus Inferred from electronic annotation. Source: Compara plasma membrane Inferred from electronic annotation. Source: Compara
Molecular_function	NAD+ nucleosidase activity Inferred from electronic annotation. Source: EC hydrolase activity, acting on glycosyl bonds Inferred from mutant phenotype PubMed 12403647. Source: MGI nucleotide binding Inferred from electronic annotation. Source: InterPro phosphorus-oxygen lyase activity Inferred from mutant phenotype PubMed 12403647. 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

Helical; 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

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

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 [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] [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. , 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]	"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.

IPI

IPI00307966.

PIR

I49586.

RefSeq

NP_031672.2. NM_007646.4.

UniGene

Mm.249873.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

P56528.

SMR

P56528. Positions 50-283.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-59864N.

PTM databases

PhosphoSite

P56528.

Proteomic databases

PaxDb

P56528.

PRIDE

P56528.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000030964; ENSMUSP00000030964; ENSMUSG00000029084.

GeneID

12494.

KEGG

mmu:12494.

Organism-specific databases

CTD

952.

MGI

MGI:107474. Cd38.

Phylogenomic databases

eggNOG

NOG42596.

HOGENOM

HOG000293141.

HOVERGEN

HBG005277.

InParanoid

P56528.

KO

K01242.

OMA

FLQCVKN.

OrthoDB

EOG4H9XMX.

Gene expression databases

ArrayExpress

P56528.

Bgee

P56528.

CleanEx

MM_CD38.

Genevestigator

P56528.

GermOnline

ENSMUSG00000029084. Mus musculus.

Family and domain databases

Gene3D

3.40.50.720. 1 hit.

InterPro

IPR003193. ADP-ribosyl_cyclase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]

PANTHER

PTHR10912. PTHR10912. 1 hit.

Pfam

PF02267. Rib_hydrolayse. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

CD38. mouse.

EvolutionaryTrace

P56528.

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:	April 3, 2013
This is version 102 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program