Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1

Gene

Cd38

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Synthesizes the second messagers cyclic ADP-ribose and nicotinate-adenine dinucleotide phosphate, the former a second messenger for glucose-induced insulin secretion. Also has cADPr hydrolase activity (By similarity).By similarity

Catalytic activityi

NAD+ + H2O = ADP-D-ribose + nicotinamide.
NADP+ + nicotinate = nicotinate-adenine dinucleotide phosphate + nicotinamide.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei123 – 1231By similarity
Active sitei205 – 2051By similarity

GO - Molecular functioni

  • hydrolase activity, acting on glycosyl bonds Source: MGI
  • NAD(P)+ nucleosidase activity Source: UniProtKB-EC
  • NAD+ nucleosidase activity Source: GO_Central
  • phosphorus-oxygen lyase activity Source: MGI
  • transferase activity Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transferase

Keywords - Ligandi

NAD, NADP

Enzyme and pathway databases

BRENDAi2.4.99.20. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1 (EC:3.2.2.6)
Alternative name(s):
2'-phospho-ADP-ribosyl cyclase
2'-phospho-ADP-ribosyl cyclase/2'-phospho-cyclic-ADP-ribose transferase (EC:2.4.99.20)
2'-phospho-cyclic-ADP-ribose transferase
ADP-ribosyl cyclase 1
Short name:
ADPRC 1
Cyclic ADP-ribose hydrolase 1
Short name:
cADPr hydrolase 1
I-19
NIM-R5 antigen
CD_antigen: CD38
Gene namesi
Name:Cd38
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:107474. Cd38.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2121CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei22 – 4423Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini45 – 304260ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • cell surface Source: MGI
  • cytosol Source: GOC
  • extracellular exosome Source: MGI
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: MGI
  • nucleus Source: Ensembl
  • plasma membrane Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 304304ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1PRO_0000144068Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi70 ↔ 861 Publication
Disulfide bondi103 ↔ 1841 Publication
Glycosylationi104 – 1041N-linked (GlcNAc...)Sequence Analysis
Glycosylationi124 – 1241N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi164 ↔ 1771 Publication
Glycosylationi213 – 2131N-linked (GlcNAc...)Sequence Analysis
Glycosylationi223 – 2231N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi258 ↔ 2791 Publication
Disulfide bondi291 ↔ 3001 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP56528.
PaxDbiP56528.
PRIDEiP56528.

PTM databases

PhosphoSiteiP56528.

Expressioni

Gene expression databases

BgeeiP56528.
CleanExiMM_CD38.
ExpressionAtlasiP56528. baseline and differential.
GenevisibleiP56528. MM.

Interactioni

Protein-protein interaction databases

BioGridi198590. 1 interaction.
DIPiDIP-59864N.
IntActiP56528. 1 interaction.
MINTiMINT-4090243.
STRINGi10090.ENSMUSP00000030964.

Structurei

Secondary structure

1
304
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi62 – 7514Combined sources
Helixi79 – 813Combined sources
Helixi86 – 9712Combined sources
Helixi107 – 1104Combined sources
Helixi111 – 1166Combined sources
Helixi149 – 1513Combined sources
Helixi153 – 1586Combined sources
Helixi188 – 20316Combined sources
Beta strandi206 – 21914Combined sources
Helixi225 – 2284Combined sources
Helixi230 – 2334Combined sources
Turni236 – 2383Combined sources
Beta strandi239 – 2479Combined sources
Beta strandi250 – 2523Combined sources
Helixi257 – 2593Combined sources
Helixi261 – 27111Combined sources
Turni272 – 2743Combined sources
Beta strandi276 – 2827Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EG9X-ray2.80A/B48-288[»]
ProteinModelPortaliP56528.
SMRiP56528. Positions 50-283.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56528.

Family & Domainsi

Sequence similaritiesi

Belongs to the ADP-ribosyl cyclase family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG42596.
GeneTreeiENSGT00390000017291.
HOGENOMiHOG000293141.
HOVERGENiHBG005277.
InParanoidiP56528.
KOiK01242.
OMAiKNPCNIT.
OrthoDBiEOG7RBZ9B.
PhylomeDBiP56528.
TreeFamiTF332530.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR003193. ADP-ribosyl_cyclase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR10912. PTHR10912. 1 hit.
PfamiPF02267. Rib_hydrolayse. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P56528-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANYEFSQVS GDRPGCRLSR KAQIGLGVGL LVLIALVVGI VVILLRPRSL
60 70 80 90 100
LVWTGEPTTK HFSDIFLGRC LIYTQILRPE MRDQNCQEIL STFKGAFVSK
110 120 130 140 150
NPCNITREDY APLVKLVTQT IPCNKTLFWS KSKHLAHQYT WIQGKMFTLE
160 170 180 190 200
DTLLGYIADD LRWCGDPSTS DMNYVSCPHW SENCPNNPIT VFWKVISQKF
210 220 230 240 250
AEDACGVVQV MLNGSLREPF YKNSTFGSVE VFSLDPNKVH KLQAWVMHDI
260 270 280 290 300
EGASSNACSS SSLNELKMIV QKRNMIFACV DNYRPARFLQ CVKNPEHPSC

RLNT
Length:304
Mass (Da):34,408
Last modified:November 23, 2004 - v2
Checksum:iDD0A7747C5F67D6F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti191 – 1911V → M in AAA03163 (PubMed:8376770).Curated
Sequence conflicti229 – 2291V → L in AAA03163 (PubMed:8376770).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS19265.1.
PIRiI49586.
RefSeqiNP_031672.2. NM_007646.4.
UniGeneiMm.249873.

Genome annotation databases

EnsembliENSMUST00000030964; ENSMUSP00000030964; ENSMUSG00000029084.
GeneIDi12494.
KEGGimmu:12494.
UCSCiuc008xic.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS19265.1.
PIRiI49586.
RefSeqiNP_031672.2. NM_007646.4.
UniGeneiMm.249873.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EG9X-ray2.80A/B48-288[»]
ProteinModelPortaliP56528.
SMRiP56528. Positions 50-283.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198590. 1 interaction.
DIPiDIP-59864N.
IntActiP56528. 1 interaction.
MINTiMINT-4090243.
STRINGi10090.ENSMUSP00000030964.

PTM databases

PhosphoSiteiP56528.

Proteomic databases

MaxQBiP56528.
PaxDbiP56528.
PRIDEiP56528.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030964; ENSMUSP00000030964; ENSMUSG00000029084.
GeneIDi12494.
KEGGimmu:12494.
UCSCiuc008xic.2. mouse.

Organism-specific databases

CTDi952.
MGIiMGI:107474. Cd38.

Phylogenomic databases

eggNOGiNOG42596.
GeneTreeiENSGT00390000017291.
HOGENOMiHOG000293141.
HOVERGENiHBG005277.
InParanoidiP56528.
KOiK01242.
OMAiKNPCNIT.
OrthoDBiEOG7RBZ9B.
PhylomeDBiP56528.
TreeFamiTF332530.

Enzyme and pathway databases

BRENDAi2.4.99.20. 3474.

Miscellaneous databases

ChiTaRSiCd38. mouse.
EvolutionaryTraceiP56528.
NextBioi281424.
PROiP56528.
SOURCEiSearch...

Gene expression databases

BgeeiP56528.
CleanExiMM_CD38.
ExpressionAtlasiP56528. baseline and differential.
GenevisibleiP56528. MM.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR003193. ADP-ribosyl_cyclase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR10912. PTHR10912. 1 hit.
PfamiPF02267. Rib_hydrolayse. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "CD38 is the major enzyme responsible for synthesis of nicotinic acid-adenine dinucleotide phosphate in mammalian tissues."
    Chini E.N., Chini C.C., Kato I., Takasawa S., Okamoto H.
    Biochem. J. 362:125-130(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SYNTHESIS OF NICOTINIC ACID-ADENINE DINUCLEOTIDE PHOSPHATE.
  5. "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.

Entry informationi

Entry nameiCD38_MOUSE
AccessioniPrimary (citable) accession number: P56528
Secondary accession number(s): Q8BFY8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 23, 2004
Last modified: July 22, 2015
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.