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P56528

- CD38_MOUSE

UniProt

P56528 - CD38_MOUSE

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Protein

ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1

Gene
Cd38
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.1 Publication

Catalytic activityi

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

Sites

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

GO - Molecular functioni

  1. hydrolase activity, acting on glycosyl bonds Source: MGI
  2. NAD(P)+ nucleosidase activity Source: UniProtKB-EC
  3. NAD+ nucleosidase activity Source: Ensembl
  4. phosphorus-oxygen lyase activity Source: MGI
  5. transferase activity Source: UniProtKB-KW

GO - Biological processi

  1. B cell receptor signaling pathway Source: Ensembl
  2. female pregnancy Source: Ensembl
  3. long term synaptic depression Source: Ensembl
  4. metabolic process Source: GOC
  5. negative regulation of apoptotic process Source: Ensembl
  6. negative regulation of bone resorption Source: Ensembl
  7. negative regulation of transcription, DNA-templated Source: Ensembl
  8. positive regulation of B cell proliferation Source: MGI
  9. positive regulation of cell growth Source: Ensembl
  10. positive regulation of cytosolic calcium ion concentration Source: Ensembl
  11. positive regulation of insulin secretion Source: Ensembl
  12. positive regulation of transcription, DNA-templated Source: Ensembl
  13. positive regulation of vasoconstriction Source: Ensembl
  14. response to drug Source: Ensembl
  15. response to estradiol Source: Ensembl
  16. response to hydroperoxide Source: Ensembl
  17. response to hypoxia Source: Ensembl
  18. response to interleukin-1 Source: Ensembl
  19. response to progesterone Source: Ensembl
  20. response to retinoic acid Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transferase

Keywords - Ligandi

NAD, NADP

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: Chromosome 5

Organism-specific databases

MGIiMGI:107474. Cd38.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2121Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei22 – 4423Helical; Signal-anchor for type II membrane protein; Reviewed predictionAdd
BLAST
Topological domaini45 – 304260Extracellular Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. cell surface Source: MGI
  2. integral component of membrane Source: UniProtKB-KW
  3. membrane Source: MGI
  4. nucleus Source: Ensembl
  5. plasma membrane Source: Ensembl
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...) Reviewed prediction
Glycosylationi124 – 1241N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi164 ↔ 1771 Publication
Glycosylationi213 – 2131N-linked (GlcNAc...) Reviewed prediction
Glycosylationi223 – 2231N-linked (GlcNAc...) Reviewed prediction
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

ArrayExpressiP56528.
BgeeiP56528.
CleanExiMM_CD38.
GenevestigatoriP56528.

Interactioni

Protein-protein interaction databases

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

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EG9X-ray2.80A/B48-288[»]
ProteinModelPortaliP56528.
SMRiP56528. Positions 50-283.

Miscellaneous databases

EvolutionaryTraceiP56528.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG42596.
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

MANYEFSQVS GDRPGCRLSR KAQIGLGVGL LVLIALVVGI VVILLRPRSL    50
LVWTGEPTTK HFSDIFLGRC LIYTQILRPE MRDQNCQEIL STFKGAFVSK 100
NPCNITREDY APLVKLVTQT IPCNKTLFWS KSKHLAHQYT WIQGKMFTLE 150
DTLLGYIADD LRWCGDPSTS DMNYVSCPHW SENCPNNPIT VFWKVISQKF 200
AEDACGVVQV MLNGSLREPF YKNSTFGSVE VFSLDPNKVH KLQAWVMHDI 250
EGASSNACSS SSLNELKMIV QKRNMIFACV DNYRPARFLQ CVKNPEHPSC 300
RLNT 304
Length:304
Mass (Da):34,408
Last modified:November 23, 2004 - v2
Checksum:iDD0A7747C5F67D6F
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti191 – 1911V → M in AAA03163. 1 Publication
Sequence conflicti229 – 2291V → L in AAA03163. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS19265.1.
PIRi I49586.
RefSeqi NP_031672.2. NM_007646.4.
UniGenei Mm.249873.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2EG9 X-ray 2.80 A/B 48-288 [» ]
ProteinModelPortali P56528.
SMRi P56528. Positions 50-283.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198590. 1 interaction.
DIPi DIP-59864N.
IntActi P56528. 1 interaction.
MINTi MINT-4090243.

PTM databases

PhosphoSitei P56528.

Proteomic databases

MaxQBi P56528.
PaxDbi P56528.
PRIDEi P56528.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000030964 ; ENSMUSP00000030964 ; ENSMUSG00000029084 .
GeneIDi 12494.
KEGGi mmu:12494.
UCSCi uc008xic.2. mouse.

Organism-specific databases

CTDi 952.
MGIi MGI:107474. Cd38.

Phylogenomic databases

eggNOGi NOG42596.
HOGENOMi HOG000293141.
HOVERGENi HBG005277.
InParanoidi P56528.
KOi K01242.
OMAi KNPCNIT.
OrthoDBi EOG7RBZ9B.
PhylomeDBi P56528.
TreeFami TF332530.

Miscellaneous databases

ChiTaRSi CD38. mouse.
EvolutionaryTracei P56528.
NextBioi 281424.
PROi P56528.
SOURCEi Search...

Gene expression databases

ArrayExpressi P56528.
Bgeei P56528.
CleanExi MM_CD38.
Genevestigatori P56528.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
InterProi IPR003193. ADP-ribosyl_cyclase.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
PANTHERi PTHR10912. PTHR10912. 1 hit.
Pfami PF02267. Rib_hydrolayse. 1 hit.
[Graphical view ]
ProtoNeti Search...

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 9, 2014
This is version 112 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

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