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P56528

- CD38_MOUSE

UniProt

P56528 - CD38_MOUSE

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
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 2 (23 Nov 2004)
      Previous versions | rss
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    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

    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

    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

    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

    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

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP56528.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 2121CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini45 – 304260ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei22 – 4423Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ADP-ribosyl cyclase family.Curated

    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

    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:
    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

    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: October 1, 2014
    This is version 113 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