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Q64277

- BST1_MOUSE

UniProt

Q64277 - BST1_MOUSE

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Protein

ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2

Gene

Bst1

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 that elicits calcium release from intracellular stores. May be involved in pre-B-cell growth.

Catalytic activityi

NAD+ + H2O = ADP-D-ribose + nicotinamide.

GO - Molecular functioni

  1. NAD(P)+ nucleosidase activity Source: UniProtKB-EC
  2. NAD+ nucleosidase activity Source: InterPro
  3. transferase activity Source: UniProtKB-KW
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 2 (EC:3.2.2.6)
Alternative name(s):
ADP-ribosyl cyclase 2
Antigen BP3
BP-3 alloantigen
Bone marrow stromal antigen 1
Short name:
BST-1
Cyclic ADP-ribose hydrolase 2
Short name:
cADPr hydrolase 2
Leukocyte antigen 65
Short name:
Ly-65
CD_antigen: CD157
Gene namesi
Name:Bst1
Synonyms:Bp-3, Bp3, Ly65
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:105370. Bst1.

Subcellular locationi

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. extracellular vesicular exosome Source: Ensembl
  3. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 24241 PublicationAdd
BLAST
Chaini25 – 286262ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2PRO_0000004034Add
BLAST
Propeptidei287 – 31125Sequence AnalysisPRO_0000004035Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi46 ↔ 60By similarity
Glycosylationi59 – 591N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi76 ↔ 156By similarity
Glycosylationi88 – 881N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi137 ↔ 150By similarity
Glycosylationi141 – 1411N-linked (GlcNAc...)Sequence Analysis
Glycosylationi185 – 1851N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi231 ↔ 252By similarity
Disulfide bondi264 ↔ 273By similarity
Lipidationi286 – 2861GPI-anchor amidated serineSequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

MaxQBiQ64277.
PaxDbiQ64277.
PRIDEiQ64277.

PTM databases

PhosphoSiteiQ64277.

Expressioni

Tissue specificityi

Expressed in the bone marrow, spleen and thymus in lymphoid organs, and the lung, kidney and heart in non-lymphoid organs.

Gene expression databases

BgeeiQ64277.
CleanExiMM_BST1.
ExpressionAtlasiQ64277. baseline and differential.
GenevestigatoriQ64277.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiQ64277. 1 interaction.
MINTiMINT-4089430.
STRINGi10090.ENSMUSP00000098796.

Structurei

3D structure databases

ProteinModelPortaliQ64277.
SMRiQ64277. Positions 29-275.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ADP-ribosyl cyclase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG42584.
GeneTreeiENSGT00390000017291.
HOGENOMiHOG000293141.
HOVERGENiHBG097049.
InParanoidiQ64277.
KOiK18152.
OrthoDBiEOG7RBZ9B.
PhylomeDBiQ64277.
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q64277-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAVQGGLLSL WLWLWLSLLT VLLGARARWR GEGTTPHLQS IFLGRCAEYT
60 70 80 90 100
TLLSLGNKNC TAIWEAFKGV LDKDPCSVLP SDYDLFINLS RHPIPRDKSL
110 120 130 140 150
FWENNHLLVM SYGENTRRLV ALCDVLYGKV GDFLSWCRQE NASGLDYQSC
160 170 180 190 200
PTSEDCENNA VDSYWKSASM QYSRDSSGVI NVMLNGSEPK GAYPTRGFFA
210 220 230 240 250
DFEIPYLQKD KVTRIEIWVM HDVGGPNVES CGEGSVKILE DRLEALGFQH
260 270 280 290 300
SCINDYRPVK FLMCVDHSTH PDCIMNSASA SMRRESASLH AIGDASLLIS
310
LLVALASSSQ A
Length:311
Mass (Da):34,616
Last modified:November 1, 1996 - v1
Checksum:i5663D3427E460AD7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 301R → T in BAC30804. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L32812 mRNA. Translation: AAA67046.1.
D31788 mRNA. Translation: BAA06597.1.
AK041059 mRNA. Translation: BAC30804.1.
CCDSiCCDS19264.1.
PIRiJC2541.
RefSeqiNP_033893.2. NM_009763.3.
UniGeneiMm.246332.

Genome annotation databases

EnsembliENSMUST00000101237; ENSMUSP00000098796; ENSMUSG00000029082.
GeneIDi12182.
KEGGimmu:12182.
UCSCiuc008xia.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L32812 mRNA. Translation: AAA67046.1 .
D31788 mRNA. Translation: BAA06597.1 .
AK041059 mRNA. Translation: BAC30804.1 .
CCDSi CCDS19264.1.
PIRi JC2541.
RefSeqi NP_033893.2. NM_009763.3.
UniGenei Mm.246332.

3D structure databases

ProteinModelPortali Q64277.
SMRi Q64277. Positions 29-275.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q64277. 1 interaction.
MINTi MINT-4089430.
STRINGi 10090.ENSMUSP00000098796.

PTM databases

PhosphoSitei Q64277.

Proteomic databases

MaxQBi Q64277.
PaxDbi Q64277.
PRIDEi Q64277.

Protocols and materials databases

DNASUi 12182.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000101237 ; ENSMUSP00000098796 ; ENSMUSG00000029082 .
GeneIDi 12182.
KEGGi mmu:12182.
UCSCi uc008xia.1. mouse.

Organism-specific databases

CTDi 683.
MGIi MGI:105370. Bst1.

Phylogenomic databases

eggNOGi NOG42584.
GeneTreei ENSGT00390000017291.
HOGENOMi HOG000293141.
HOVERGENi HBG097049.
InParanoidi Q64277.
KOi K18152.
OrthoDBi EOG7RBZ9B.
PhylomeDBi Q64277.
TreeFami TF332530.

Miscellaneous databases

NextBioi 280573.
PROi Q64277.
SOURCEi Search...

Gene expression databases

Bgeei Q64277.
CleanExi MM_BST1.
ExpressionAtlasi Q64277. baseline and differential.
Genevestigatori Q64277.

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. "The murine BP-3 gene encodes a relative of the CD38/NAD glycohydrolase family."
    Dong C., Wang J., Neame P., Cooper M.D.
    Int. Immunol. 6:1353-1360(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-44; 168-180 AND 261-274.
    Strain: BALB/c.
    Tissue: Lymphoma.
  2. "Molecular cloning of murine BST-1 having homology with CD38 and Aplysia ADP-ribosyl cyclase."
    Itoh M., Ishihara K., Tomizawa H., Tanaka H., Kobune Y., Ishikawa J., Kaisho T., Hirano T.
    Biochem. Biophys. Res. Commun. 203:1309-1317(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "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: Aorta.

Entry informationi

Entry nameiBST1_MOUSE
AccessioniPrimary (citable) accession number: Q64277
Secondary accession number(s): Q8BRY3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

External Data

Dasty 3