ID   BST1_MOUSE              Reviewed;         311 AA.
AC   Q64277; Q8BRY3;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 166.
DE   RecName: Full=ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2;
DE            EC=3.2.2.6 {ECO:0000250|UniProtKB:Q10588};
DE   AltName: Full=ADP-ribosyl cyclase 2;
DE   AltName: Full=Antigen BP3;
DE   AltName: Full=BP-3 alloantigen;
DE   AltName: Full=Bone marrow stromal antigen 1;
DE            Short=BST-1;
DE   AltName: Full=Cyclic ADP-ribose hydrolase 2;
DE            Short=cADPR hydrolase 2;
DE   AltName: Full=Leukocyte antigen 65;
DE            Short=Ly-65;
DE   AltName: CD_antigen=CD157;
DE   Flags: Precursor;
GN   Name=Bst1; Synonyms=Bp-3, Bp3, Ly65;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 25-44; 168-180 AND
RP   261-274.
RC   STRAIN=BALB/cJ; TISSUE=Lymphoma;
RX   PubMed=7819143; DOI=10.1093/intimm/6.9.1353;
RA   Dong C., Wang J., Neame P., Cooper M.D.;
RT   "The murine BP-3 gene encodes a relative of the CD38/NAD glycohydrolase
RT   family.";
RL   Int. Immunol. 6:1353-1360(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7916574; DOI=10.1006/bbrc.1994.2325;
RA   Itoh M., Ishihara K., Tomizawa H., Tanaka H., Kobune Y., Ishikawa J.,
RA   Kaisho T., Hirano T.;
RT   "Molecular cloning of murine BST-1 having homology with CD38 and Aplysia
RT   ADP-ribosyl cyclase.";
RL   Biochem. Biophys. Res. Commun. 203:1309-1317(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Aorta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Catalyzes both the synthesis of cyclic ADP-beta-D-ribose
CC       (cADPR) from NAD(+), and its hydrolysis to ADP-D-ribose (ADPR). Cyclic
CC       ADPR is known to serve as an endogenous second messenger that elicits
CC       calcium release from intracellular stores, and thus regulates the
CC       mobilization of intracellular calcium. May be involved in pre-B-cell
CC       growth. {ECO:0000250|UniProtKB:Q10588}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide;
CC         Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6;
CC         Evidence={ECO:0000250|UniProtKB:Q10588};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302;
CC         Evidence={ECO:0000250|UniProtKB:Q10588};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) = cyclic ADP-beta-D-ribose + H(+) + nicotinamide;
CC         Xref=Rhea:RHEA:38611, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:73672;
CC         Evidence={ECO:0000250|UniProtKB:Q10588};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38612;
CC         Evidence={ECO:0000250|UniProtKB:Q10588};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cyclic ADP-beta-D-ribose + H2O = ADP-D-ribose;
CC         Xref=Rhea:RHEA:38615, ChEBI:CHEBI:15377, ChEBI:CHEBI:57967,
CC         ChEBI:CHEBI:73672; Evidence={ECO:0000250|UniProtKB:Q10588};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38616;
CC         Evidence={ECO:0000250|UniProtKB:Q10588};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q10588}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q10588};
CC       Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q10588}.
CC   -!- TISSUE SPECIFICITY: Expressed in the bone marrow, spleen and thymus in
CC       lymphoid organs, and the lung, kidney and heart in non-lymphoid organs.
CC   -!- SIMILARITY: Belongs to the ADP-ribosyl cyclase family. {ECO:0000305}.
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DR   EMBL; L32812; AAA67046.1; -; mRNA.
DR   EMBL; D31788; BAA06597.1; -; mRNA.
DR   EMBL; AK041059; BAC30804.1; -; mRNA.
DR   CCDS; CCDS19264.1; -.
DR   PIR; JC2541; JC2541.
DR   RefSeq; NP_033893.2; NM_009763.3.
DR   AlphaFoldDB; Q64277; -.
DR   SMR; Q64277; -.
DR   STRING; 10090.ENSMUSP00000098796; -.
DR   GlyCosmos; Q64277; 4 sites, No reported glycans.
DR   GlyGen; Q64277; 4 sites.
DR   iPTMnet; Q64277; -.
DR   PhosphoSitePlus; Q64277; -.
DR   SwissPalm; Q64277; -.
DR   EPD; Q64277; -.
DR   jPOST; Q64277; -.
DR   MaxQB; Q64277; -.
DR   PaxDb; 10090-ENSMUSP00000098796; -.
DR   PeptideAtlas; Q64277; -.
DR   ProteomicsDB; 273707; -.
DR   DNASU; 12182; -.
DR   GeneID; 12182; -.
DR   KEGG; mmu:12182; -.
DR   UCSC; uc008xia.1; mouse.
DR   AGR; MGI:105370; -.
DR   CTD; 683; -.
DR   MGI; MGI:105370; Bst1.
DR   eggNOG; ENOG502S1HV; Eukaryota.
DR   InParanoid; Q64277; -.
DR   OrthoDB; 4265952at2759; -.
DR   PhylomeDB; Q64277; -.
DR   TreeFam; TF332530; -.
DR   Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR   Reactome; R-MMU-196807; Nicotinate metabolism.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   BioGRID-ORCS; 12182; 5 hits in 78 CRISPR screens.
DR   ChiTaRS; Bst1; mouse.
DR   PRO; PR:Q64277; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q64277; Protein.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0001931; C:uropod; ISO:MGI.
DR   GO; GO:0061811; F:ADP-ribosyl cyclase activity; ISO:MGI.
DR   GO; GO:0061812; F:cyclic ADP-ribose hydrolase; ISO:MGI.
DR   GO; GO:0050135; F:NAD(P)+ nucleosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003953; F:NAD+ nucleosidase activity; IBA:GO_Central.
DR   GO; GO:0061809; F:NAD+ nucleotidase, cyclic ADP-ribose generating; IEA:UniProtKB-EC.
DR   GO; GO:0016849; F:phosphorus-oxygen lyase activity; IBA:GO_Central.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030890; P:positive regulation of B cell proliferation; IBA:GO_Central.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISO:MGI.
DR   GO; GO:0050848; P:regulation of calcium-mediated signaling; ISO:MGI.
DR   GO; GO:0001952; P:regulation of cell-matrix adhesion; ISO:MGI.
DR   GO; GO:0050727; P:regulation of inflammatory response; ISO:MGI.
DR   GO; GO:0090022; P:regulation of neutrophil chemotaxis; ISO:MGI.
DR   GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
DR   CDD; cd04759; Rib_hydrolase; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR003193; ADP-ribosyl_cyclase.
DR   PANTHER; PTHR10912; ADP-RIBOSYL CYCLASE; 1.
DR   PANTHER; PTHR10912:SF4; ADP-RIBOSYL CYCLASE_CYCLIC ADP-RIBOSE HYDROLASE 2; 1.
DR   Pfam; PF02267; Rib_hydrolayse; 1.
DR   SUPFAM; SSF52309; N-(deoxy)ribosyltransferase-like; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   GPI-anchor; Hydrolase; Lipoprotein; Membrane; NAD; Reference proteome;
KW   Signal; Transferase.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:7819143"
FT   CHAIN           25..286
FT                   /note="ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2"
FT                   /id="PRO_0000004034"
FT   PROPEP          287..311
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000004035"
FT   BINDING         102
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q10588"
FT   BINDING         102
FT                   /ligand="nicotinamide"
FT                   /ligand_id="ChEBI:CHEBI:17154"
FT                   /evidence="ECO:0000250|UniProtKB:Q10588"
FT   BINDING         165
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q10588"
FT   BINDING         203
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q10588"
FT   LIPID           286
FT                   /note="GPI-anchor amidated serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        59
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        88
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        141
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        185
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        46..60
FT                   /evidence="ECO:0000250|UniProtKB:Q10588"
FT   DISULFID        76..156
FT                   /evidence="ECO:0000250|UniProtKB:Q10588"
FT   DISULFID        137..150
FT                   /evidence="ECO:0000250|UniProtKB:Q10588"
FT   DISULFID        231..252
FT                   /evidence="ECO:0000250|UniProtKB:Q10588"
FT   DISULFID        264..273
FT                   /evidence="ECO:0000250|UniProtKB:Q10588"
FT   CONFLICT        30
FT                   /note="R -> T (in Ref. 3; BAC30804)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   311 AA;  34616 MW;  5663D3427E460AD7 CRC64;
     MAVQGGLLSL WLWLWLSLLT VLLGARARWR GEGTTPHLQS IFLGRCAEYT TLLSLGNKNC
     TAIWEAFKGV LDKDPCSVLP SDYDLFINLS RHPIPRDKSL FWENNHLLVM SYGENTRRLV
     ALCDVLYGKV GDFLSWCRQE NASGLDYQSC PTSEDCENNA VDSYWKSASM QYSRDSSGVI
     NVMLNGSEPK GAYPTRGFFA DFEIPYLQKD KVTRIEIWVM HDVGGPNVES CGEGSVKILE
     DRLEALGFQH SCINDYRPVK FLMCVDHSTH PDCIMNSASA SMRRESASLH AIGDASLLIS
     LLVALASSSQ A
//