BST1_MOUSE
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 25-MAY-2022, entry version 158.
DE RecName: Full=ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2;
DE EC=3.2.2.6;
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: Synthesizes the second messengers cyclic ADP-ribose and
CC nicotinate-adenine dinucleotide phosphate, the former a second
CC messenger that elicits calcium release from intracellular stores. May
CC be involved in pre-B-cell growth.
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
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 GlyGen; Q64277; 4 sites.
DR iPTMnet; Q64277; -.
DR PhosphoSitePlus; Q64277; -.
DR SwissPalm; Q64277; -.
DR EPD; Q64277; -.
DR jPOST; Q64277; -.
DR MaxQB; Q64277; -.
DR PaxDb; Q64277; -.
DR PeptideAtlas; Q64277; -.
DR PRIDE; Q64277; -.
DR ProteomicsDB; 273707; -.
DR DNASU; 12182; -.
DR GeneID; 12182; -.
DR KEGG; mmu:12182; -.
DR UCSC; uc008xia.1; mouse.
DR CTD; 683; -.
DR MGI; MGI:105370; Bst1.
DR eggNOG; ENOG502S1HV; Eukaryota.
DR InParanoid; Q64277; -.
DR OrthoDB; 1460460at2759; -.
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 73 CRISPR screens.
DR ChiTaRS; Bst1; mouse.
DR PRO; PR:Q64277; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q64277; protein.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019898; C:extrinsic component of membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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 InterPro; IPR003193; ADP-ribosyl_cyclase.
DR PANTHER; PTHR10912; PTHR10912; 1.
DR Pfam; PF02267; Rib_hydrolayse; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW GPI-anchor; Hydrolase; Lipoprotein; Membrane; NAD; NADP;
KW Reference proteome; 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 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"
FT DISULFID 76..156
FT /evidence="ECO:0000250"
FT DISULFID 137..150
FT /evidence="ECO:0000250"
FT DISULFID 231..252
FT /evidence="ECO:0000250"
FT DISULFID 264..273
FT /evidence="ECO:0000250"
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
