BST1_RAT
ID BST1_RAT Reviewed; 319 AA.
AC Q63072;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 136.
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=Bone marrow stromal antigen 1;
DE Short=BST-1;
DE AltName: Full=Cyclic ADP-ribose hydrolase 2;
DE Short=cADPr hydrolase 2;
DE AltName: CD_antigen=CD157;
DE Flags: Precursor;
GN Name=Bst1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Pancreatic islet;
RX PubMed=8522202; DOI=10.1016/0378-1119(95)00540-m;
RA Furuya Y., Takasawa S., Yonekura H., Tanaka T., Takahara J., Okamoto H.;
RT "Cloning of a cDNA encoding rat bone marrow stromal cell antigen 1 (BST-1)
RT from the islets of Langerhans.";
RL Gene 165:329-330(1995).
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: Pancreatic islets, kidney, spleen, heart, thymus,
CC intestine and salivary gland.
CC -!- SIMILARITY: Belongs to the ADP-ribosyl cyclase family. {ECO:0000305}.
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DR EMBL; D49955; BAA08710.1; -; mRNA.
DR PIR; JC4390; JC4390.
DR RefSeq; NP_110475.1; NM_030848.1.
DR AlphaFoldDB; Q63072; -.
DR SMR; Q63072; -.
DR STRING; 10116.ENSRNOP00000004094; -.
DR GlyGen; Q63072; 4 sites.
DR PaxDb; Q63072; -.
DR PRIDE; Q63072; -.
DR Ensembl; ENSRNOT00000004094; ENSRNOP00000004094; ENSRNOG00000003064.
DR GeneID; 81506; -.
DR KEGG; rno:81506; -.
DR CTD; 683; -.
DR RGD; 620344; Bst1.
DR eggNOG; ENOG502S1HV; Eukaryota.
DR GeneTree; ENSGT00390000017291; -.
DR InParanoid; Q63072; -.
DR OrthoDB; 1460460at2759; -.
DR PhylomeDB; Q63072; -.
DR Reactome; R-RNO-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR Reactome; R-RNO-196807; Nicotinate metabolism.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:Q63072; -.
DR Proteomes; UP000002494; Chromosome 14.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019898; C:extrinsic component of membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0001931; C:uropod; ISO:RGD.
DR GO; GO:0061811; F:ADP-ribosyl cyclase activity; ISO:RGD.
DR GO; GO:0061812; F:cyclic ADP-ribose hydrolase; ISO:RGD.
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:RGD.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISO:RGD.
DR GO; GO:0050848; P:regulation of calcium-mediated signaling; ISO:RGD.
DR GO; GO:0001952; P:regulation of cell-matrix adhesion; ISO:RGD.
DR GO; GO:0050727; P:regulation of inflammatory response; ISO:RGD.
DR GO; GO:0090022; P:regulation of neutrophil chemotaxis; ISO:RGD.
DR GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
DR CDD; cd04759; Rib_hydrolase; 1.
DR InterPro; IPR003193; ADP-ribosyl_cyclase.
DR PANTHER; PTHR10912; PTHR10912; 1.
DR Pfam; PF02267; Rib_hydrolayse; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Hydrolase;
KW Lipoprotein; Membrane; NAD; NADP; Reference proteome; Signal; Transferase.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..294
FT /note="ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2"
FT /id="PRO_0000004036"
FT PROPEP 295..319
FT /evidence="ECO:0000255"
FT /id="PRO_0000004037"
FT LIPID 294
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 52..68
FT /evidence="ECO:0000250"
FT DISULFID 84..164
FT /evidence="ECO:0000250"
FT DISULFID 145..158
FT /evidence="ECO:0000250"
FT DISULFID 239..260
FT /evidence="ECO:0000250"
FT DISULFID 272..281
FT /evidence="ECO:0000250"
SQ SEQUENCE 319 AA; 35131 MW; 46831685DE2B2472 CRC64;
MAVQACALSL RLGLWMSLLL PVLPGAGARA AGARWSGEGT TPHLQSIFLG RCAEYTTLLS
LEPGNKNCTA IWEAFKVVLD KDPCSVLPSD YDLFINLSRH AIPRDKSLFW ENNHLLVMSY
AENTRRLMPL CDVLYGKVGD FLSWCRQENA SGLDYQSCPT AEDCENNAVD AYWKSASMQY
SRDSSGVINV MLNGSEPKGA YPTKGFFADF EIPYLQKDKI TRIEIWVMHE VGGPHVESCG
EGSVKILEDR LEALGFQHSC INDYPPVKFL MCVDHSTHPD CAMNSASASM WRESPALHAI
GDISLIISLL VALASSSQA
