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Database: UniProt
Entry: F6ZFG5_MONDO
LinkDB: F6ZFG5_MONDO
Original site: F6ZFG5_MONDO 
ID   F6ZFG5_MONDO            Unreviewed;       349 AA.
AC   F6ZFG5;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 3.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase {ECO:0000256|ARBA:ARBA00011982};
DE            EC=3.2.2.6 {ECO:0000256|ARBA:ARBA00011982};
GN   Name=BST1 {ECO:0000313|Ensembl:ENSMODP00000001210.4};
OS   Monodelphis domestica (Gray short-tailed opossum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX   NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000001210.4, ECO:0000313|Proteomes:UP000002280};
RN   [1] {ECO:0000313|Ensembl:ENSMODP00000001210.4, ECO:0000313|Proteomes:UP000002280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17495919; DOI=10.1038/nature05805;
RA   Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L., Duke S.,
RA   Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J., Kamal M.,
RA   Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A., Benos P.V.,
RA   Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L., Deakin J.E.,
RA   Fazzari M.J., Glass J.L., Grabherr M., Greally J.M., Gu W., Hore T.A.,
RA   Huttley G.A., Kleber M., Jirtle R.L., Koina E., Lee J.T., Mahony S.,
RA   Marra M.A., Miller R.D., Nicholls R.D., Oda M., Papenfuss A.T., Parra Z.E.,
RA   Pollock D.D., Ray D.A., Schein J.E., Speed T.P., Thompson K.,
RA   VandeBerg J.L., Wade C.M., Walker J.A., Waters P.D., Webber C.,
RA   Weidman J.R., Xie X., Zody M.C., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Bloom T., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M.,
RA   Samollow P.B., Lander E.S., Lindblad-Toh K.;
RT   "Genome of the marsupial Monodelphis domestica reveals innovation in non-
RT   coding sequences.";
RL   Nature 447:167-177(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMODP00000001210.4}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the ADP-ribosyl cyclase family.
CC       {ECO:0000256|ARBA:ARBA00005406}.
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DR   RefSeq; XP_001369737.2; XM_001369700.3.
DR   AlphaFoldDB; F6ZFG5; -.
DR   STRING; 13616.ENSMODP00000001210; -.
DR   Ensembl; ENSMODT00000001235.4; ENSMODP00000001210.4; ENSMODG00000001017.4.
DR   GeneID; 100015733; -.
DR   KEGG; mdo:100015733; -.
DR   CTD; 683; -.
DR   eggNOG; ENOG502S1HV; Eukaryota.
DR   GeneTree; ENSGT00390000017291; -.
DR   HOGENOM; CLU_067834_1_0_1; -.
DR   InParanoid; F6ZFG5; -.
DR   OMA; RCYEYIR; -.
DR   OrthoDB; 4265952at2759; -.
DR   TreeFam; TF332530; -.
DR   Proteomes; UP000002280; Chromosome 5.
DR   Bgee; ENSMODG00000001017; Expressed in lung and 15 other cell types or tissues.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0001931; C:uropod; IEA:Ensembl.
DR   GO; GO:0061811; F:ADP-ribosyl cyclase activity; IEA:Ensembl.
DR   GO; GO:0061812; F:cyclic ADP-ribose hydrolase; IEA:Ensembl.
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:0032956; P:regulation of actin cytoskeleton organization; IEA:Ensembl.
DR   GO; GO:0050848; P:regulation of calcium-mediated signaling; IEA:Ensembl.
DR   GO; GO:0001952; P:regulation of cell-matrix adhesion; IEA:Ensembl.
DR   GO; GO:0050727; P:regulation of inflammatory response; IEA:Ensembl.
DR   GO; GO:0090022; P:regulation of neutrophil chemotaxis; IEA:Ensembl.
DR   GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
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   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002280};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        34..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        319..340
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   349 AA;  39882 MW;  82158AA01E1A918B CRC64;
     MQELQFLGAT GCKPHCREEI LRARNSSMEP SKLVLLQLKL FLILLLGAAG VCMGAGEKLW
     KGLGTTPHLE SIFRGRCNEF ISLENPELGD KNCSEIWEAF KTVFHKDPCS VLPSDYDLFI
     NLSRHPIPRD KSLFWENNYD VVTAYAQNGR RLLPITNMLY GRIVDLLDWC RKENSSELDY
     QSCPTTEDCE NNAMDSFWKK ASSQYAYDSS GVIYVMLNGS EPSGAYPVKG FFADYEIPNF
     QKDKVTRFVI WVMHEIGQPH IESCGEGSMK ILENRLKEME FKYECINDYR PVKLLKCLDY
     STHPECVFTS AAESTQQRIP FLFGGGWGSS LAFLLFFFGI NFRNSILTF
//
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