BQT3_SCHPO
ID BQT3_SCHPO Reviewed; 255 AA.
AC O74510;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Bouquet formation protein 3;
GN Name=bqt3; ORFNames=SPCC594.07c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=19948484; DOI=10.1083/jcb.200902122;
RA Chikashige Y., Yamane M., Okamasa K., Tsutsumi C., Kojidani T., Sato M.,
RA Haraguchi T., Hiraoka Y.;
RT "Membrane proteins Bqt3 and -4 anchor telomeres to the nuclear envelope to
RT ensure chromosomal bouquet formation.";
RL J. Cell Biol. 187:413-427(2009).
CC -!- FUNCTION: Connects telomeres to the nuclear envelop (NE) during both
CC vegetative growth and meiosis. This connection ensures clustering of
CC telomeres to the spindle pole body (SPB) when cells enter meiotic
CC prophase. {ECO:0000269|PubMed:19948484}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:19948484}; Multi-pass
CC membrane protein {ECO:0000255}. Nucleus inner membrane
CC {ECO:0000269|PubMed:19948484}; Multi-pass membrane protein
CC {ECO:0000255}.
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DR EMBL; CU329672; CAA20666.1; -; Genomic_DNA.
DR PIR; T41451; T41451.
DR RefSeq; NP_587793.1; NM_001022786.2.
DR AlphaFoldDB; O74510; -.
DR BioGRID; 276141; 30.
DR STRING; 4896.SPCC594.07c.1; -.
DR PaxDb; O74510; -.
DR EnsemblFungi; SPCC594.07c.1; SPCC594.07c.1:pep; SPCC594.07c.
DR GeneID; 2539582; -.
DR KEGG; spo:SPCC594.07c; -.
DR PomBase; SPCC594.07c; bqt3.
DR VEuPathDB; FungiDB:SPCC594.07c; -.
DR HOGENOM; CLU_1046471_0_0_1; -.
DR OMA; FSIWNCA; -.
DR PRO; PR:O74510; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005637; C:nuclear inner membrane; IDA:PomBase.
DR GO; GO:1990862; C:nuclear membrane complex Bqt3-Bqt4; IPI:PomBase.
DR GO; GO:0140473; F:telomere-nuclear envelope anchor activity; IPI:PomBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0045141; P:meiotic telomere clustering; IMP:PomBase.
DR GO; GO:0032200; P:telomere organization; IMP:PomBase.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Chromosome partition; Endoplasmic reticulum;
KW Meiosis; Membrane; Nucleus; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..255
FT /note="Bouquet formation protein 3"
FT /id="PRO_0000304117"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 255 AA; 28899 MW; 8ACFD401E558B9AE CRC64;
MSGSKCCSSS NTIKVSIYLF LHTLTYGLLN YHLNPRLLAS TGVVESDIPY WMSYLSIIMH
VGQSLLLQKF NLGYGWLLLT KYPVYVLLST YYLTPLSQIA WAFIIDAISL LVARCFSRAN
PIKCSNQVNT QYSVSFLFTI MASVLISVLN YISQKIFLNG LILGNSHNVV TSLVAPPLPL
QYLAHVPIGY VIQRVVFSER PIPQSLFLMI FLTLWNCFIP YSILFSMNWS AMFQVVGAYL
SQIWIITFIC WALSL
