BQT4_SCHPO
ID BQT4_SCHPO Reviewed; 432 AA.
AC O60158; Q9USF5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Bouquet formation protein 4;
GN Name=bqt4; ORFNames=SPBC19C7.10;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 165-369, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
RP SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH RAP1.
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).
RN [4]
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).
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 -!- SUBUNIT: Interacts with rap1. {ECO:0000269|PubMed:19948484}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus
CC {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}. Nucleus
CC inner membrane {ECO:0000269|PubMed:19948484}; Peripheral membrane
CC protein {ECO:0000305}.
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DR EMBL; CU329671; CAB43057.1; -; Genomic_DNA.
DR EMBL; AB027792; BAA87096.1; -; Genomic_DNA.
DR PIR; T39816; T39816.
DR RefSeq; NP_596166.1; NM_001022086.2.
DR PDB; 5YBX; X-ray; 2.50 A; A=2-140.
DR PDB; 5YC2; X-ray; 2.70 A; A/C=9-140.
DR PDB; 5YCA; X-ray; 1.57 A; A=9-140.
DR PDB; 6A6W; X-ray; 2.60 A; A=2-140.
DR PDBsum; 5YBX; -.
DR PDBsum; 5YC2; -.
DR PDBsum; 5YCA; -.
DR PDBsum; 6A6W; -.
DR AlphaFoldDB; O60158; -.
DR SMR; O60158; -.
DR BioGRID; 277218; 40.
DR STRING; 4896.SPBC19C7.10.1; -.
DR iPTMnet; O60158; -.
DR SwissPalm; O60158; -.
DR MaxQB; O60158; -.
DR PaxDb; O60158; -.
DR PRIDE; O60158; -.
DR EnsemblFungi; SPBC19C7.10.1; SPBC19C7.10.1:pep; SPBC19C7.10.
DR GeneID; 2540694; -.
DR KEGG; spo:SPBC19C7.10; -.
DR PomBase; SPBC19C7.10; bqt4.
DR VEuPathDB; FungiDB:SPBC19C7.10; -.
DR eggNOG; ENOG502S0ET; Eukaryota.
DR HOGENOM; CLU_657479_0_0_1; -.
DR InParanoid; O60158; -.
DR OMA; PESYFLM; -.
DR PRO; PR:O60158; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005635; C:nuclear envelope; IDA:PomBase.
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:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0003677; F:DNA binding; IDA:PomBase.
DR GO; GO:0140473; F:telomere-nuclear envelope anchor activity; IMP:PomBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0070197; P:meiotic attachment of telomere to nuclear envelope; IEA:InterPro.
DR GO; GO:0045141; P:meiotic telomere clustering; IMP:PomBase.
DR GO; GO:0044820; P:mitotic telomere tethering at nuclear periphery; IMP:PomBase.
DR GO; GO:0000723; P:telomere maintenance; EXP:PomBase.
DR GO; GO:0032200; P:telomere organization; IMP:PomBase.
DR Gene3D; 3.10.260.10; -; 1.
DR InterPro; IPR037548; Bqt4.
DR InterPro; IPR036887; HTH_APSES_sf.
DR InterPro; IPR018004; KilA_N/APSES_HTH.
DR InterPro; IPR003163; Tscrpt_reg_HTH_APSES-type.
DR PANTHER; PTHR38044; PTHR38044; 1.
DR SMART; SM01252; KilA-N; 1.
DR SUPFAM; SSF54616; SSF54616; 1.
DR PROSITE; PS51299; HTH_APSES; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Chromosome partition; Cytoplasm;
KW DNA-binding; Meiosis; Membrane; Nucleus; Reference proteome.
FT CHAIN 1..432
FT /note="Bouquet formation protein 4"
FT /id="PRO_0000317335"
FT DOMAIN 38..147
FT /note="HTH APSES-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00630"
FT DNA_BIND 73..94
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00630"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:5YCA"
FT HELIX 26..31
FT /evidence="ECO:0007829|PDB:5YCA"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:5YCA"
FT STRAND 42..52
FT /evidence="ECO:0007829|PDB:5YCA"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:5YCA"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:5YCA"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:5YCA"
FT HELIX 73..80
FT /evidence="ECO:0007829|PDB:5YCA"
FT HELIX 86..99
FT /evidence="ECO:0007829|PDB:5YCA"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:5YC2"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:5YCA"
FT HELIX 115..124
FT /evidence="ECO:0007829|PDB:5YCA"
FT HELIX 128..136
FT /evidence="ECO:0007829|PDB:5YCA"
SQ SEQUENCE 432 AA; 47827 MW; 415DBE3BF9B43699 CRC64;
MTENEKSRSL PAERNPLYKD DTLDHTPLIP KCRAQVIEFP DGPATFVRLK CTNPESKVPH
FLMRMAKDSS ISATSMFRSA FPKATQEEED LEMRWIRDNL NPIEDKRVAG LWVPPADALA
LAKDYSMTPF INALLEASST PSTYATPSRP TAQKSETSEG EPESSTSATT TSVARRTRQR
LAEHLENSKK TILQHDNKEE DKEIHSEENE TKDEIKSEKK EPEIKKQEGG SSTEKVGQPS
SSDDKAKGST SKDQPSEEEE KTSDIQDRKI KTPIKPSLLG KIRSSVNKGM TDVASQVNRG
MTDVASQVNK GVNGVASQVN KGMNGVANQV NKGVTGVASQ VRKPVGKLEK KFENLEKSIG
DTLKSSIRSS PKSKKRSRED FEENEDYNAM VPVKRSRITK LESEVYYEKR KVRALGGIAI
GLGVGAILPF LF
