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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
 
 
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