BLT1_SCHPO
ID BLT1_SCHPO Reviewed; 700 AA.
AC O74338;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Mitosis inducer protein blt1;
GN Name=blt1; ORFNames=SPBC1A4.05;
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 INTERACTION WITH SAD1, AND SUBCELLULAR LOCATION.
RX PubMed=14655046; DOI=10.1007/s00438-003-0938-8;
RA Miki F., Kurabayashi A., Tange Y., Okazaki K., Shimanuki M., Niwa O.;
RT "Two-hybrid search for proteins that interact with Sad1 and Kms1, two
RT membrane-bound components of the spindle pole body in fission yeast.";
RL Mol. Genet. Genomics 270:449-461(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-636, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [4]
RP SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH CDR2 AND MID1.
RX PubMed=19474789; DOI=10.1038/nature08074;
RA Moseley J.B., Mayeux A., Paoletti A., Nurse P.;
RT "A spatial gradient coordinates cell size and mitotic entry in fission
RT yeast.";
RL Nature 459:857-860(2009).
CC -!- FUNCTION: At the onset of mitosis, forms a medial ring structure before
CC the arrangement of the medial actin ring. Essential for the central
CC positioning of the division septum before the cell divides.
CC {ECO:0000269|PubMed:19474789}.
CC -!- SUBUNIT: Interacts with cdr2, mid1 and sad1.
CC {ECO:0000269|PubMed:14655046, ECO:0000269|PubMed:19474789}.
CC -!- INTERACTION:
CC O74338; Q09822: cdc15; NbExp=2; IntAct=EBI-1542378, EBI-1148185;
CC -!- SUBCELLULAR LOCATION: Cell septum {ECO:0000269|PubMed:14655046,
CC ECO:0000269|PubMed:19474789}.
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DR EMBL; CU329671; CAA20109.1; -; Genomic_DNA.
DR PIR; T39853; T39853.
DR RefSeq; NP_595807.1; NM_001021710.2.
DR AlphaFoldDB; O74338; -.
DR SMR; O74338; -.
DR BioGRID; 276909; 51.
DR DIP; DIP-38843N; -.
DR IntAct; O74338; 6.
DR STRING; 4896.SPBC1A4.05.1; -.
DR iPTMnet; O74338; -.
DR MaxQB; O74338; -.
DR PaxDb; O74338; -.
DR PRIDE; O74338; -.
DR EnsemblFungi; SPBC1A4.05.1; SPBC1A4.05.1:pep; SPBC1A4.05.
DR PomBase; SPBC1A4.05; blt1.
DR VEuPathDB; FungiDB:SPBC1A4.05; -.
DR HOGENOM; CLU_393873_0_0_1; -.
DR OMA; FPSQEKW; -.
DR PRO; PR:O74338; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0030428; C:cell septum; IEA:UniProtKB-SubCell.
DR GO; GO:0071341; C:medial cortical node; IDA:PomBase.
DR GO; GO:0110085; C:mitotic actomyosin contractile ring; IDA:PomBase.
DR GO; GO:0120105; C:mitotic actomyosin contractile ring, intermediate layer; IDA:PomBase.
DR GO; GO:0106006; F:cytoskeletal protein-membrane anchor activity; IMP:PomBase.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IGI:PomBase.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Coiled coil; Mitosis; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..700
FT /note="Mitosis inducer protein blt1"
FT /id="PRO_0000116767"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 496..575
FT /evidence="ECO:0000255"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..700
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 636
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 700 AA; 78117 MW; 0A55373AFC35E77E CRC64;
MSKSAFTSKS QLKGIDGSFN DPFRQPSMNL PTPPHDDGLP SIPRSTALPN LSNRLSPYSH
RNYLPIPEAD SRNLEVLNSI SLTTGSVVNQ INKLYQRSCD NANYLQDLRS LILQTPTAEA
NATQVTESLN QIQKILQEAS SKDREQIVQV IKELNKGNSL EVRRELGNCL AHLKKGTLNI
DNALQASLQK YWKELQYFNV SKDKLLSLEE SIKLLSARLE ETDTPSSTHW IEINAGFKEV
GDELSENFQR KQEILSGLQN NVILRTNNRK PVGSDGSNSN FNGGEEQMDS KDQEEIQDYL
NSLLSVHEKD GVLLQKFHNS YVQYQKLAVA LSKYENFDAD KLFQQMNLAK QSNETLLQTL
TEQTDQLLSF KETMDSFKFI LGPSMENQAL QQGILAEQQD LVAQLRDIVL RSETLAENPS
NMPGSCLPGA SSNTADEFTE QLNLLKNEVA RLSAICPSPN SGINASVLTN ADNLEKENLL
LVNNNAFKVD DRSVSSVALD DHNRQLQMNV EELEGKKADL TSKINRLDKD FVKLNTTYSL
LTDQVKTKQL ALQEIESRVI RLEERLNMLQ KLSMQPAISS SSEFVPIESH PSSSAVVPIE
EPKNSIIEKK RVPHNAARNS VNLEVTLPNS KKRFSSFSGS SSKLPVRPST ALTDKRKPSW
SRRLAAAIGF SSGSPEKKHV ITSSDAGHQR SKSRSFSSKM
