SEP1_SCHPO
ID SEP1_SCHPO Reviewed; 663 AA.
AC O43058; P79006;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Forkhead protein sep1;
GN Name=sep1; ORFNames=SPBC4C3.12;
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 [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RX PubMed=9427538; DOI=10.1016/s0378-1119(97)00390-9;
RA Ribar B., Banrevi A., Sipiczki M.;
RT "sep1+ encodes a transcription-factor homologue of the HNF-3/forkhead DNA-
RT binding-domain family in Schizosaccharomyces pombe.";
RL Gene 202:1-5(1997).
RN [2]
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 [3]
RP FUNCTION.
RX PubMed=15509866; DOI=10.1242/jcs.01473;
RA Buck V., Ng S.S., Ruiz-Garcia A.B., Papadopoulou K., Bhatti S.,
RA Samuel J.M., Anderson M., Millar J.B.A., McInerny C.J.;
RT "Fkh2p and Sep1p regulate mitotic gene transcription in fission yeast.";
RL J. Cell Sci. 117:5623-5632(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-446, 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).
CC -!- FUNCTION: Required for promoter sequence element PCB-driven, M-phase-
CC specific transcription. Acts as a transcriptional activator with a role
CC in the regulation of mitosis. Regulates septation and the periodic
CC transcription of cdc15. {ECO:0000269|PubMed:15509866}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089,
CC ECO:0000269|PubMed:9427538}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC49903.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U88191; AAC49903.1; ALT_FRAME; Genomic_DNA.
DR EMBL; CU329671; CAA16826.1; -; Genomic_DNA.
DR PIR; JC6500; JC6500.
DR PIR; T40493; T40493.
DR RefSeq; NP_596301.1; NM_001022222.2.
DR AlphaFoldDB; O43058; -.
DR SMR; O43058; -.
DR BioGRID; 277383; 114.
DR STRING; 4896.SPBC4C3.12.1; -.
DR iPTMnet; O43058; -.
DR MaxQB; O43058; -.
DR PaxDb; O43058; -.
DR PRIDE; O43058; -.
DR EnsemblFungi; SPBC4C3.12.1; SPBC4C3.12.1:pep; SPBC4C3.12.
DR GeneID; 2540866; -.
DR KEGG; spo:SPBC4C3.12; -.
DR PomBase; SPBC4C3.12; sep1.
DR VEuPathDB; FungiDB:SPBC4C3.12; -.
DR eggNOG; KOG2294; Eukaryota.
DR HOGENOM; CLU_408345_0_0_1; -.
DR InParanoid; O43058; -.
DR OMA; YIPSYTR; -.
DR Reactome; R-SPO-3232118; SUMOylation of transcription factors.
DR Reactome; R-SPO-9018519; Estrogen-dependent gene expression.
DR PRO; PR:O43058; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0097221; C:M/G1 phase-specific MADS box-forkhead transcription factor complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:PomBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:PomBase.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:PomBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:PomBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00059; FH; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR001766; Fork_head_dom.
DR InterPro; IPR030456; TF_fork_head_CS_2.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00250; Forkhead; 1.
DR PRINTS; PR00053; FORKHEAD.
DR SMART; SM00339; FH; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS00658; FORK_HEAD_2; 1.
DR PROSITE; PS50039; FORK_HEAD_3; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; DNA-binding; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Septation; Transcription; Transcription regulation.
FT CHAIN 1..663
FT /note="Forkhead protein sep1"
FT /id="PRO_0000091907"
FT DNA_BIND 128..222
FT /note="Fork-head"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT REGION 220..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 377..387
FT /note="PVSHLEKDVET -> TCITFGEGCCN (in Ref. 1; AAC49903)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 663 AA; 73032 MW; A66099437B7714C2 CRC64;
MNFNSTNPYY FTHEKNLNNA SKYSELPIAY QEIPLQSLPP YPKVASKLKG VVAGGKENNI
ASFQKPSSKA TRPYIPSYTR LTYSVPPLPI PPPSEQSLDT IIYRNPSVSS SQSQEPEEFF
LPLDDGKKPP YSYAMLIGMS IIRSPDRRLT LSAIYDWISN TFSFYNKSNN GWQNSIRHNL
SLNKAFMKIE RPRNLPGKGH FWSIRPGHEE QFLKLKLRKP GVNSRPAPPV QDVTSSTKYG
SSTGSSGFNT FNTSPHIFNQ RHQYLQNYYT ASLTNIPTIS NVNATNFHPL HSQQPYVDTP
GIDAPSDLEA KFSDLGVSSV VSVTSPLQSC TNSPSPPLSS PASSASPSES LRNESLGIKS
AKSLGLNKDD APVEGPPVSH LEKDVETPSV HDSVLGFNDT VTNLGKKGLK DGTTNTLQIP
AVRLPSLPSS PTIKNPSGLL LKRSNSIDFP TPPKALCPKL FCFRDDIVAD DYTKFSLLSP
IRSDMSGISA SPNTNLKEHR TRILQMLATP DAKQLSSLTS SDAEFWSVTP LKSSILRNGD
ASKQVTLSES PKGDSLLDGG SLSYFTNNIS SVAGLETPSK LPMSKSFDTF EDDFLDPMDM
LSFENHFSDF NSNRKVSPVK REVRRKYISS ATTIHSSAAQ DDTYLPSPTK RKMPLLRQTS
TLF
