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SRE2_SCHPO
ID   SRE2_SCHPO              Reviewed;         793 AA.
AC   O43019;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Putative transcription factor sre2;
DE   AltName: Full=Sterol regulatory element-binding protein 2;
GN   Name=sre2; ORFNames=SPBC354.05c;
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   PREDICTED FUNCTION.
RX   PubMed=11790253; DOI=10.1186/gb-2001-2-12-research0050;
RA   Zupicich J., Brenner S.E., Skarnes W.C.;
RT   "Computational prediction of membrane-tethered transcription factors.";
RL   Genome Biol. 2:RESEARCH0050.1-RESEARCH0050.6(2001).
RN   [3]
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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344; SER-345; SER-355 AND
RP   TYR-356, AND IDENTIFICATION BY 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: Putative transcription factor.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000305|PubMed:16823372}. Membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000305}. Note=May be released from membranes by
CC       a process known as regulated intramembrane proteolysis (RIP).
CC   -!- PTM: May undergo proteolytic cleavage to release the soluble
CC       transcription factor from the membrane.
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DR   EMBL; CU329671; CAA17805.1; -; Genomic_DNA.
DR   PIR; T40285; T40285.
DR   RefSeq; NP_595229.1; NM_001021135.2.
DR   AlphaFoldDB; O43019; -.
DR   SMR; O43019; -.
DR   BioGRID; 277559; 210.
DR   STRING; 4896.SPBC354.05c.1; -.
DR   iPTMnet; O43019; -.
DR   MaxQB; O43019; -.
DR   PaxDb; O43019; -.
DR   PRIDE; O43019; -.
DR   EnsemblFungi; SPBC354.05c.1; SPBC354.05c.1:pep; SPBC354.05c.
DR   GeneID; 2541044; -.
DR   KEGG; spo:SPBC354.05c; -.
DR   PomBase; SPBC354.05c; sre2.
DR   VEuPathDB; FungiDB:SPBC354.05c; -.
DR   eggNOG; KOG2588; Eukaryota.
DR   HOGENOM; CLU_354177_0_0_1; -.
DR   InParanoid; O43019; -.
DR   PRO; PR:O43019; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0000785; C:chromatin; IDA:PomBase.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0016021; C:integral component of membrane; ISM:PomBase.
DR   GO; GO:0005634; C:nucleus; IC:PomBase.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISM:PomBase.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISM:PomBase.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; NAS:PomBase.
DR   Gene3D; 4.10.280.10; -; 1.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   Pfam; PF00010; HLH; 1.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; SSF47459; 1.
DR   PROSITE; PS50888; BHLH; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Membrane; Nucleus; Phosphoprotein; Reference proteome;
KW   Transcription; Transcription regulation; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..793
FT                   /note="Putative transcription factor sre2"
FT                   /id="PRO_0000356242"
FT   TRANSMEM        719..739
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        748..768
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          426..495
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          323..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          367..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         344
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         345
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         355
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         356
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   793 AA;  86834 MW;  B9A4E0BBFA79C3A5 CRC64;
     MCPSQHSSLK DIHRQLENTA ISNPTENADP SSYVDGSNIM DFKHPSIVSS SASSSYPISH
     VPSVGTRGIP RSYSMASAYP YQVNSNSMDA STAFNLNQDV ADKPMLARNS IDSSINTELG
     PLESNHWFTQ AQDHSRQYSS SWDPSIDPFE VKNSLHDSTD LSITHHPHLP INHQGNTWKH
     ANESLQSNQG PVPNTKFVGL ETTQTDSYQQ SSVNSVVKIE EADATYALRE ESGQFNTFTG
     AENPSISPHS LNPNFPQYTE KPALTLLQSP KQNSNYDTSN FQNSVSDSSM QFTNEGMPSP
     VKGIMSSDDA VAFNFSQYST VYPQNAPENG NEFETPNKLK RTVSSPCASI SSKRSYGDIA
     QDCSYISSKT NGGGPSDSPS SSSTSVRGSV NDSNSPISSS ATFAIQSNGV EPVGLSTQEQ
     NLSPLSKRSA HNMIEKRYRS NLNDKIAELR DAVPTLRSGY NSTTADELKG TYVPLSRKLN
     KATILSKATE YIKSLQSKNK KLIEENKILQ KRLSEYTSVI QASLTAPSQP ASLSLLGPPG
     NTPGHRNVPP ILKRSSIGTP SQQAYFPDAP HNCHSVPQNS SYPRPPMQVN RSPIDSMQTI
     PHANFNEMHN AYSSRYPLKY SKSCNAVSHT SMMHPQEYGG SLPSSTVPSD YNQPQLVSPR
     AQADQQGLSY KNVGRAVLNG LVGLETVHML TNPDDAGSSN RFSMSVLPIS PSLHSILRFL
     LLLLAFLCFA MHILLTPEAT LRKWASSIYL SFRLECVFIS FLIFSVPIYD WGNYLNLRGK
     LLSELNLESG VAT
 
 
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