ID   SUS1_SCHPO              Reviewed;         108 AA.
AC   Q7LL15;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Transcription and mRNA export factor sus1 {ECO:0000255|HAMAP-Rule:MF_03046};
GN   Name=sus1; ORFNames=SPBC6B1.12c;
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).
CC   -!- FUNCTION: Involved in mRNA export coupled transcription activation by
CC       association with both the TREX-2 and the SAGA complexes. At the
CC       promoters, SAGA is required for recruitment of the basal transcription
CC       machinery. It influences RNA polymerase II transcriptional activity
CC       through different activities such as TBP interaction and promoter
CC       selectivity, interaction with transcription activators, and chromatin
CC       modification through histone acetylation and deubiquitination. Within
CC       the SAGA complex, participates in a subcomplex required for
CC       deubiquitination of H2B and for the maintenance of steady-state H3
CC       methylation levels. The TREX-2 complex functions in docking export-
CC       competent ribonucleoprotein particles (mRNPs) to the nuclear entrance
CC       of the nuclear pore complex (nuclear basket). TREX-2 participates in
CC       mRNA export and accurate chromatin positioning in the nucleus by
CC       tethering genes to the nuclear periphery. May also be involved in
CC       cytoplasmic mRNA decay by interaction with components of P-bodies (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the nuclear pore complex (NPC)-associated TREX-2
CC       complex (transcription and export complex 2), composed of at least
CC       sus1, sac3, thp1, sem1, and cdc31. TREX-2 contains 2 sus1 chains. The
CC       TREX-2 complex interacts with the nucleoporin nup1. Component of the
CC       1.8 MDa SAGA transcription coactivator-HAT complex. SAGA is built of 5
CC       distinct domains with specialized functions. Within the SAGA complex,
CC       sus1, sgf11, sgf73 and ubp8 form an additional subcomplex of SAGA
CC       called the DUB module (deubiquitination module). Interacts directly
CC       with thp1, sac3, sgf11, and with the RNA polymerase II.
CC       {ECO:0000255|HAMAP-Rule:MF_03046}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000255|HAMAP-
CC       Rule:MF_03046}. Cytoplasm, P-body {ECO:0000255|HAMAP-Rule:MF_03046}.
CC   -!- SIMILARITY: Belongs to the ENY2 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03046}.
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DR   EMBL; CU329671; CAF28466.1; -; Genomic_DNA.
DR   RefSeq; NP_001018822.1; NM_001022002.2.
DR   AlphaFoldDB; Q7LL15; -.
DR   SMR; Q7LL15; -.
DR   BioGRID; 280381; 8.
DR   IntAct; Q7LL15; 2.
DR   MINT; Q7LL15; -.
DR   STRING; 4896.SPBC6B1.12c.1; -.
DR   iPTMnet; Q7LL15; -.
DR   MaxQB; Q7LL15; -.
DR   PaxDb; Q7LL15; -.
DR   PRIDE; Q7LL15; -.
DR   EnsemblFungi; SPBC6B1.12c.1; SPBC6B1.12c.1:pep; SPBC6B1.12c.
DR   GeneID; 3361305; -.
DR   KEGG; spo:SPBC6B1.12c; -.
DR   PomBase; SPBC6B1.12c; sus1.
DR   VEuPathDB; FungiDB:SPBC6B1.12c; -.
DR   HOGENOM; CLU_134052_2_0_1; -.
DR   InParanoid; Q7LL15; -.
DR   OMA; YTRGIAR; -.
DR   PhylomeDB; Q7LL15; -.
DR   PRO; PR:Q7LL15; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0071819; C:DUBm complex; IBA:GO_Central.
DR   GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-UniRule.
DR   GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR   GO; GO:0000124; C:SAGA complex; IDA:PomBase.
DR   GO; GO:0070390; C:transcription export complex 2; ISO:PomBase.
DR   GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR   GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0016578; P:histone deubiquitination; IBA:GO_Central.
DR   GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IBA:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:PomBase.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; EXP:PomBase.
DR   GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.246.140; -; 1.
DR   HAMAP; MF_03046; ENY2_Sus1; 1.
DR   InterPro; IPR018783; TF_ENY2.
DR   InterPro; IPR038212; TF_EnY2_sf.
DR   PANTHER; PTHR12514; PTHR12514; 1.
DR   Pfam; PF10163; EnY2; 1.
PE   3: Inferred from homology;
KW   Activator; Chromatin regulator; Cytoplasm; mRNA transport; Nucleus;
KW   Protein transport; Reference proteome; Transcription;
KW   Transcription regulation; Translocation; Transport.
FT   CHAIN           1..108
FT                   /note="Transcription and mRNA export factor sus1"
FT                   /id="PRO_0000350748"
SQ   SEQUENCE   108 AA;  12313 MW;  91F54D90F0469567 CRC64;
     MYDLIFSTKM TTEKIVEQLY ETGDYERLAN ELEYKLESCG WTTQLRDYTR GIVNSDSKID
     FQKLYESALQ SATESIPDSV KMDLLKDIKT CVLKLANPPE SANGGNKM