SUS1_PICGU
ID SUS1_PICGU Reviewed; 97 AA.
AC A5DG59;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Transcription and mRNA export factor SUS1 {ECO:0000255|HAMAP-Rule:MF_03046};
GN Name=SUS1 {ECO:0000255|HAMAP-Rule:MF_03046}; ORFNames=PGUG_02260;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; CH408156; EDK38162.2; -; Genomic_DNA.
DR RefSeq; XP_001486589.1; XM_001486539.1.
DR AlphaFoldDB; A5DG59; -.
DR SMR; A5DG59; -.
DR STRING; 4929.XP_001486589.1; -.
DR EnsemblFungi; EDK38162; EDK38162; PGUG_02260.
DR GeneID; 5128081; -.
DR KEGG; pgu:PGUG_02260; -.
DR VEuPathDB; FungiDB:PGUG_02260; -.
DR eggNOG; ENOG502S9WJ; Eukaryota.
DR HOGENOM; CLU_134052_2_1_1; -.
DR InParanoid; A5DG59; -.
DR OMA; YESGWFD; -.
DR OrthoDB; 1538551at2759; -.
DR Proteomes; UP000001997; Unassembled WGS sequence.
DR GO; GO:0071819; C:DUBm complex; IEA:UniProtKB-UniRule.
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; IEA:UniProtKB-UniRule.
DR GO; GO:0070390; C:transcription export complex 2; IEA:UniProtKB-UniRule.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016578; P:histone deubiquitination; IEA:UniProtKB-UniRule.
DR GO; GO:0006406; P:mRNA export from nucleus; IEA:UniProtKB-UniRule.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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..97
FT /note="Transcription and mRNA export factor SUS1"
FT /id="PRO_0000367571"
SQ SEQUENCE 97 AA; 11520 MW; 4FBD9BCE0B1B1D01 CRC64;
MSQDELDQIR AKIQDHLISS GNYELINKQL KLKLYENGWY DKVGQLATTE LQQEDNKNLT
FERLYAMVKP QAESMVPDEV RQEIMTRIRE YLEDVIQ
