ID   SHE2_ASHGO              Reviewed;         279 AA.
AC   Q758R0;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=SWI5-dependent HO expression protein 2;
GN   Name=SHE2; OrderedLocusNames=AEL307C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: RNA-binding protein that binds specific mRNAs including the
CC       ASH1 mRNA, coding for a repressor of the HO endonuclease. Part of the
CC       mRNA localization machinery that restricts accumulation of certain
CC       proteins to the bud and in the daughter cell (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer and homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P36068}. Nucleus
CC       {ECO:0000250|UniProtKB:P36068}. Note=Shuttles between the nucleus and
CC       cytoplasm and is exported in an mRNA-dependent manner. The presence in
CC       the nucleus is essential for PUF6 and LOC1 to bind the ASH1 mRNA.
CC       {ECO:0000250|UniProtKB:P36068}.
CC   -!- SIMILARITY: Belongs to the SHE2 family. {ECO:0000305}.
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DR   EMBL; AE016818; AAS52377.1; -; Genomic_DNA.
DR   RefSeq; NP_984553.1; NM_209906.1.
DR   AlphaFoldDB; Q758R0; -.
DR   SMR; Q758R0; -.
DR   STRING; 33169.AAS52377; -.
DR   EnsemblFungi; AAS52377; AAS52377; AGOS_AEL307C.
DR   GeneID; 4620728; -.
DR   KEGG; ago:AGOS_AEL307C; -.
DR   eggNOG; ENOG502RXWH; Eukaryota.
DR   HOGENOM; CLU_1129832_0_0_1; -.
DR   InParanoid; Q758R0; -.
DR   OMA; HFVKFTQ; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0005934; C:cellular bud tip; IEA:EnsemblFungi.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:EnsemblFungi.
DR   GO; GO:1990825; F:sequence-specific mRNA binding; IEA:EnsemblFungi.
DR   GO; GO:0008298; P:intracellular mRNA localization; IEA:EnsemblFungi.
DR   GO; GO:0007533; P:mating type switching; IEA:EnsemblFungi.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.200.20; -; 1.
DR   InterPro; IPR024261; RNA-bd_She2.
DR   InterPro; IPR036827; She2_dom_sf.
DR   Pfam; PF11435; She2p; 1.
DR   SUPFAM; SSF116942; SSF116942; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; mRNA transport; Nucleus; Reference proteome; RNA-binding;
KW   Transport.
FT   CHAIN           1..279
FT                   /note="SWI5-dependent HO expression protein 2"
FT                   /id="PRO_0000408916"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..31
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   279 AA;  33146 MW;  3499748652DF5649 CRC64;
     MPIPDMSSQY PHQQEDMSQE EEPRGRKPQS MVDQEKQDYL DFIVPRLQIT GKILQLTEEV
     IQEQANYISR YIDFLNKYIN YQRKVSTLRF ERATLIKYVK KLRFLNDFLY TYNADVNMIT
     EPLQKLVRPL GSFFIRYLEI IDLLNYYLTQ SLRNETISKT LNQDLVLSQE CIAMADKTYR
     VYVKFVQWFI ESSSSVTTGD LTMEIVQFTR KCAVEDGIDL GETDDVLLQE VQLVTSSEEF
     EDLLEKWQQV LHFQCADLDD TFNDNIRHWS ELFDKKKEK