ID   SHE3_YEAS6              Reviewed;         425 AA.
AC   B5VE90;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=SWI5-dependent HO expression protein 3;
GN   Name=SHE3; ORFNames=AWRI1631_22130;
OS   Saccharomyces cerevisiae (strain AWRI1631) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=545124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AWRI1631;
RX   PubMed=18778279; DOI=10.1111/j.1567-1364.2008.00434.x;
RA   Borneman A.R., Forgan A.H., Pretorius I.S., Chambers P.J.;
RT   "Comparative genome analysis of a Saccharomyces cerevisiae wine strain.";
RL   FEMS Yeast Res. 8:1185-1195(2008).
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. Required for the delivery
CC       of cortical endoplasmic reticulum into the emerging bud (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SHE3 family. {ECO:0000305}.
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DR   EMBL; ABSV01000129; EDZ73757.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5VE90; -.
DR   SMR; B5VE90; -.
DR   Proteomes; UP000008988; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0048309; P:endoplasmic reticulum inheritance; IEA:InterPro.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   InterPro; IPR031398; She3.
DR   Pfam; PF17078; SHE3; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Endoplasmic reticulum; Membrane; mRNA transport;
KW   Phosphoprotein; RNA-binding; Transport.
FT   CHAIN           1..425
FT                   /note="SWI5-dependent HO expression protein 3"
FT                   /id="PRO_0000408939"
FT   REGION          24..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          322..425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          68..197
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        323..359
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..407
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         343
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38272"
FT   MOD_RES         394
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38272"
SQ   SEQUENCE   425 AA;  47530 MW;  5FA9A7C0C071BA3E CRC64;
     MSDQDNTQTS SSKLAPHHNI FMANLESSPT KDRNTSSQNA SSSRVIESLH DQIDMLTKTN
     LQLTTQSQNL LSKLELAQSK ESKLLENLNL LKNENENLNS IFERKNKKLK ELEKDYSELS
     NRYNEQKEKM DQLSKLAKKS SAIEQSCSEK LQNMEVNYNS LLESQNLYRD HYSDEISKLN
     EKIGLLELEL SNQNLNYGSD TSSNSDIELN LNKFNDSVKD LKSLETEKDS KLSKIITHSL
     DELNLQSWLN LYQTNENLIS TFAEKMDLKD VLKRNDEKIS NKGAVVQTLK KNVQTQVESN
     NADALSSNNA QDMLPIKMVK LRKTPNTNDS SSNGNSSNNK RRSFYTASPL LSSGSIPKSA
     SPVLPGVKRT ASVRKPSSSS SKTNVTHNND PSTSPTISVP PGVTRTVSST HKKKRNSMVV
     HGAQS