ID   SHE3_ZYGRC              Reviewed;         482 AA.
AC   C5DUI8;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=SWI5-dependent HO expression protein 3;
GN   Name=SHE3; OrderedLocusNames=ZYRO0C17094g;
OS   Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568
OS   / NRRL Y-229) (Candida mogii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX   NCBI_TaxID=559307;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2623 / CBS 732 / BCRC 21506 / NBRC 1130 / NCYC 568 / NRRL
RC   Y-229;
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA   Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA   Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA   Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA   Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA   Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA   Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA   Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA   Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(2009).
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; CU928175; CAR27449.1; -; Genomic_DNA.
DR   RefSeq; XP_002496382.1; XM_002496337.1.
DR   AlphaFoldDB; C5DUI8; -.
DR   SMR; C5DUI8; -.
DR   STRING; 559307.C5DUI8; -.
DR   PRIDE; C5DUI8; -.
DR   EnsemblFungi; CAR27449; CAR27449; ZYRO0C17094g.
DR   GeneID; 8203613; -.
DR   KEGG; zro:ZYRO0C17094g; -.
DR   HOGENOM; CLU_038734_0_0_1; -.
DR   InParanoid; C5DUI8; -.
DR   Proteomes; UP000008536; Chromosome C.
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   Reference proteome; RNA-binding; Transport.
FT   CHAIN           1..482
FT                   /note="SWI5-dependent HO expression protein 3"
FT                   /id="PRO_0000408942"
FT   REGION          1..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          163..190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          353..378
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          390..482
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          127..292
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        75..90
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        163..187
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        356..375
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        410..427
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        434..482
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   482 AA;  52960 MW;  A0002275E0B7E758 CRC64;
     MTEDFEVNLG TGGEDNSSST MEHRVLDSPP RVVIPEDTES PAKLAPNHGI FMASINKSSP
     AGKKSGEGAV LGMGAQSTKD NSTPRQNSSM LSTRVIESLH DQVDTLTSTN LQLTVQSKNL
     LDKLDTAQQK ESKMLENSAS LKHENENLVS MLNRKTRRLK DVEEELASHK KNHDSLEEEK
     TALQKKWESS SSEEATLRQQ MEMVQAQYDA LVDSHQYYKS HYSSQISTLS EQLENLKLEQ
     RNYTQRVSDE ANTFNAKLLE FDSKHANLQQ AEETRVKYLE SKYDSLTQQL DLPSWVQLYR
     ESKNMVLEFA EKMKLKIPSD FETLIQDPEL TALEAKNPNS NNAAALPLRV AKQRAGGGNA
     TSTQSGTSGS NAAHGKRSSF YGGMASSYPA STLPGTLPGV RRSSSRRKPS SRVASDNSNS
     GDSSPIFPHS AVATAPRSSA TAPSSRVSST STSSSTNHFA FHNNNSNNTY RKRQESTSVG
     NS