ID   SHE3_CANDC              Reviewed;         551 AA.
AC   B9WJ48;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=SWI5-dependent HO expression protein 3;
GN   Name=SHE3; ORFNames=CD36_63970;
OS   Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS   NRRL Y-17841) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=573826;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841;
RX   PubMed=19745113; DOI=10.1101/gr.097501.109;
RA   Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA   Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA   de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA   Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA   Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT   "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT   Candida albicans.";
RL   Genome Res. 19:2231-2244(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; FM992693; CAX41269.1; -; Genomic_DNA.
DR   RefSeq; XP_002421110.1; XM_002421065.1.
DR   AlphaFoldDB; B9WJ48; -.
DR   SMR; B9WJ48; -.
DR   STRING; 42374.XP_002421110.1; -.
DR   EnsemblFungi; CAX41269; CAX41269; CD36_63970.
DR   GeneID; 8048891; -.
DR   KEGG; cdu:CD36_63970; -.
DR   CGD; CAL0000162424; Cd36_63970.
DR   VEuPathDB; FungiDB:CD36_63970; -.
DR   eggNOG; ENOG502QSQX; Eukaryota.
DR   HOGENOM; CLU_042310_0_0_1; -.
DR   OrthoDB; 1158686at2759; -.
DR   Proteomes; UP000002605; Chromosome 6.
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; RNA-binding;
KW   Transport.
FT   CHAIN           1..551
FT                   /note="SWI5-dependent HO expression protein 3"
FT                   /id="PRO_0000408929"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          285..551
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          20..110
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        285..323
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        344..418
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        419..448
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        449..551
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   551 AA;  62956 MW;  E7537BBD2F65DE5A CRC64;
     MTDTPNSPSK NTTKSASSST KVIDSLHSKI DQLTDELTAL KQSHQELTKK HSITAKKNDS
     FVDQLANAKH ENDMLSALLK RKERRILDLE DQFNELTSQN ESLVLSNKNM KIRCDNLQSN
     SNANIAEFER LKISYDALIA SQMEYKNHYQ QELNNLQIAF DNYKLENTKR FEELQTSIVN
     NDKDIDTLLD SLTNKRKAMD NIYVNKNNKV LQLLGNLAHL AKLHGQDTKS QVEQNLNIIE
     QLLVKYPDLQ EKILEKEKIE IDLTEIIAHS NDVLTNSSFD EDTTLINSPD LENNHNFNNH
     NTSGSATPNN NNHNNNSNSH SLQSKKRKNY KRNSLILKES PPIISENVPS SLPKKPQVNN
     NLINIPKSRS KFNTPPTTPR QTTPRQFTNH NNDFEITHQW SSNNNNNNNN NNNNHRRNNS
     VDSRSDNGHH PHRRNNSYDS RPDHGQQHRR QPSQQNNNYN NNNYNNNNNN NNNINNNSNG
     FVKRSGSVRN GNNYNNNNGN GNGNGNGNAN NNANNHGNKS KRRSTYNNNN NNNNNSKRNS
     QLFDNNFALN V