ID   SHE3_CANTT              Reviewed;         494 AA.
AC   C5MH60;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=SWI5-dependent HO expression protein 3;
GN   Name=SHE3; ORFNames=CTRG_05414;
OS   Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=294747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-3404 / T1;
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: 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; GG692402; EER30962.1; -; Genomic_DNA.
DR   RefSeq; XP_002551116.1; XM_002551070.1.
DR   AlphaFoldDB; C5MH60; -.
DR   SMR; C5MH60; -.
DR   STRING; 5482.XP_002551116.1; -.
DR   EnsemblFungi; EER30962; EER30962; CTRG_05414.
DR   GeneID; 8299739; -.
DR   KEGG; ctp:CTRG_05414; -.
DR   VEuPathDB; FungiDB:CTRG_05414; -.
DR   eggNOG; ENOG502QSQX; Eukaryota.
DR   HOGENOM; CLU_042310_0_0_1; -.
DR   OrthoDB; 1158686at2759; -.
DR   Proteomes; UP000002037; 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   Reference proteome; RNA-binding; Transport.
FT   CHAIN           1..494
FT                   /note="SWI5-dependent HO expression protein 3"
FT                   /id="PRO_0000408931"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          291..494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          24..173
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        291..314
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        331..494
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   494 AA;  56196 MW;  8A3726FA57F622EA CRC64;
     MPDTPVSPSK NNVKTSSTPV SSSTKVIDSL HSKIDELTDE LTTLKQSHQE LTKKHSIVAK
     KNDSFVDQLA NAKHENDMLS ALLKRKERRI LDLEDQYNDL NSQIENLSLS NKNMKIRCEN
     LQNNSNASIA EFERLKISYD ALIASQMEYK NHYQQELNTL QTSFDKYRTE NTKRYEDLQS
     SISSNDKDID TLLDSLTNKR KTMDNIYVNK NNKILQLLTS LASLIKLHAE DTKGQVEQNV
     DVIKILMEKY PDLQEKILEK EKVEVDLDEI ISHSNEILAN TSFEEDATLI NSPDLDSQSN
     LNSGAATPVQ NSGPFRKKKN YKRNSMILKD SPSGIPENSV PSSLPKKPQV NNNIINIPKN
     RSKFNTPPTT PRQFSNQSTD FEVTHQWNGN NNQHNNSGHY NNNNHRRTTS YDARSDNGGN
     RRQHSQGSNY NNNNNNNNNN NNGFVRRSGS VRNGSNNNNN NNHGKQAKRR STYNPNNNSK
     RNSQIFDSNF ALNV