SHE3_CANGA
ID SHE3_CANGA Reviewed; 358 AA.
AC Q6FMH8;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=SWI5-dependent HO expression protein 3;
GN Name=SHE3; OrderedLocusNames=CAGL0K07942g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR380957; CAG61529.1; -; Genomic_DNA.
DR RefSeq; XP_448566.1; XM_448566.1.
DR AlphaFoldDB; Q6FMH8; -.
DR SMR; Q6FMH8; -.
DR STRING; 5478.XP_448566.1; -.
DR EnsemblFungi; CAG61529; CAG61529; CAGL0K07942g.
DR GeneID; 2890368; -.
DR KEGG; cgr:CAGL0K07942g; -.
DR CGD; CAL0134323; CAGL0K07942g.
DR VEuPathDB; FungiDB:CAGL0K07942g; -.
DR eggNOG; ENOG502QSQX; Eukaryota.
DR HOGENOM; CLU_773848_0_0_1; -.
DR InParanoid; Q6FMH8; -.
DR OMA; HFMANIN; -.
DR Proteomes; UP000002428; Chromosome K.
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..358
FT /note="SWI5-dependent HO expression protein 3"
FT /id="PRO_0000408930"
FT REGION 279..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 39..118
FT /evidence="ECO:0000255"
FT COILED 181..215
FT /evidence="ECO:0000255"
FT COMPBIAS 279..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 358 AA; 40029 MW; 1F10C97C8418723A CRC64;
MSLENAVRVV STDEKGNQAS STKLIELLHS RVDALTTTNI ELTTKLQELL GNLDTVQQRE
RKLKESAASL RHEGDNVTLM LNRKERKLTE VKEAIVELTT KLGEAKEVNH SLKQKFEDEG
LTSEESLRES ISEVKTEYDT LVKSHEIYES SNDIQCKSLE DRFSQALLIH GENMKALDGT
AEQILANNSE LVSQLRATEN KAESARTSIR NASIDTAAKV DLEKWLFLYK EAQRICEEFA
SKTDTKLPDE LQAIIDDPVL KELDARFALD EIQYGKTRNK RIPSNPLLSN SQAAARRVAS
PSANYSPRVS SAQGSLPGIT RTPSMKVNNK FSDSNAQEVP TRLHSHGSRS KRSSMVFK