SHE3_ASHGO
ID SHE3_ASHGO Reviewed; 470 AA.
AC Q75EN7;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=SWI5-dependent HO expression protein 3;
GN Name=SHE3; OrderedLocusNames=AAR042W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016814; AAS50407.1; -; Genomic_DNA.
DR RefSeq; NP_982583.1; NM_207936.1.
DR AlphaFoldDB; Q75EN7; -.
DR SMR; Q75EN7; -.
DR STRING; 33169.AAS50407; -.
DR EnsemblFungi; AAS50407; AAS50407; AGOS_AAR042W.
DR GeneID; 4618697; -.
DR KEGG; ago:AGOS_AAR042W; -.
DR eggNOG; ENOG502QSQX; Eukaryota.
DR HOGENOM; CLU_038734_0_0_1; -.
DR InParanoid; Q75EN7; -.
DR OMA; HFMANIN; -.
DR Proteomes; UP000000591; Chromosome I.
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..470
FT /note="SWI5-dependent HO expression protein 3"
FT /id="PRO_0000408927"
FT REGION 48..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 82..234
FT /evidence="ECO:0000255"
FT COMPBIAS 329..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 470 AA; 52007 MW; 85022B3A248DF43E CRC64;
MAATNAVEAG YGGAAENGGC AEGLLGSPMR FSPSSKLKVN HGHFMANINN NAGPGKGGTA
AGGTSPTREA SYANVSGSGK VIENLHQQVD ALTSTNLQLT KQSNQLLEKL EGCNAREAKY
LETISSLKHE NENLNSMLNR KTRRVKDLDM ELVQLRTSHE EATASHNQLK YQLENKFAHE
TELEQQCQLL QAQYDAVVDA QRRYREHYQK EIEELREALE ALKKDNDKFL GEHMARLTRS
QLDIDKSMSD YNGKFHRMEL SQKEAVIELN EKYDRMRADL DVDGWIVLYK QMRDIAFDYA
KQLDLSLPKE FAELHGEDGY YAKMLDEDRQ SSPVSTSSTA VEPMSQPSPS MSAQTLSPPP
LRVPKNRTPI TKRSSFYGNT MPGANISLTS ATGLLPGVKR TGSIRSFHGR APSEGLSDTP
TIFTASRNAS PMEFPQRSAL TSAASANATV RHSSVPRHRR NQSSQVGNNK