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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
 
 
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