SHE3_KLULA
ID SHE3_KLULA Reviewed; 345 AA.
AC Q6CRH4;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=SWI5-dependent HO expression protein 3;
GN Name=SHE3; OrderedLocusNames=KLLA0D09042g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382124; CAH00561.1; -; Genomic_DNA.
DR RefSeq; XP_453465.1; XM_453465.1.
DR AlphaFoldDB; Q6CRH4; -.
DR SMR; Q6CRH4; -.
DR STRING; 28985.XP_453465.1; -.
DR PRIDE; Q6CRH4; -.
DR EnsemblFungi; CAH00561; CAH00561; KLLA0_D09042g.
DR GeneID; 2892922; -.
DR KEGG; kla:KLLA0_D09042g; -.
DR eggNOG; ENOG502QSQX; Eukaryota.
DR HOGENOM; CLU_038734_0_0_1; -.
DR InParanoid; Q6CRH4; -.
DR OMA; NISHYNH; -.
DR Proteomes; UP000000598; Chromosome D.
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..345
FT /note="SWI5-dependent HO expression protein 3"
FT /id="PRO_0000408932"
FT REGION 273..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 92..272
FT /evidence="ECO:0000255"
SQ SEQUENCE 345 AA; 39235 MW; 40D5AB21B366E756 CRC64;
MKMTEAQEFL TPTKGVNSSK FNINHGHFIT NLENQESPSK LGAYTPGKYS TSRVIESLHK
QIDELTSTNL KMTSQCHQLV NELESSGKKQ NKQLETISRL QTENMNLNAI LDRKTNRMNE
LESSLKKQTV FNEDAAKKNL ELEETVKKLS LENEKLTEQS TLYKIQYEAI VDAHQSYKQF
FTNETSTLRN DLMSLKQSMT KQLESKTKEV LAIDEKIQNK LESLDSAQES FKKHASEQIE
DNIKELRLDS WQSSLREAQA LLKEYKSQAQ AEGITIQEQP KASIPQLRNP KRKTSGQKRT
SFYGTPTGFS IPSNKQTPPS SSSTQLPGLK RASSIRISSD PNRNR