SHE3_YEAS1
ID SHE3_YEAS1 Reviewed; 425 AA.
AC B3LN26;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 31.
DE RecName: Full=SWI5-dependent HO expression protein 3;
GN Name=SHE3; ORFNames=SCRG_02838;
OS Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=285006;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM11-1a;
RG The Broad Institute Genome Sequencing Platform;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA Kruglyak L.;
RT "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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; CH408048; EDV11979.1; -; Genomic_DNA.
DR AlphaFoldDB; B3LN26; -.
DR SMR; B3LN26; -.
DR EnsemblFungi; EDV11979; EDV11979; SCRG_02838.
DR HOGENOM; CLU_038734_0_0_1; -.
DR Proteomes; UP000008335; 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 Phosphoprotein; RNA-binding; Transport.
FT CHAIN 1..425
FT /note="SWI5-dependent HO expression protein 3"
FT /id="PRO_0000408937"
FT REGION 24..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 68..197
FT /evidence="ECO:0000255"
FT COMPBIAS 323..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38272"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38272"
SQ SEQUENCE 425 AA; 47516 MW; 590414D3E140BB7A CRC64;
MSDQDNTQTS SSKLAPHHNI FMANLESSPT KDRNTSSQNA SSSRVIESLH DQIDMLTKTN
LQLTTQSQNL LSKLELAQSK ESKLLENLNL LKNENENLNS IFERKNKKLK ELEKDYSELS
NRYNEQKEKM DQLSKLAKNS SAIEQSCSEK LQNMEVNYNS LLESQNLYRD HYSDEISKLN
EKIGLLELEL SNQNLNYGSD TSSNSDIELN LNKFNDSVKD LKSLETEKDS KLSKIITHSL
DELNLQSWLN LYQTNENLIS TFAEKMDLKD VLKRNDEKIS NKGAVVQTLK KNVQTQVESN
NADALSSNNA QDMLPIKMVK LRKTPNTNDS SSNGNSSNNK RRSFYTASPL LSSGSIPKSA
SPVLPGVKRT ASVRKPSSSS SKTNVTHNND PSTSPTISVP PGVTRTVSST HKKKRNSMVV
HGAQS