SHFL_DANRE
ID SHFL_DANRE Reviewed; 327 AA.
AC A7YY07;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Shiftless antiviral inhibitor of ribosomal frameshifting protein homolog {ECO:0000305};
DE Short=SHFL;
DE AltName: Full=Repressor of yield of DENV protein homolog;
GN Name=shfl; ORFNames=zgc:171711;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB; TISSUE=Gill;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Inhibits programmed -1 ribosomal frameshifting (-1PRF) of a
CC variety of mRNAs from viruses and cellular genes. Interacts with the
CC -1PRF signal of target mRNA and translating ribosomes and causes
CC premature translation termination at the frameshifting site. May
CC exhibit antiviral activity. {ECO:0000250|UniProtKB:Q9NUL5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NUL5}. Nucleus
CC {ECO:0000250|UniProtKB:Q9NUL5}. Cytoplasm, P-body
CC {ECO:0000250|UniProtKB:Q9NUL5}. Note=Predominantly found in t for
CC dsDNA. {ECO:0000250|UniProtKB:Q9NUL5}.
CC -!- SIMILARITY: Belongs to the SHFL family. {ECO:0000305}.
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DR EMBL; BC148174; AAI48175.1; -; mRNA.
DR RefSeq; NP_001098997.1; NM_001105527.1.
DR AlphaFoldDB; A7YY07; -.
DR STRING; 7955.ENSDARP00000068467; -.
DR PaxDb; A7YY07; -.
DR GeneID; 797287; -.
DR KEGG; dre:797287; -.
DR CTD; 55337; -.
DR ZFIN; ZDB-GENE-070928-25; shfl.
DR eggNOG; ENOG502QVND; Eukaryota.
DR InParanoid; A7YY07; -.
DR OrthoDB; 1485595at2759; -.
DR PhylomeDB; A7YY07; -.
DR PRO; PR:A7YY07; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:1990825; F:sequence-specific mRNA binding; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:2001125; P:negative regulation of translational frameshifting; ISS:UniProtKB.
DR GO; GO:0006449; P:regulation of translational termination; ISS:UniProtKB.
DR GO; GO:0035456; P:response to interferon-beta; ISS:UniProtKB.
DR GO; GO:0075523; P:viral translational frameshifting; ISS:UniProtKB.
DR InterPro; IPR026795; SHFL.
DR PANTHER; PTHR16135; PTHR16135; 1.
DR Pfam; PF15135; UPF0515; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Nucleus; Reference proteome; RNA-binding.
FT CHAIN 1..327
FT /note="Shiftless antiviral inhibitor of ribosomal
FT frameshifting protein homolog"
FT /id="PRO_0000318704"
FT REGION 82..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 163..179
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q9NUL5"
FT MOTIF 304..312
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250|UniProtKB:Q9NUL5"
FT COMPBIAS 91..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 327 AA; 37546 MW; DA4976FD1AA24E80 CRC64;
MSRMHEEVEL EKSVRRLREK FHGLIEIDTA VLLMRRYVKN HRMVAMWIAL MADNDRELDE
EDQAALNNDP VAKNVIMKLK AEEQQQEEKH AKSSSSGSSG AGPSAKAKKQ PSDDRDITEL
GTRLRVLPLT MENKRMFDQA QANQIPSDTH QFACESCDRD WWRRVPQRKR VSRCHRCKKK
NDPVPPDRMW GIAEFTCPNC TRNFKGFGRM DGRSPCYGCR SAIYPMKILP PRRKNMMPGP
KQRNQHSCFA EDCYHRMEPH VPGTECVHPH SRQKNRKPRV VYPSPAHISS GSTVNTCLSQ
GSLIESINEL ILDDIEEESE DDSDSSS