ID   SHFL_XENTR              Reviewed;         304 AA.
AC   A0JP89;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 56.
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;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (NOV-2006) 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; BC127301; AAI27302.1; -; mRNA.
DR   RefSeq; NP_001090662.1; NM_001097193.1.
DR   AlphaFoldDB; A0JP89; -.
DR   STRING; 8364.ENSXETP00000013541; -.
DR   PRIDE; A0JP89; -.
DR   DNASU; 100036634; -.
DR   GeneID; 100036634; -.
DR   KEGG; xtr:100036634; -.
DR   CTD; 55337; -.
DR   Xenbase; XB-GENE-951923; shfl.
DR   InParanoid; A0JP89; -.
DR   OrthoDB; 1485595at2759; -.
DR   Proteomes; UP000008143; Chromosome 3.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000022042; Expressed in liver and 13 other tissues.
DR   ExpressionAtlas; A0JP89; baseline.
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..304
FT                   /note="Shiftless antiviral inhibitor of ribosomal
FT                   frameshifting protein homolog"
FT                   /id="PRO_0000318706"
FT   MOTIF           140..156
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NUL5"
FT   MOTIF           278..287
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NUL5"
SQ   SEQUENCE   304 AA;  35246 MW;  046AA8F3E62ACC97 CRC64;
     MDGNVQEELE LEKSIRRFRE KFHGKVTLET AVALMRRFTN NHDQVCKYII LCMDNDTDLD
     VRNDLRNDPV ARNVINKIKS DDQKAKEMPK DKDIKDLAKR MNTLPLTEKN LKMFNDAAEN
     RIPSRDRQFA CKECDFVWWR RVPQRKEVSR CHRCRKKFDP VPENKMWGIA EYHCPVCRRM
     FRGFGQIEVS SPCYVCRNPV LPSCILPPRR NQGPRTRNTH SCLAENCYNR RVPFVAGLQC
     AHPKSRIMNQ LPKVLHPSEP HISTGSTIAT CLSQGSLTEN DIDDIILDDI KEEEEDEGSD
     DSDG