SHFL_RAT
ID SHFL_RAT Reviewed; 163 AA.
AC Q5RJN4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Shiftless antiviral inhibitor of ribosomal frameshifting protein homolog {ECO:0000305};
DE Short=SHFL {ECO:0000305};
DE AltName: Full=Repressor of yield of DENV protein homolog {ECO:0000250|UniProtKB:Q9NUL5};
DE Short=RyDEN {ECO:0000250|UniProtKB:Q9NUL5};
GN Name=Shfl; Synonyms=Ryden {ECO:0000250|UniProtKB:Q9NUL5};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 -!- SUBUNIT: Interacts with PABPC1. Found in a complex with PABPC1 and
CC LARP1. Interacts with ELAV1, MOV10 and UPF1; the interactions increase
CC in presence of RNA. Binds to ribosomes. Interacts with GSPT1.
CC {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; BC086569; AAH86569.1; -; mRNA.
DR RefSeq; NP_001020225.1; NM_001025054.1.
DR AlphaFoldDB; Q5RJN4; -.
DR SMR; Q5RJN4; -.
DR STRING; 10116.ENSRNOP00000027949; -.
DR jPOST; Q5RJN4; -.
DR PaxDb; Q5RJN4; -.
DR PRIDE; Q5RJN4; -.
DR GeneID; 500956; -.
DR KEGG; rno:500956; -.
DR UCSC; RGD:1565995; rat.
DR CTD; 55337; -.
DR RGD; 1565995; LOC500956.
DR eggNOG; ENOG502QVND; Eukaryota.
DR HOGENOM; CLU_087318_0_0_1; -.
DR InParanoid; Q5RJN4; -.
DR PhylomeDB; Q5RJN4; -.
DR PRO; PR:Q5RJN4; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; Q5RJN4; RN.
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:0051607; P:defense response to virus; 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:0045071; P:negative regulation of viral genome replication; 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:0034341; P:response to interferon-gamma; ISS:UniProtKB.
DR GO; GO:0034340; P:response to type I interferon; ISS:UniProtKB.
DR GO; GO:0034342; P:response to type III interferon; 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 Antiviral defense; Cytoplasm; Nucleus; Reference proteome; RNA-binding.
FT CHAIN 1..163
FT /note="Shiftless antiviral inhibitor of ribosomal
FT frameshifting protein homolog"
FT /id="PRO_0000318703"
FT REGION 51..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..150
FT /note="Interaction with PABPC1"
FT /evidence="ECO:0000250|UniProtKB:Q9NUL5"
FT MOTIF 121..137
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q9NUL5"
FT COMPBIAS 56..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 163 AA; 18865 MW; 336307C56F3A4190 CRC64;
MAQDGVELEK SVRRLREKFH GKVSPKKAGA LMRKFGSDHT GVGRSIVYGV KQKDGQELSN
DLDAQDPPED MKQDQDIQAV ATSLLPLTQA NLRMFQRAQD DLIPAVDRQF ACSSCDHVWW
RRVPQRKEVS RCRKCRKRYE PVPNDKMWGL AEFHCPKCRH NFR
