ID   SHFL_BOVIN              Reviewed;         290 AA.
AC   Q32L09;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 77.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-2005) 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 (By
CC       similarity). May exhibit antiviral activity (By similarity).
CC       {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 the
CC       cytoplasm. {ECO:0000250|UniProtKB:Q9NUL5}.
CC   -!- SIMILARITY: Belongs to the SHFL family. {ECO:0000305}.
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DR   EMBL; BC109821; AAI09822.1; -; mRNA.
DR   RefSeq; NP_001033270.1; NM_001038181.1.
DR   AlphaFoldDB; Q32L09; -.
DR   STRING; 9913.ENSBTAP00000020765; -.
DR   PaxDb; Q32L09; -.
DR   PRIDE; Q32L09; -.
DR   Ensembl; ENSBTAT00000084842; ENSBTAP00000070425; ENSBTAG00000015636.
DR   GeneID; 539087; -.
DR   KEGG; bta:539087; -.
DR   CTD; 55337; -.
DR   VEuPathDB; HostDB:ENSBTAG00000015636; -.
DR   VGNC; VGNC:55202; SHFL.
DR   eggNOG; ENOG502QVND; Eukaryota.
DR   GeneTree; ENSGT00390000005065; -.
DR   OMA; CRKCKVK; -.
DR   OrthoDB; 1485595at2759; -.
DR   Proteomes; UP000009136; Chromosome 7.
DR   Bgee; ENSBTAG00000015636; Expressed in monocyte and 104 other tissues.
DR   ExpressionAtlas; Q32L09; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
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: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   Acetylation; Antiviral defense; Cytoplasm; Nucleus; Reference proteome;
KW   RNA-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NUL5"
FT   CHAIN           2..290
FT                   /note="Shiftless antiviral inhibitor of ribosomal
FT                   frameshifting protein homolog"
FT                   /id="PRO_0000318700"
FT   REGION          49..71
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   REGION          269..290
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           121..137
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NUL5"
FT   MOTIF           261..269
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NUL5"
FT   COMPBIAS        56..71
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NUL5"
SQ   SEQUENCE   290 AA;  33205 MW;  01269A47A778568F CRC64;
     MSQEGVELEK SVRRLREKFH GKVSSKKAGT LMRKFGSDHT GVGRSIVYGV KQKDGQELSN
     DLDTQDPPED MKQDRDIQAV ATSLLPLTED NLRMFQRAQE DLIPAVDRQF ACSSCDHVWW
     RRVPQRKEVS RCRKCRKRYD PVPSDKMWGV AEFHCPKCRH NFRGWAQMGS RSPCYGCGFP
     VYPTRILPPR WDRDPDRRST HTHSCSAEDC YNRREPHVPG TSCAHPKSRK QNHLPKVLHP
     SNLHISSGST VATCLSQGGL LEDLDNLILE DLKEEEEEEE EEEEEGGHGE