SHFL_MOUSE
ID SHFL_MOUSE Reviewed; 290 AA.
AC Q8CAK3; Q05BY8;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 122.
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 {ECO:0000312|MGI:MGI:2441788};
GN Synonyms=Ryden {ECO:0000250|UniProtKB:Q9NUL5};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CAK3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CAK3-2; Sequence=VSP_031275;
CC -!- SIMILARITY: Belongs to the SHFL family. {ECO:0000305}.
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DR EMBL; AK038619; BAC30066.1; -; mRNA.
DR EMBL; AK149161; BAE28753.1; -; mRNA.
DR EMBL; BC031510; AAH31510.1; -; mRNA.
DR EMBL; BC043448; AAH43448.1; -; mRNA.
DR CCDS; CCDS22885.1; -. [Q8CAK3-1]
DR RefSeq; NP_783618.1; NM_175687.2. [Q8CAK3-1]
DR AlphaFoldDB; Q8CAK3; -.
DR SMR; Q8CAK3; -.
DR BioGRID; 235173; 3.
DR STRING; 10090.ENSMUSP00000045384; -.
DR iPTMnet; Q8CAK3; -.
DR PhosphoSitePlus; Q8CAK3; -.
DR EPD; Q8CAK3; -.
DR MaxQB; Q8CAK3; -.
DR PaxDb; Q8CAK3; -.
DR PeptideAtlas; Q8CAK3; -.
DR PRIDE; Q8CAK3; -.
DR ProteomicsDB; 253329; -. [Q8CAK3-1]
DR ProteomicsDB; 253330; -. [Q8CAK3-2]
DR Antibodypedia; 51349; 37 antibodies from 11 providers.
DR Ensembl; ENSMUST00000043911; ENSMUSP00000045384; ENSMUSG00000038884. [Q8CAK3-1]
DR GeneID; 319278; -.
DR KEGG; mmu:319278; -.
DR UCSC; uc012gow.1; mouse. [Q8CAK3-1]
DR CTD; 55337; -.
DR MGI; MGI:2441788; Shfl.
DR VEuPathDB; HostDB:ENSMUSG00000038884; -.
DR eggNOG; ENOG502QVND; Eukaryota.
DR GeneTree; ENSGT00390000005065; -.
DR HOGENOM; CLU_087318_0_0_1; -.
DR InParanoid; Q8CAK3; -.
DR OMA; CRKCKVK; -.
DR OrthoDB; 1485595at2759; -.
DR PhylomeDB; Q8CAK3; -.
DR TreeFam; TF337433; -.
DR BioGRID-ORCS; 319278; 2 hits in 72 CRISPR screens.
DR ChiTaRS; A230050P20Rik; mouse.
DR PRO; PR:Q8CAK3; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8CAK3; protein.
DR Bgee; ENSMUSG00000038884; Expressed in superior frontal gyrus and 194 other tissues.
DR Genevisible; Q8CAK3; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
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 Alternative splicing; Antiviral defense; Cytoplasm; Nucleus;
KW Reference proteome; RNA-binding.
FT CHAIN 1..290
FT /note="Shiftless antiviral inhibitor of ribosomal
FT frameshifting protein homolog"
FT /id="PRO_0000318702"
FT REGION 51..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 221..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 VAR_SEQ 164..290
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031275"
SQ SEQUENCE 290 AA; 33015 MW; 2AA2E2D9D991CFA6 CRC64;
MAQDGVELEK SVRRLREKFH GKVSPKKAGA LMRKFGSDHT GVGRSIVYGV KQKDGQELSN
DLDAQDPPED MKQDQDIQAV ATSLLPLTQA NLRMFQRAQD DLIPAVDRQF ACSSCDHVWW
RRVPQRKEVS RCRKCRKRYE PVPLDKMWGL AEFHCPKCRH NFRGWAQMGS PSPCYGCGFP
VYPTRILPPR WDRDLDRRST HTHSCSAADC YNRREPHVPG TSCAHPKSRK QNHLPKVLHP
SNPHISSGST VATCLSQGGL VDDLDHLILE DLKEEEEEEE EEEEDGGPRE
