F_HCV77
ID F_HCV77 Reviewed; 162 AA.
AC P0C045;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=F protein;
DE AltName: Full=Alternate reading frame protein/F-protein;
DE Short=ARFP/F;
DE AltName: Full=Frameshifted protein;
DE AltName: Full=p16;
DE AltName: Full=p17;
OS Hepatitis C virus genotype 1a (isolate H77) (HCV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Hepacivirus; hepatitis C virus genotype 1a.
OX NCBI_TaxID=63746;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1658800; DOI=10.1073/pnas.88.22.10292;
RA Inchauspe G., Zebedee S., Lee D.H.H., Sugitani M., Nasoff M., Prince A.M.;
RT "Genomic structure of the human prototype strain H of hepatitis C virus:
RT comparison with American and Japanese isolates.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:10292-10296(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate H77;
RX PubMed=9228008; DOI=10.1126/science.277.5325.570;
RA Kolykhalov A.A., Agapov E.V., Blight K.J., Mihalik K., Feinstone S.M.,
RA Rice C.M.;
RT "Transmission of hepatitis C by intrahepatic inoculation with transcribed
RT RNA.";
RL Science 277:570-574(1997).
RN [3]
RP RIBOSOMAL FRAMESHIFT.
RX PubMed=11447125; DOI=10.1093/emboj/20.14.3840;
RA Xu Z., Choi J., Yen T.S.B., Lu W., Strohecker A., Govindarajan S.,
RA Chien D., Selby M.J., Ou J.-H.;
RT "Synthesis of a novel hepatitis C virus protein by ribosomal frameshift.";
RL EMBO J. 20:3840-3848(2001).
RN [4]
RP CHARACTERIZATION, AND SUBCELLULAR LOCATION.
RX PubMed=12810869; DOI=10.1099/vir.0.19065-0;
RA Roussel J., Pillez A., Montpellier C., Duverlie G., Cahour A.,
RA Dubuisson J., Wychowski C.;
RT "Characterization of the expression of the hepatitis C virus F protein.";
RL J. Gen. Virol. 84:1751-1759(2003).
RN [5]
RP REVIEW.
RX PubMed=15732002; DOI=10.1055/s-2005-864786;
RA Branch A.D., Stump D.D., Gutierrez J.A., Eng F., Walewski J.L.;
RT "The hepatitis C virus alternate reading frame (ARF) and its family of
RT novel products: the alternate reading frame protein/F-protein, the double-
RT frameshift protein, and others.";
RL Semin. Liver Dis. 25:105-117(2005).
RN [6]
RP FUNCTION.
RC STRAIN=isolate JFH-1;
RX PubMed=27404108; DOI=10.1371/journal.pone.0158419;
RA Park S.B., Seronello S., Mayer W., Ojcius D.M.;
RT "Hepatitis C Virus Frameshift/Alternate Reading Frame Protein Suppresses
RT Interferon Responses Mediated by Pattern Recognition Receptor Retinoic-
RT Acid-Inducible Gene-I.";
RL PLoS ONE 11:e0158419-e0158419(2016).
CC -!- FUNCTION: Contributes to the DDX58/RIG-I-mediated inhibition of type I
CC interferon production. {ECO:0000269|PubMed:27404108}.
CC -!- INTERACTION:
CC P0C045; Q63HM2: PCNX4; Xeno; NbExp=3; IntAct=EBI-9351969, EBI-1104540;
CC P0C045; Q9UHV9: PFDN2; Xeno; NbExp=4; IntAct=EBI-9351969, EBI-359873;
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:12810869}.
CC Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:12810869}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Comment=The exact location of the ribosomal frameshift is unknown.
CC The F protein seems to be generated by a -2 ribosomal frameshift
CC located in the vicinity of codon 11 of the core protein coding
CC sequence. However, some F proteins may also be generated by +1
CC ribosomal frameshift. Since the core gene encodes alternative reading
CC frame proteins (ARFPs), many functions depicted for the core protein
CC might belong to the ARFPs. {ECO:0000269|PubMed:11447125};
CC Name=F protein; Synonyms=Frameshifted protein;
CC IsoId=P0C045-1; Sequence=Displayed;
CC Name=Genome polyprotein;
CC IsoId=P27958-1; Sequence=External;
CC -!- MISCELLANEOUS: This protein is very unstable.
CC -!- MISCELLANEOUS: [Isoform F protein]: Produced by ribosomal
CC frameshifting.
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DR EMBL; M67463; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AF009606; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR IntAct; P0C045; 13.
DR PRIDE; P0C045; -.
DR euHCVdb; AF009606; -.
DR euHCVdb; M67463; -.
DR Proteomes; UP000000518; Genome.
DR Proteomes; UP000115192; Genome.
DR GO; GO:0042025; C:host cell nucleus; IDA:AgBase.
DR GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019028; C:viral capsid; IEA:InterPro.
DR GO; GO:0001848; F:complement binding; IPI:AgBase.
DR GO; GO:0019899; F:enzyme binding; IPI:AgBase.
DR GO; GO:0097655; F:serpin family protein binding; IPI:AgBase.
DR GO; GO:0031267; F:small GTPase binding; IPI:AgBase.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0035375; F:zymogen binding; IPI:AgBase.
DR GO; GO:0051494; P:negative regulation of cytoskeleton organization; IDA:AgBase.
DR GO; GO:0039540; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of host RIG-I activity; IEA:UniProtKB-KW.
DR InterPro; IPR002522; HCV_core_N.
DR Pfam; PF01543; HCV_capsid; 1.
PE 1: Evidence at protein level;
KW Host cytoplasm; Host-virus interaction;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host RIG-I by virus; Inhibition of host RLR pathway by virus;
KW Reference proteome; Ribosomal frameshifting; Viral immunoevasion.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000250"
FT CHAIN 2..162
FT /note="F protein"
FT /id="PRO_0000109553"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 162 AA; 17006 MW; AE9D5391D19211B6 CRC64;
MSTNPKPQRK KPNVTPTVAH RTSSSRVAVR SLVEFTCCRA GALDWVCARR GRLPSGRNLE
VDVSLSPRHV GPRAGPGLSP GTLGPSMAMR VAGGRDGSCL PVALGLAGAP QTPGVGRAIW
VRSSIPLRAA SPTSWGTYRS SAPLLEALPG PWRMASGFWK TA
