ID F_HCVH Reviewed; 162 AA.
AC P0C045;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 30-NOV-2016, entry version 42.
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 H) (HCV).
OC Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
OC Flaviviridae; Hepacivirus.
OX NCBI_TaxID=11108;
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.,
RA Prince A.M.;
RT "Genomic structure of the human prototype strain H of hepatitis C
RT virus: 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
RT transcribed RNA.";
RL Science 277:570-574(1997).
RN [3]
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
RT protein.";
RL J. Gen. Virol. 84:1751-1759(2003).
RN [4]
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
RT double-frameshift protein, and others.";
RL Semin. Liver Dis. 25:105-117(2005).
CC -!- INTERACTION:
CC Q63HM2:PCNX4 (xeno); NbExp=3; IntAct=EBI-9351969, EBI-1104540;
CC Q9UHV9:PFDN2 (xeno); NbExp=4; IntAct=EBI-9351969, EBI-359873;
CC -!- SUBCELLULAR LOCATION: Host cytoplasm
CC {ECO:0000269|PubMed:12810869}. Host cytoplasm, host perinuclear
CC 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
CC unknown. The F protein seems to be generated by a -2 ribosomal
CC frameshift located in the vicinity of codon 11 of the core
CC protein coding sequence. However, some F proteins may also be
CC generated by +1 ribosomal frameshift. Since the core gene
CC encodes alternative reading frame proteins (ARFPs), many
CC functions depicted for the core protein might belong to the
CC ARFPs.;
CC Name=F protein; Synonyms=Frameshifted protein;
CC IsoId=P0C045-1; Sequence=Displayed;
CC Note=Produced by ribosomal frameshifting.;
CC Name=Genome polyprotein;
CC IsoId=P27958-1; Sequence=External;
CC Note=Produced by conventional translation.;
CC -!- MISCELLANEOUS: This protein is very unstable.
DR EMBL; M67463; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AF009606; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR ProteinModelPortal; P0C045; -.
DR IntAct; P0C045; 13.
DR euHCVdb; AF009606; -.
DR euHCVdb; M67463; -.
DR Proteomes; UP000000518; 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:0001948; F:glycoprotein binding; IPI:AgBase.
DR GO; GO:0017137; F:Rab GTPase binding; IPI:AgBase.
DR GO; GO:0097655; F:serpin family protein 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 InterPro; IPR002522; HCV_core_N.
DR Pfam; PF01543; HCV_capsid; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Host cytoplasm; Reference proteome;
KW Ribosomal frameshifting.
FT INIT_MET 1 1 Removed; by host. {ECO:0000250}.
FT CHAIN 2 162 F protein.
FT /FTId=PRO_0000109553.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 66 127 ipfam:HCV_capsid [T]
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
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