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Frameshifted structural polyprotein (p130) [Cleaved into: Capsid protein (EC 3.4.21.90) (Coat protein) (C); p62 (E3/E2); Protein E3 (Spike glycoprotein E3); Envelope glycoprotein E2 (Spike glycoprotein E2); Protein TF]

 POLSF_SFV               Reviewed;         830 AA.
P0DJZ6;
09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
09-DEC-2015, sequence version 1.
25-APR-2018, entry version 10.
RecName: Full=Frameshifted structural polyprotein;
AltName: Full=p130;
Contains:
RecName: Full=Capsid protein;
EC=3.4.21.90;
AltName: Full=Coat protein;
Short=C;
Contains:
RecName: Full=p62;
AltName: Full=E3/E2;
Contains:
RecName: Full=Protein E3;
AltName: Full=Spike glycoprotein E3;
Contains:
RecName: Full=Envelope glycoprotein E2;
AltName: Full=Spike glycoprotein E2;
Contains:
RecName: Full=Protein TF;
Semliki forest virus (SFV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Togaviridae; Alphavirus.
NCBI_TaxID=11033;
NCBI_TaxID=7158; Aedes.
NCBI_TaxID=9368; Atelerix albiventris (Middle-African hedgehog) (Four-toed hedgehog).
NCBI_TaxID=7178; Culex tritaeniorhynchus (Mosquito).
NCBI_TaxID=170865; Halcyon.
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=158617; Quelea.
NCBI_TaxID=34630; Rhipicephalus.
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=A7;
PubMed=9225028; DOI=10.1099/0022-1317-78-7-1551;
Tarbatt C.J., Glasgow G.M., Mooney D.A., Sheahan B.J., Atkins G.J.;
"Sequence analysis of the avirulent, demyelinating A7 strain of
Semliki Forest virus.";
J. Gen. Virol. 78:1551-1557(1997).
[2]
FUNCTION (CAPSID PROTEIN), AUTOCATALYTIC CLEAVAGE BY CAPSID PROTEIN,
AND MUTAGENESIS OF 219-SER-GLY-220.
PubMed=3553612;
Melancon P., Garoff H.;
"Processing of the Semliki Forest virus structural polyprotein: role
of the capsid protease.";
J. Virol. 61:1301-1309(1987).
[3]
FUNCTION (ENVELOPE GLYCOPROTEIN E2).
PubMed=1714373;
Kail M., Hollinshead M., Ansorge W., Pepperkok R., Frank R.,
Griffiths G., Vaux D.;
"The cytoplasmic domain of alphavirus E2 glycoprotein contains a short
linear recognition signal required for viral budding.";
EMBO J. 10:2343-2351(1991).
[4]
CLEAVAGE SITE OF P62, AND MUTAGENESIS OF ARG-330 AND ARG-333.
PubMed=2005112;
Jain S.K., DeCandido S., Kielian M.;
"Processing of the p62 envelope precursor protein of Semliki Forest
virus.";
J. Biol. Chem. 266:5756-5761(1991).
[5]
FUNCTION (CAPSID PROTEIN), AND AUTOCATALYTIC CLEAVAGE BY CAPSID
PROTEIN.
PubMed=9642067; DOI=10.1006/jmbi.1998.1817;
Skoging U., Liljestrom P.;
"Role of the C-terminal tryptophan residue for the structure-function
of the alphavirus capsid protein.";
J. Mol. Biol. 279:865-872(1998).
[6]
PROTEOLYTIC PROCESSING OF P62 BY HOST FURIN.
PubMed=12584323; DOI=10.1128/JVI.77.5.2981-2989.2003;
Zhang X., Fugere M., Day R., Kielian M.;
"Furin processing and proteolytic activation of Semliki Forest
virus.";
J. Virol. 77:2981-2989(2003).
[7]
FUNCTION (PROTEIN TF), AND SUBCELLULAR LOCATION (PROTEIN TF).
PubMed=18822126; DOI=10.1186/1743-422X-5-108;
Firth A.E., Chung B.Y., Fleeton M.N., Atkins J.F.;
"Discovery of frameshifting in Alphavirus 6K resolves a 20-year
enigma.";
Virol. J. 5:108-108(2008).
[8]
FUNCTION (PROTEIN E3).
PubMed=23864626; DOI=10.1128/JVI.01507-13;
Uchime O., Fields W., Kielian M.;
"The role of E3 in pH protection during alphavirus assembly and
exit.";
J. Virol. 87:10255-10262(2013).
-!- FUNCTION: Capsid protein: Possesses a protease activity that
results in its autocatalytic cleavage from the nascent structural
protein. Following its self-cleavage, the capsid protein
transiently associates with ribosomes, and within several minutes
the protein binds to viral RNA and rapidly assembles into
icosahedric core particles. The resulting nucleocapsid eventually
associates with the cytoplasmic domain of E2 at the cell membrane,
leading to budding and formation of mature virions. New virions
attach to target cells, and after clathrin-mediated endocytosis
their membrane fuses with the host endosomal membrane. This leads
to the release of the nucleocapsid into the cytoplasm, followed by
an uncoating event necessary for the genomic RNA to become
accessible. The uncoating might be triggered by the interaction of
capsid proteins with ribosomes. Binding of ribosomes would release
the genomic RNA since the same region is genomic RNA-binding and
ribosome-binding. {ECO:0000269|PubMed:3553612,
ECO:0000269|PubMed:9642067}.
-!- FUNCTION: Protein E3: Provides the signal sequence for p62 (E3/E2)
translocation to the host endoplasmic reticulum. Mediates pH
protection of E1 during secretory pathway trans- port.
{ECO:0000269|PubMed:23864626}.
-!- FUNCTION: Envelope glycoprotein E2: Plays a role in viral
attachment to target host cell, by binding to the cell receptor.
Synthesized as a p62 precursor which is processed by furin at the
cell membrane just before virion budding, giving rise to E2-E1
heterodimer. The p62-E1 heterodimer is stable, whereas E2-E1 is
unstable and dissociate at low pH. p62 is processed at the last
step, presumably to avoid E1 fusion activation before its final
export to cell surface. E2 C-terminus contains a transitory
transmembrane that would be disrupted by palmitoylation, resulting
in reorientation of the C-terminal tail from lumenal to
cytoplasmic side. This step is critical since E2 C-terminus is
involved in budding by interacting with capsid proteins. This
release of E2 C-terminus in cytoplasm occurs lately in protein
export, and precludes premature assembly of particles at the
endoplasmic reticulum membrane. {ECO:0000269|PubMed:1714373}.
-!- FUNCTION: Protein TF: Virion component that may play a role during
viral assembly. {ECO:0000269|PubMed:18822126}.
-!- CATALYTIC ACTIVITY: Autocatalytic release of the core protein from
the N-terminus of the togavirus structural polyprotein by
hydrolysis of a -Trp-|-Ser- bond.
-!- SUBUNIT: p62 and E1 form a heterodimer shortly after synthesis.
Processing of p62 into E2 and E3 results in a heterodimer of E2
and E1. Spike at virion surface are constituted of three E2-E1
heterodimers. After target cell attachment and endocytosis, E1
change conformation to form homotrimers.
{ECO:0000250|UniProtKB:P03315}.
-!- SUBCELLULAR LOCATION: Capsid protein: Virion {ECO:0000250}. Host
cytoplasm {ECO:0000250}.
-!- SUBCELLULAR LOCATION: p62: Virion membrane {ECO:0000250}; Single-
pass type I membrane protein {ECO:0000250}. Host cell membrane
{ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Envelope glycoprotein E2: Virion membrane
{ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Host cell membrane {ECO:0000250}; Single-pass type I membrane
protein {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Protein TF: Virion
{ECO:0000269|PubMed:18822126}.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=2;
Name=Frameshifted structural polyprotein;
IsoId=P0DJZ6-1; Sequence=Displayed;
Note=Produced by -1 ribosomal frameshifting in Protein 6K ORF.;
Name=Structural polyprotein;
IsoId=P03315-1; Sequence=External;
Note=Produced by conventional translation.;
-----------------------------------------------------------------------
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EMBL; Z48163; -; NOT_ANNOTATED_CDS; Genomic_RNA.
SMR; P0DJZ6; -.
Proteomes; UP000108382; Genome.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0039619; C:T=4 icosahedral viral capsid; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
InterPro; IPR002548; Alpha_E1_glycop.
InterPro; IPR000936; Alpha_E2_glycop.
InterPro; IPR002533; Alpha_E3_glycop.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR000930; Peptidase_S3.
Pfam; PF01589; Alpha_E1_glycop; 1.
Pfam; PF00943; Alpha_E2_glycop; 1.
Pfam; PF01563; Alpha_E3_glycop; 1.
Pfam; PF00944; Peptidase_S3; 1.
PRINTS; PR00798; TOGAVIRIN.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS51690; ALPHAVIRUS_CP; 1.
1: Evidence at protein level;
Autocatalytic cleavage; Capsid protein;
Clathrin-mediated endocytosis of virus by host;
Cleavage on pair of basic residues; Complete proteome; Disulfide bond;
Fusion of virus membrane with host endosomal membrane;
Fusion of virus membrane with host membrane; Glycoprotein;
Host cell membrane; Host cytoplasm; Host membrane;
Host-virus interaction; Hydrolase; Lipoprotein; Membrane; Palmitate;
Protease; Ribosomal frameshifting; Serine protease;
T=4 icosahedral capsid protein; Transmembrane; Transmembrane helix;
Viral attachment to host cell; Viral envelope protein;
Viral penetration into host cytoplasm; Virion;
Virus endocytosis by host; Virus entry into host cell.
CHAIN 1 267 Capsid protein.
{ECO:0000250|UniProtKB:P03315}.
/FTId=PRO_0000434879.
CHAIN 268 755 p62. {ECO:0000250|UniProtKB:P03315}.
/FTId=PRO_0000434880.
CHAIN 268 333 Protein E3.
{ECO:0000250|UniProtKB:P03315}.
/FTId=PRO_0000434881.
CHAIN 334 755 Envelope glycoprotein E2.
{ECO:0000250|UniProtKB:P03315}.
/FTId=PRO_0000434882.
CHAIN 756 830 Protein TF.
{ECO:0000250|UniProtKB:P03315}.
/FTId=PRO_0000434883.
TRANSMEM 702 722 Helical. {ECO:0000255}.
TRANSMEM 771 791 Helical. {ECO:0000255}.
TRANSMEM 793 813 Helical. {ECO:0000255}.
DOMAIN 119 267 Peptidase S3. {ECO:0000255|PROSITE-
ProRule:PRU01027}.
REGION 1 113 Intrinsically disordered, in contact with
genomic RNA in nucleocapsid.
{ECO:0000255}.
REGION 94 106 Ribosome-binding.
{ECO:0000250|UniProtKB:P03315}.
REGION 728 748 Transient transmembrane before p62-6K
protein processing. {ECO:0000255}.
COMPBIAS 66 71 Poly-Lys. {ECO:0000255}.
COMPBIAS 100 104 Poly-Lys. {ECO:0000255}.
ACT_SITE 145 145 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU01027}.
ACT_SITE 151 151 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU01027}.
ACT_SITE 219 219 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU01027}.
SITE 267 268 Cleavage; by capsid protein.
{ECO:0000250|UniProtKB:P03315}.
SITE 333 334 Cleavage; by host furin.
{ECO:0000250|UniProtKB:P03315}.
SITE 755 756 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P03315}.
LIPID 718 718 S-palmitoyl cysteine; by host.
{ECO:0000255}.
LIPID 728 728 S-palmitoyl cysteine; by host.
{ECO:0000250}.
LIPID 748 748 S-palmitoyl cysteine; by host.
{ECO:0000250}.
LIPID 749 749 S-palmitoyl cysteine; by host.
{ECO:0000250}.
CARBOHYD 280 280 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 327 327 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 533 533 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 595 595 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 119 134 {ECO:0000250|UniProtKB:P03315}.
MUTAGEN 219 220 SG->RST: Loss of autocatalytic cleavage
by capsid protein.
{ECO:0000269|PubMed:3553612}.
MUTAGEN 330 330 R->S: Complete loss of p62 precursor
processing. {ECO:0000269|PubMed:2005112}.
MUTAGEN 333 333 R->F: Complete loss of p62 precursor
processing. {ECO:0000269|PubMed:2005112}.
SEQUENCE 830 AA; 92349 MW; C095CB68C85C4985 CRC64;
MNYIPTQTFY GRRWRPRPAA RPWPLQATPV APVVPDFQAQ QMQQLISAVN ALTMRQNAIA
PARPPKPKKK KTTKPKPKTQ PKKINGKTQQ QKKKDKQADK KKKKPGKRER MCMKIENDCI
FEVKHEGKVT GYACLVGDKV MKPAHVKGVI DNADLAKLAF KKSSKYDLEC AQIPVHMRSD
ASKYTHEKPE GHYNWHHGAV QYSGGRFTIP TGAGKPGDSG RPIFDNKGRV VAIVLGGANE
GSRTALSVVT WNKDMVTRVT PEGSEEWSAP LITAMCVLAN ATFPCFQPPC VPCCYENNAE
ATLRMLEDNV DRPGYYDLLQ AALTCRNGTR HRRSVSQHFN VYKATRPYIA YCADCGAGHS
CHSPVAIEAV RSEATDGMLK IQFSAQIGID KSDNHDYTKI RYADGHAIEN AVRSSLKVAT
SGDCFVHGTM GHFILAKCPP GEFLQVSIQD TRNAVRACRI QYHHDPQPVG REKFTIRPHY
GKEIPCTTYQ QTTAETVEEI DMHMPPDTPD RTLLSQQSGN VKITVGGKKV KYNCTCGTGN
VGTTNSDMTI NTCLIEQCHV SVTDHKKWQF NSPFVPRADE PARKGKVHIP FPLDNITCRV
PMAREPTVIH GKREVTLHLH PDHPTLFSYR TLGEDPQYHE EWVTAAVERT IPVPVDGMEY
HWGNNDPVRL WSQLTTEGKP HGWPHQIVQY YYGLYPAATV SAVVGMSLLA LISIFASCYM
LVAARSKCLT PYALTPGAAV PWTLGILCCA PRAHAASVAE TMAYLWDQNQ ALFWLEFAAP
VACILIITYC LRNVLCCCKS LSFLSATEPR GHRQSLRTFD SNAERGGVPV


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