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Structural polyprotein (p130) [Cleaved into: Capsid protein (EC 3.4.21.-) (Coat protein) (C); p62 (E3/E2); E3 protein (Spike glycoprotein E3); E2 envelope glycoprotein (Spike glycoprotein E2); 6K protein; E1 envelope glycoprotein (Spike glycoprotein E1)]

 POLS_SPDV               Reviewed;        1320 AA.
Q8JJX0;
30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
23-MAY-2018, entry version 97.
RecName: Full=Structural polyprotein;
AltName: Full=p130;
Contains:
RecName: Full=Capsid protein;
EC=3.4.21.-;
AltName: Full=Coat protein;
Short=C;
Contains:
RecName: Full=Precursor of protein E3/E2;
AltName: Full=p62;
AltName: Full=pE2;
Contains:
RecName: Full=Assembly protein E3;
Contains:
RecName: Full=Spike glycoprotein E2;
AltName: Full=E2 envelope glycoprotein;
Contains:
RecName: Full=6K protein;
Contains:
RecName: Full=Spike glycoprotein E1;
AltName: Full=E1 envelope glycoprotein;
Salmon pancreas disease virus (SPDV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Togaviridae; Alphavirus.
NCBI_TaxID=84589;
NCBI_TaxID=8030; Salmo salar (Atlantic salmon).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=12021349; DOI=10.1128/JVI.76.12.6155-6163.2002;
Weston J.H., Villoing S., Bremont M., Castric J., Pfeffer M.,
Jewhurst V., McLoughlin M., Rodseth O., Christie K.E., Koumans J.,
Todd D.;
"Comparison of two aquatic alphaviruses, Salmon pancreas disease virus
and Sleeping disease virus, by using genome sequence analysis,
monoclonal reactivity and cross-infection.";
J. Virol. 76:6155-6163(2002).
-!- 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 the spike glycoprotein
E2 at the cell membrane, leading to budding and formation of
mature virions. In case of infection, 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:0000250|UniProtKB:P03315}.
-!- FUNCTION: Assembly protein E3: Provides the signal sequence for
the translocation of the precursor of protein E3/E2 to the host
endoplasmic reticulum. Mediates pH protection of spike
glycoprotein E1 during the transport via the secretory pathway.
{ECO:0000250|UniProtKB:P03315}.
-!- FUNCTION: Spike 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:0000250|UniProtKB:P03315}.
-!- FUNCTION: 6K protein: Constitutive membrane protein involved in
virus glycoprotein processing, cell permeabilization, and the
budding of viral particles. Disrupts the calcium homeostasis of
the cell, probably at the endoplasmic reticulum level. This leads
to cytoplasmic calcium elevation. Because of its lipophilic
properties, the 6K protein is postulated to influence the
selection of lipids that interact with the transmembrane domains
of the glycoproteins, which, in turn, affects the deformability of
the bilayer required for the extreme curvature that occurs as
budding proceeds. Present in low amount in virions, about 3%
compared to viral glycoproteins. {ECO:0000250|UniProtKB:P03315}.
-!- FUNCTION: Spike glycoprotein E1: Class II viral fusion protein.
Fusion activity is inactive as long as E1 is bound to E2 in mature
virion. After virus attachment to target cell and endocytosis,
acidification of the endosome would induce dissociation of E1/E2
heterodimer and concomitant trimerization of the E1 subunits. This
E1 trimer is fusion active, and promotes release of viral
nucleocapsid in cytoplasm after endosome and viral membrane
fusion. Efficient fusion requires the presence of cholesterol and
sphingolipid in the target membrane. Fusion is optimal at levels
of about 1 molecule of cholesterol per 2 molecules of
phospholipids, and is specific for sterols containing a 3-beta-
hydroxyl group. {ECO:0000250|UniProtKB:P03315}.
-!- CATALYTIC ACTIVITY: Autocatalytic release of the core protein from
the N-terminus of the togavirus structural polyprotein by
hydrolysis of a -Trp-|-Ser- bond. {ECO:0000250|UniProtKB:P03316}.
-!- SUBUNIT: Precursor of protein E3/E2: The precursor of protein
E3/E2 and E1 form a heterodimer shortly after synthesis. Spike
glycoprotein E1: The precursor of protein E3/E2 and E1 form a
heterodimer shortly after synthesis. Spike glycoprotein E1:
Processing of the precursor of protein E3/E2 into E2 and E3
results in a heterodimer of the spike glycoproteins E2 and E1.
Spike glycoprotein E2: Processing of the precursor of protein
E3/E2 into E2 and E3 results in a heterodimer of the spike
glycoproteins E2 and E1. Spike glycoprotein E1: Spike at virion
surface are constituted of three E2-E1 heterodimers. Spike
glycoprotein E2: Spike at virion surface are constituted of three
E2-E1 heterodimers. Spike glycoprotein E1: After target cell
attachment and endocytosis, E1 change conformation to form
homotrimers. 6K protein: Interacts with spike glycoprotein E1. 6K
protein: Interacts with spike glycoprotein E2. Spike glycoprotein
E1: Interacts with 6K protein. Spike glycoprotein E2: Interacts
with 6K protein. {ECO:0000250|UniProtKB:P03315,
ECO:0000250|UniProtKB:P03316}.
-!- SUBCELLULAR LOCATION: Capsid protein: Virion
{ECO:0000250|UniProtKB:P03316}. Host cytoplasm
{ECO:0000250|UniProtKB:P03316}. Host cell membrane
{ECO:0000250|UniProtKB:P03316}.
-!- SUBCELLULAR LOCATION: Spike glycoprotein E2: Virion membrane
{ECO:0000250|UniProtKB:Q8JUX5}; Single-pass type I membrane
protein {ECO:0000255}. Host cell membrane
{ECO:0000250|UniProtKB:P03316}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:Q8JUX5}.
-!- SUBCELLULAR LOCATION: 6K protein: Host cell membrane
{ECO:0000250|UniProtKB:P03316}; Multi-pass membrane protein
{ECO:0000255}. Virion membrane {ECO:0000250|UniProtKB:P03316};
Multi-pass membrane protein {ECO:0000255}.
-!- SUBCELLULAR LOCATION: Spike glycoprotein E1: Virion membrane
{ECO:0000250|UniProtKB:Q8JUX5}; Single-pass type I membrane
protein {ECO:0000255}. Host cell membrane
{ECO:0000250|UniProtKB:P03316, ECO:0000250|UniProtKB:Q8JUX5};
Single-pass type I membrane protein {ECO:0000255}.
-!- DOMAIN: Structural polyprotein: As soon as the capsid protein has
been autocleaved, an internal uncleaved signal peptide directs the
remaining polyprotein to the endoplasmic reticulum.
{ECO:0000250|UniProtKB:P03315}.
-!- PTM: Structural polyprotein: Specific enzymatic cleavages in vivo
yield mature proteins. Capsid protein is auto-cleaved during
polyprotein translation, unmasking a signal peptide at the N-
terminus of the precursor of E3/E2. The remaining polyprotein is
then targeted to the host endoplasmic reticulum, where host signal
peptidase cleaves it into pE2, 6K and E1 proteins. pE2 is further
processed to mature E3 and E2 by host furin in trans-Golgi
vesicle. {ECO:0000250|UniProtKB:P03315}.
-!- PTM: Spike glycoprotein E2: Palmitoylated via thioester bonds.
These palmitoylations may induce disruption of the C-terminus
transmembrane. This would result in the reorientation of E2 C-
terminus from lumenal to cytoplasmic side.
{ECO:0000250|UniProtKB:P03315}.
-!- PTM: Spike glycoprotein E1: N-glycosylated.
{ECO:0000250|UniProtKB:P03315}.
-!- PTM: Spike glycoprotein E2: N-glycosylated.
{ECO:0000250|UniProtKB:P03315}.
-!- PTM: Assembly protein E3: N-glycosylated.
{ECO:0000250|UniProtKB:P03315}.
-!- PTM: 6K protein: Palmitoylated via thioester bonds.
{ECO:0000250|UniProtKB:P03315}.
-!- MISCELLANEOUS: Structural polyprotein: Translated from a
subgenomic RNA synthesized during togavirus replication.
{ECO:0000250|UniProtKB:Q86925}.
-----------------------------------------------------------------------
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EMBL; AJ316244; CAC87722.1; -; Genomic_RNA.
RefSeq; NP_647497.1; NC_003930.1.
ProteinModelPortal; Q8JJX0; -.
SMR; Q8JJX0; -.
PRIDE; Q8JJX0; -.
GeneID; 2193532; -.
KEGG; vg:2193532; -.
KO; K19288; -.
OrthoDB; VOG0900008L; -.
Proteomes; UP000007227; 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: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: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.
Gene3D; 2.60.40.350; -; 1.
Gene3D; 2.60.98.10; -; 3.
InterPro; IPR002548; Alpha_E1_glycop.
InterPro; IPR000936; Alpha_E2_glycop.
InterPro; IPR002533; Alpha_E3_glycop.
InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf.
InterPro; IPR036253; Glycoprot_cen/dimer_sf.
InterPro; IPR038055; Glycoprot_E_dimer_dom.
InterPro; IPR014756; Ig_E-set.
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.
SUPFAM; SSF56983; SSF56983; 1.
SUPFAM; SSF81296; SSF81296; 1.
PROSITE; PS51690; ALPHAVIRUS_CP; 1.
3: Inferred from homology;
Capsid protein; 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; Serine protease; T=4 icosahedral capsid protein;
Transmembrane; Transmembrane helix; Viral attachment to host cell;
Viral penetration into host cytoplasm; Virion;
Virus entry into host cell.
CHAIN 1 282 Capsid protein. {ECO:0000250}.
/FTId=PRO_0000238778.
CHAIN 283 791 Precursor of protein E3/E2.
{ECO:0000250}.
/FTId=PRO_0000238779.
CHAIN 283 353 Assembly protein E3. {ECO:0000250}.
/FTId=PRO_0000238780.
CHAIN 354 791 Spike glycoprotein E2. {ECO:0000250}.
/FTId=PRO_0000238781.
CHAIN 792 859 6K protein. {ECO:0000250}.
/FTId=PRO_0000238782.
CHAIN 860 1320 Spike glycoprotein E1. {ECO:0000250}.
/FTId=PRO_0000238783.
TOPO_DOM 1 734 Extracellular. {ECO:0000255}.
TRANSMEM 735 755 Helical. {ECO:0000255}.
TOPO_DOM 756 791 Cytoplasmic. {ECO:0000255}.
TOPO_DOM 792 807 Extracellular. {ECO:0000255}.
TRANSMEM 808 828 Helical. {ECO:0000255}.
TOPO_DOM 829 836 Cytoplasmic. {ECO:0000255}.
TRANSMEM 837 857 Helical. {ECO:0000255}.
TOPO_DOM 858 1286 Extracellular. {ECO:0000255}.
TRANSMEM 1287 1307 Helical. {ECO:0000255}.
TOPO_DOM 1308 1320 Cytoplasmic. {ECO:0000255}.
DOMAIN 134 282 Peptidase S3. {ECO:0000255|PROSITE-
ProRule:PRU01027}.
REGION 103 121 Ribosome-binding. {ECO:0000250}.
REGION 283 302 Functions as an uncleaved signal peptide
for the precursor of protein E3/E2.
{ECO:0000250|UniProtKB:P03315}.
REGION 760 784 Transient transmembrane before p62-6K
protein processing. {ECO:0000255}.
REGION 954 971 E1 fusion peptide loop.
{ECO:0000250|UniProtKB:Q8JUX5}.
ACT_SITE 160 160 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU01027}.
ACT_SITE 182 182 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU01027}.
ACT_SITE 233 233 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU01027}.
SITE 282 283 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:P03315}.
SITE 353 354 Cleavage; by host signal peptidase.
{ECO:0000250}.
SITE 791 792 Cleavage; by host signal peptidase.
{ECO:0000250}.
SITE 859 860 Cleavage; by host signal peptidase.
{ECO:0000250}.
LIPID 784 784 S-palmitoyl cysteine; by host.
{ECO:0000250}.
LIPID 785 785 S-palmitoyl cysteine; by host.
{ECO:0000250}.
LIPID 1310 1310 S-stearoyl cysteine; by host.
{ECO:0000250}.
DISULFID 909 984 {ECO:0000250}.
DISULFID 922 964 {ECO:0000250}.
DISULFID 923 966 {ECO:0000250}.
DISULFID 928 948 {ECO:0000250}.
DISULFID 1134 1146 {ECO:0000250}.
DISULFID 1176 1252 {ECO:0000250}.
DISULFID 1181 1256 {ECO:0000250}.
DISULFID 1203 1246 {ECO:0000250}.
SEQUENCE 1320 AA; 142895 MW; 04C76DEBE9CD4048 CRC64;
MFPMQFTNSA YRQMEPMFAP GSRGQVQPYR PRTKRRQEPQ VGNAAITALA NQMSALQLQV
AGLAGQARVD RRGPRRVQKN KQKKKNSSNG EKPKEKKKKQ KQQEKKGSGG EKVKKTRNRP
GKEVRISVKC ARQSTFPVYH EGAISGYAVL IGSRVFKPAH VKGKIDHPEL ADIKFQVAED
MDLEAAAYPK SMRDQAAEPA TMMDRVYNWE YGTIRVEDNV IIDASGRGKP GDSGRAITDN
SGKVVGIVLG GGPDGRRTRL SVIGFDKKMK AREIAYSDAI PWTRAPALLL LPMVIVCTYN
SNTFDCSKPS CQDCCITAEP EKAMTMLKDN LNDPNYWDLL IAVTTCGSAR RKRAVSTSPA
AFYDTQILAA HAAASPYRAY CPDCDGTACI SPIAIDEVVS SGSDHVLRMR VGSQSGVTAK
GGAAGETSLR YLGRDGKVHA ADNTRLVVRT TAKCDVLQAT GHYILANCPV GQSLTVAATL
DGTRHQCTTV FEHQVTEKFT RERSKGHHLS DMTKKCTRFS TTPKKSALYL VDVYDALPIS
VEISTVVTCS DSQCTVRVPP GTTVKFDKKC KSADSATVTF TSDSQTFTCE EPVLTAASIT
QGKPHLRSAM LPSGGKEVKA RIPFPFPPET ATCRVSVAPL PSITYEESDV LLAGTAKYPV
LLTTRNLGFH SNATSEWIQG KYLRRIPVTP QGIELTWGNN APMHFWSSVR YASGDADAYP
WELLVYHTKH HPEYAWAFVG VACGLLAIAA CMFACACSRV RYSLVANTFN SNPPPLTALT
AALCCIPGAR ADQPYLDIIA YLWTNSKVAF GLQFAAPVAC VLIITYALRH CRLCCKSFLG
VRGWSALLVI LAYVQSCKSY EHTVVVPMDP RAPSYEAVIN RNGYDPLKLT ISVNFTVISP
TTALEYWTCA GVPIVEPPHV GCCTSVSCPS DLSTLHAFTG KAVSDVHCDV HTNVYPLLWG
AAHCFCSTEN TQVSAVAATV SEFCAQDSER AEAFSVHSSS VTAEVLVTLG EVVTAVHVYV
DGVTSARGTD LKIVAGPITT DYSPFDRKVV RIGEEVYNYD WPPYGAGRPG TFGDIQARST
NYVKPNDLYG DIGIEVLQPT NDHVHVAYTY TTSGLLRWLQ DAPKPLSVTA PHGCKISANP
LLALDCGVGA VPMSINIPDA KFTRKLKDPK PSALKCVVDS CEYGVDYGGA ATITYEGHEA
GKCGIHSLTP GVPLRTSVVE VVAGANTVKT TFSSPTPEVA LEVEICSAIV KCAGECTPPK
EHVVATRPRH GSDPGGYISG PAMRWAGGIV GTLVVLFLIL AVIYCVVKKC RSKRIRIVKS


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