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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.
22-NOV-2017, entry version 94.
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=p62;
AltName: Full=E3/E2;
Contains:
RecName: Full=E3 protein;
AltName: Full=Spike glycoprotein E3;
Contains:
RecName: Full=E2 envelope glycoprotein;
AltName: Full=Spike glycoprotein E2;
Contains:
RecName: Full=6K protein;
Contains:
RecName: Full=E1 envelope glycoprotein;
AltName: Full=Spike glycoprotein E1;
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 E2 at the cell membrane,
leading to budding and formation of mature virions. New virions
attach to target cells, and after endocytosis their membrane fuses
with the target cell 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
(By similarity). {ECO:0000250}.
-!- FUNCTION: E3 protein's function is unknown. {ECO:0000250}.
-!- FUNCTION: E2 is responsible for 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 (By
similarity). {ECO:0000250}.
-!- FUNCTION: 6K is a 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 (By similarity). {ECO:0000250}.
-!- FUNCTION: E1 is a 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 (By similarity). {ECO:0000250}.
-!- 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 (By similarity).
{ECO:0000250}.
-!- 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: E2 envelope glycoprotein: 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: E1 envelope glycoprotein: 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: 6K protein: Host cell membrane
{ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Virion
membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
-!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
Capsid protein is auto-cleaved during polyprotein translation,
unmasking p62 signal peptide. The remaining polyprotein is then
targeted to the endoplasmic reticulum, where host signal peptidase
cleaves it into p62, 6K and E1 proteins. p62 is further processed
to mature E3 and E2 by host furin in trans-Golgi vesicle (By
similarity). {ECO:0000250}.
-!- PTM: E2 and 6K are palmitoylated via thioester bonds.
-!- MISCELLANEOUS: Structural polyprotein is translated from a
subgenomic RNA synthesized during togaviruses replication.
-----------------------------------------------------------------------
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EMBL; AJ316244; CAC87722.1; -; Genomic_RNA.
RefSeq; NP_647497.1; NC_003930.1.
ProteinModelPortal; Q8JJX0; -.
SMR; 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.
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; 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; Signal; 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 p62. {ECO:0000250}.
/FTId=PRO_0000238779.
CHAIN 283 353 E3 protein. {ECO:0000250}.
/FTId=PRO_0000238780.
SIGNAL 283 298 Not cleaved. {ECO:0000255}.
CHAIN 354 791 E2 envelope glycoprotein. {ECO:0000250}.
/FTId=PRO_0000238781.
CHAIN 792 859 6K protein. {ECO:0000250}.
/FTId=PRO_0000238782.
CHAIN 860 1320 E1 envelope glycoprotein. {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 858 859 Extracellular. {ECO:0000255}.
TOPO_DOM 860 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 760 784 Transient transmembrane before p62-6K
protein processing. {ECO:0000255}.
REGION 954 971 E1 fusion peptide loop. {ECO:0000250}.
ACT_SITE 160 160 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU01027}.
ACT_SITE 166 166 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 capsid protein.
{ECO:0000250}.
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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