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Protein

Structural polyprotein

Gene
N/A
Organism
Sindbis virus (SINV)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Capsid protein: Forms an icosahedral capsid with a T=4 symmetry composed of 240 copies of the capsid protein surrounded by a lipid membrane through which penetrate 80 spikes composed of trimers of E1-E2 heterodimers. 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.2 Publications
Assembly protein E3: May be a disulfide isomerase that catalyzes the proper folding and disulfide bond formation in pE2/E2. E3 possesses labile disulfide bonds and is in close proximity to E2 throughout the assembly pathway.1 Publication
Spike glycoprotein E2: Plays an essential role in viral attachment to target host cell, by binding to the cell receptor. Synthesized as a pE2 precursor which is processed by furin at the cell membrane just before virion budding, giving rise to E2-E1 heterodimer. The pE2-E1 heterodimer is stable, whereas E2-E1 is unstable and dissociate at low pH. pE2 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 similarity1 Publication
Protein 6K: Acts as a viroporin that participates in virus glycoprotein processing, cell permeabilization and budding of viral particles. Disrupts the calcium homeostasis of the cell, probably at the endoplasmic reticulum level resulting in the increased levels of cytoplasmic calcium. 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.5 Publications
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.2 Publications

Miscellaneous

Structural polyprotein: Translated from a subgenomic RNA synthesized during togavirus replication.By similarity

Catalytic activityi

Autocatalytic release of the core protein from the N-terminus of the togavirus structural polyprotein by hydrolysis of a -Trp-|-Ser- bond.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei141Charge relay systemPROSITE-ProRule annotation1 Publication1
Active sitei163Charge relay systemPROSITE-ProRule annotation1 Publication1
Active sitei215Charge relay systemPROSITE-ProRule annotation1 Publication1

GO - Molecular functioni

GO - Biological processi

  • clathrin-dependent endocytosis of virus by host cell Source: UniProtKB-KW
  • fusion of virus membrane with host endosome membrane Source: UniProtKB-KW
  • membrane fusion Source: CACAO
  • virion attachment to host cell Source: CACAO

Keywordsi

Molecular functionHydrolase, Protease, Serine protease
Biological processClathrin-mediated endocytosis of virus by host, Fusion of virus membrane with host endosomal membrane, Fusion of virus membrane with host membrane, Host-virus interaction, Viral attachment to host cell, Viral penetration into host cytoplasm, Virus endocytosis by host, Virus entry into host cell

Protein family/group databases

MEROPSiS03.001

Names & Taxonomyi

Protein namesi
Recommended name:
Structural polyprotein
Alternative name(s):
p130
Cleaved into the following 6 chains:
Alternative name(s):
Coat protein
Short name:
C
Alternative name(s):
p62
pE2
Alternative name(s):
E2 envelope glycoprotein
Alternative name(s):
E1 envelope glycoprotein
OrganismiSindbis virus (SINV)
Taxonomic identifieri11034 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageTogaviridaeAlphavirus
Virus hostiAcrocephalus scirpaceus (Eurasian reed-warbler) [TaxID: 48156]
Aedes [TaxID: 7158]
Culex [TaxID: 53527]
Homo sapiens (Human) [TaxID: 9606]
Motacilla alba (White wagtail) (Pied wagtail) [TaxID: 45807]
Streptopelia turtur [TaxID: 177155]
Proteomesi
  • UP000006710 Componenti: Genome

Subcellular locationi

Capsid protein :
  • Virion 1 Publication
  • Host cytoplasm 1 Publication
  • Host cell membrane 1 Publication
Precursor of protein E3/E2 :
Spike glycoprotein E2 :
  • Virion membrane 1 Publication; Single-pass type I membrane protein Sequence analysis
  • Host cell membrane 2 Publications; Single-pass type I membrane protein Sequence analysis
6K protein :
Spike glycoprotein E1 :
  • Virion membrane 1 Publication; Single-pass type I membrane protein Sequence analysis
  • Host cell membrane 2 Publications; Single-pass type I membrane protein Sequence analysis

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei696 – 716HelicalSequence analysisAdd BLAST21
Transmembranei726 – 746HelicalSequence analysisAdd BLAST21
Transmembranei777 – 797HelicalSequence analysisAdd BLAST21
Transmembranei1215 – 1235HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

  • host cell cytoplasm Source: UniProtKB-SubCell
  • host cell plasma membrane Source: CACAO
  • icosahedral viral capsid, spike Source: CACAO
  • integral component of membrane Source: UniProtKB-KW
  • T=4 icosahedral viral capsid Source: UniProtKB-KW
  • viral envelope Source: UniProtKB-KW
  • virion membrane Source: UniProtKB-SubCell

Keywords - Cellular componenti

Capsid protein, Host cell membrane, Host cytoplasm, Host membrane, Membrane, T=4 icosahedral capsid protein, Viral envelope protein, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi141H → A or P: Complete loss of autocatalytic cleavage by capsid protein. 1 Publication1
Mutagenesisi141H → R: No loss of autocatalytic cleavage by capsid protein. No infectious virus is produced. 1 Publication1
Mutagenesisi147D → H or Y: No loss of autocatalytic cleavage by capsid protein. No infectious virus is produced. 1 Publication1
Mutagenesisi163D → H: No loss of autocatalytic cleavage by capsid protein. No infectious virus is produced. 1 Publication1
Mutagenesisi163D → N: No loss of autocatalytic cleavage by capsid protein. Infectious virus is produced. 1 Publication1
Mutagenesisi215S → A or I: Complete loss of autocatalytic cleavage by capsid protein. 1 Publication1
Mutagenesisi215S → C: 40% reduction in autocatalytic cleavage by capsid protein. No infectious virus is produced. 1 Publication1
Mutagenesisi215S → T: 90% reduction in autocatalytic cleavage by capsid protein. No infectious virus is produced. 1 Publication1
Mutagenesisi264W → F: 73% loss of cleavage by capsid protease. 1 Publication1
Mutagenesisi724C → A: Loss of palmitoylation. 1 Publication1
Mutagenesisi744 – 745CC → AA: Complete loss of infectivity. 2
Mutagenesisi744C → A: Loss of palmitoylation. 1 Publication1
Mutagenesisi745C → A: Loss of palmitoylation. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000413211 – 264Capsid proteinAdd BLAST264
ChainiPRO_0000226238265 – 751Precursor of protein E3/E2By similarityAdd BLAST487
ChainiPRO_0000041322265 – 328Assembly protein E3Add BLAST64
ChainiPRO_0000041323329 – 751Spike glycoprotein E2Add BLAST423
ChainiPRO_0000041324752 – 8066K proteinAdd BLAST55
ChainiPRO_0000041325807 – 1245Spike glycoprotein E1Add BLAST439

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi278N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi283 ↔ 2891 Publication
Glycosylationi524N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi646N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Lipidationi724S-palmitoyl cysteine; by host1 Publication1
Lipidationi744S-palmitoyl cysteine; by host1 Publication1
Lipidationi745S-palmitoyl cysteine; by host1 Publication1
Disulfide bondi855 ↔ 920By similarity
Disulfide bondi868 ↔ 900By similarity
Disulfide bondi869 ↔ 902By similarity
Disulfide bondi874 ↔ 884By similarity
Glycosylationi945N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi1051N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi1065 ↔ 1077By similarity
Disulfide bondi1107 ↔ 1182By similarity
Disulfide bondi1112 ↔ 1186By similarity
Disulfide bondi1134 ↔ 1176By similarity

Post-translational modificationi

Structural polyprotein: Specific enzymatic cleavages in vivo yield mature proteins (By similarity). Capsid protein is auto-cleaved during polyprotein translation, unmasking a signal peptide at the N-terminus of the precursor of E3/E2 (PubMed:2335827). The remaining polyprotein is then targeted to the host endoplasmic reticulum, where host signal peptidase cleaves it into pE2, 6K and E1 proteins (By similarity). pE2 is further processed to mature E3 and E2 by host furin in trans-Golgi vesicle (By similarity).By similarity1 Publication
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.2 Publications
Spike glycoprotein E1: N-glycosylated.By similarity
Spike glycoprotein E2: N-glycosylated.By similarity
Assembly protein E3: N-glycosylated.By similarity
6K protein: Palmitoylated via thioester bonds.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei264 – 265Cleavage; by autolysisBy similarity2
Sitei328 – 329Cleavage; by host furinBy similarity2
Sitei751 – 752Cleavage; by host signal peptidaseBy similarity2
Sitei806 – 807Cleavage; by host signal peptidaseBy similarity2

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

PTM databases

SwissPalmiP03316

Miscellaneous databases

PMAP-CutDBiP03316

Interactioni

Subunit structurei

Precursor of protein E3/E2: The precursor of protein E3/E2 and E1 form a heterodimer shortly after synthesis (PubMed:8623521). Spike glycoprotein E1: The precursor of protein E3/E2 and E1 form a heterodimer shortly after synthesis (PubMed:8623521). 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 (PubMed:8623521). 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 (PubMed:8623521). Spike glycoprotein E1: Spike at virion surface are constituted of three E2-E1 heterodimers (PubMed:8623521). Spike glycoprotein E2: Spike at virion surface are constituted of three E2-E1 heterodimers (PubMed:8623521). Spike glycoprotein E1: After target cell attachment and endocytosis, E1 change conformation to form homotrimers (By similarity). 6K protein: Interacts with spike glycoprotein E1 (PubMed:8892914). 6K protein: Interacts with spike glycoprotein E2 (PubMed:8892914). Spike glycoprotein E1: Interacts with 6K protein (PubMed:8892914). Spike glycoprotein E2: Interacts with 6K protein (PubMed:8892914).By similarity2 Publications

GO - Molecular functioni

  • ubiquitin-like protein ligase binding Source: ParkinsonsUK-UCL

Protein-protein interaction databases

DIPiDIP-29032N

Structurei

Secondary structure

11245
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi114 – 119Combined sources6
Turni121 – 123Combined sources3
Beta strandi125 – 132Combined sources8
Beta strandi135 – 139Combined sources5
Beta strandi144 – 148Combined sources5
Helixi151 – 153Combined sources3
Beta strandi157 – 159Combined sources3
Helixi160 – 162Combined sources3
Beta strandi164 – 168Combined sources5
Helixi171 – 173Combined sources3
Beta strandi176 – 178Combined sources3
Beta strandi186 – 191Combined sources6
Beta strandi194 – 199Combined sources6
Beta strandi202 – 206Combined sources5
Beta strandi218 – 220Combined sources3
Beta strandi222 – 224Combined sources3
Beta strandi226 – 235Combined sources10
Beta strandi237 – 247Combined sources11
Beta strandi249 – 251Combined sources3
Beta strandi253 – 256Combined sources4
Beta strandi342 – 345Combined sources4
Beta strandi347 – 351Combined sources5
Beta strandi353 – 357Combined sources5
Beta strandi361 – 363Combined sources3
Beta strandi367 – 374Combined sources8
Beta strandi376 – 380Combined sources5
Beta strandi382 – 385Combined sources4
Beta strandi391 – 393Combined sources3
Beta strandi405 – 407Combined sources3
Beta strandi410 – 425Combined sources16
Beta strandi428 – 432Combined sources5
Beta strandi439 – 447Combined sources9
Beta strandi449 – 454Combined sources6
Beta strandi464 – 466Combined sources3
Beta strandi473 – 483Combined sources11
Beta strandi589 – 596Combined sources8
Beta strandi603 – 607Combined sources5
Beta strandi610 – 630Combined sources21
Beta strandi637 – 643Combined sources7
Beta strandi654 – 661Combined sources8
Beta strandi807 – 814Combined sources8
Beta strandi821 – 825Combined sources5
Beta strandi833 – 842Combined sources10
Beta strandi845 – 854Combined sources10
Beta strandi857 – 860Combined sources4
Beta strandi883 – 889Combined sources7
Turni894 – 899Combined sources6
Beta strandi903 – 905Combined sources3
Beta strandi907 – 916Combined sources10
Turni918 – 922Combined sources5
Beta strandi925 – 934Combined sources10
Beta strandi937 – 943Combined sources7
Beta strandi946 – 951Combined sources6
Beta strandi954 – 957Combined sources4
Beta strandi959 – 961Combined sources3
Beta strandi966 – 969Combined sources4
Beta strandi981 – 985Combined sources5
Beta strandi990 – 992Combined sources3
Beta strandi1003 – 1005Combined sources3
Beta strandi1008 – 1013Combined sources6
Turni1014 – 1016Combined sources3
Helixi1045 – 1050Combined sources6
Helixi1057 – 1059Combined sources3
Beta strandi1066 – 1068Combined sources3
Turni1069 – 1072Combined sources4
Beta strandi1073 – 1075Combined sources3
Beta strandi1080 – 1089Combined sources10
Helixi1090 – 1092Combined sources3
Beta strandi1102 – 1111Combined sources10
Beta strandi1116 – 1118Combined sources3
Beta strandi1120 – 1130Combined sources11
Beta strandi1137 – 1140Combined sources4
Beta strandi1144 – 1146Combined sources3
Beta strandi1148 – 1150Combined sources3
Beta strandi1157 – 1163Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KXAX-ray3.10A106-264[»]
1KXBX-ray2.90A106-264[»]
1KXCX-ray3.10A106-264[»]
1KXDX-ray3.00A106-264[»]
1KXEX-ray3.20A106-264[»]
1KXFX-ray2.38A106-264[»]
1LD4electron microscopy11.40A/B/C/D1-264[»]
M/N/O/P807-1245[»]
1SVPX-ray2.00A/B106-266[»]
1Z8Yelectron microscopy9.00A/C/E/G807-1096[»]
B/D/F/H1101-1189[»]
I/K/M/O1215-1245[»]
J/L/N/P691-726[»]
Q/R/S/T114-264[»]
2SNVX-ray2.80A114-264[»]
2SNWX-ray2.70A/B107-264[»]
3J0Felectron microscopy-A/B/C/D1-264[»]
E/F/G/H807-1245[»]
I/J/K/L329-751[»]
3MUUX-ray3.29A/B/C/D/E/F329-672[»]
A/B/C/D/E/F807-1192[»]
3MUWelectron microscopy-A/D/E/F807-1190[»]
U/X/Y/Z329-672[»]
ProteinModelPortaliP03316
SMRiP03316
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03316

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini114 – 264Peptidase S3PROSITE-ProRule annotationAdd BLAST151

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni93 – 101Ribosome-bindingBy similarity9
Regioni265 – 279Functions as an uncleaved signal peptide for the precursor of protein E3/E2By similarityAdd BLAST15
Regioni890 – 907E1 fusion peptide loopBy similarityAdd BLAST18

Domaini

Structural polyprotein: As soon as the capsid protein has been autocleaved, an internal uncleaved signal peptide directs the remaining polyprotein to the endoplasmic reticulum.By similarity

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

KOiK19288
OrthoDBiVOG0900007W

Family and domain databases

Gene3Di2.60.40.350, 1 hit
2.60.98.10, 3 hits
InterProiView protein in InterPro
IPR002548 Alpha_E1_glycop
IPR000936 Alpha_E2_glycop
IPR002533 Alpha_E3_glycop
IPR000336 Flavivir/Alphavir_Ig-like_sf
IPR036253 Glycoprot_cen/dimer_sf
IPR038055 Glycoprot_E_dimer_dom
IPR014756 Ig_E-set
IPR009003 Peptidase_S1_PA
IPR000930 Peptidase_S3
PfamiView protein in Pfam
PF01589 Alpha_E1_glycop, 1 hit
PF00943 Alpha_E2_glycop, 1 hit
PF01563 Alpha_E3_glycop, 1 hit
PF00944 Peptidase_S3, 1 hit
PRINTSiPR00798 TOGAVIRIN
SUPFAMiSSF50494 SSF50494, 1 hit
SSF56983 SSF56983, 1 hit
SSF81296 SSF81296, 1 hit
PROSITEiView protein in PROSITE
PS51690 ALPHAVIRUS_CP, 1 hit

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by ribosomal frameshifting. AlignAdd to basket

Isoform Structural polyprotein (identifier: P03316-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MNRGFFNMLG RRPFPAPTAM WRPRRRRQAA PMPARNGLAS QIQQLTTAVS
60 70 80 90 100
ALVIGQATRP QPPRPRPPPR QKKQAPKQPP KPKKPKTQEK KKKQPAKPKP
110 120 130 140 150
GKRQRMALKL EADRLFDVKN EDGDVIGHAL AMEGKVMKPL HVKGTIDHPV
160 170 180 190 200
LSKLKFTKSS AYDMEFAQLP VNMRSEAFTY TSEHPEGFYN WHHGAVQYSG
210 220 230 240 250
GRFTIPRGVG GRGDSGRPIM DNSGRVVAIV LGGADEGTRT ALSVVTWNSK
260 270 280 290 300
GKTIKTTPEG TEEWSAAPLV TAMCLLGNVS FPCDRPPTCY TREPSRALDI
310 320 330 340 350
LEENVNHEAY DTLLNAILRC GSSGRSKRSV IDDFTLTSPY LGTCSYCHHT
360 370 380 390 400
VPCFSPVKIE QVWDEADDNT IRIQTSAQFG YDQSGAASAN KYRYMSLKQD
410 420 430 440 450
HTVKEGTMDD IKISTSGPCR RLSYKGYFLL AKCPPGDSVT VSIVSSNSAT
460 470 480 490 500
SCTLARKIKP KFVGREKYDL PPVHGKKIPC TVYDRLKETT AGYITMHRPR
510 520 530 540 550
PHAYTSYLEE SSGKVYAKPP SGKNITYECK CGDYKTGTVS TRTEITGCTA
560 570 580 590 600
IKQCVAYKSD QTKWVFNSPD LIRHDDHTAQ GKLHLPFKLI PSTCMVPVAH
610 620 630 640 650
APNVIHGFKH ISLQLDTDHL TLLTTRRLGA NPEPTTEWIV GKTVRNFTVD
660 670 680 690 700
RDGLEYIWGN HEPVRVYAQE SAPGDPHGWP HEIVQHYYHR HPVYTILAVA
710 720 730 740 750
SATVAMMIGV TVAVLCACKA RRECLTPYAL APNAVIPTSL ALLCCVRSAN
760 770 780 790 800
AETFTETMSY LWSNSQPFFW VQLCIPLAAF IVLMRCCSCC LPFLVVAGAY
810 820 830 840 850
LAKVDAYEHA TTVPNVPQIP YKALVERAGY APLNLEITVM SSEVLPSTNQ
860 870 880 890 900
EYITCKFTTV VPSPKIKCCG SLECQPAAHA DYTCKVFGGV YPFMWGGAQC
910 920 930 940 950
FCDSENSQMS EAYVELSADC ASDHAQAIKV HTAAMKVGLR IVYGNTTSFL
960 970 980 990 1000
DVYVNGVTPG TSKDLKVIAG PISASFTPFD HKVVIHRGLV YNYDFPEYGA
1010 1020 1030 1040 1050
MKPGAFGDIQ ATSLTSKDLI ASTDIRLLKP SAKNVHVPYT QASSGFEMWK
1060 1070 1080 1090 1100
NNSGRPLQET APFGCKIAVN PLRAVDCSYG NIPISIDIPN AAFIRTSDAP
1110 1120 1130 1140 1150
LVSTVKCEVS ECTYSADFGG MATLQYVSDR EGQCPVHSHS STATLQESTV
1160 1170 1180 1190 1200
HVLEKGAVTV HFSTASPQAN FIVSLCGKKT TCNAECKPPA DHIVSTPHKN
1210 1220 1230 1240
DQEFQAAISK TSWSWLFALF GGASSLLIIG LMIFACSMML TSTRR
Note: Produced by conventional translation.
Length:1,245
Mass (Da):136,766
Last modified:July 21, 1986 - v1
Checksum:iB77C18131703F1E6
GO
Isoform Frameshifted structural polyprotein (identifier: P0DOK0-1) [UniParc]FASTAAdd to basket
The sequence of this isoform can be found in the external entry P0DOK0.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Produced by ribosomal frameshifting.
Length:821
Mass (Da):91,215
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti329 – 331SVI → RVT in strain: AR339. 3
Natural varianti333D → G in strain: HRLP. 1
Natural varianti351V → E in strain: AR339 and HRLP. 1
Natural varianti398K → E in strain: AR339. 1
Natural varianti442S → R Causes attenuation of the virus. 1
Natural varianti447N → KNGSF in strain: ov-100. 1
Natural varianti500R → G in strain: AR339. 1
Natural varianti719K → L in strain: TE12. 1
Natural varianti919D → V in strain: HRLP. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01403 Genomic RNA Translation: CAA24684.1
J02363 Genomic RNA Translation: AAA96976.1
M13818 Genomic RNA Translation: AAA47485.1
AB372876 Genomic RNA Translation: BAH70330.1
PIRiA03916 VHWVB
A25894 VHWVSB
B03916 VHWVB2
RefSeqiNP_062890.1, NC_001547.1 [P03316-1]

Genome annotation databases

GeneIDi1502155
KEGGivg:1502155

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Similar proteinsi

Entry informationi

Entry nameiPOLS_SINDV
AccessioniPrimary (citable) accession number: P03316
Secondary accession number(s): C4T9C2
, P11259, Q88870, Q88871, Q88872, Q88873, Q88874
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 25, 2018
This is version 159 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health