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P03316

- POLS_SINDV

UniProt

P03316 - POLS_SINDV

Protein

Structural polyprotein

Gene
N/A
Organism
Sindbis virus (SINV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    Functioni

    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 icosaedric 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 By similarity.By similarity
    E3 protein's function is unknown.By similarity
    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.By similarity
    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.4 Publications
    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.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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei141 – 1411Charge relay systemPROSITE-ProRule annotation
    Active sitei147 – 1471Charge relay systemPROSITE-ProRule annotation
    Active sitei215 – 2151Charge relay systemPROSITE-ProRule annotation
    Sitei264 – 2652Cleavage; by capsid proteinBy similarity
    Sitei328 – 3292Cleavage; by host furinBy similarity
    Sitei751 – 7522Cleavage; by host signal peptidaseBy similarity
    Sitei806 – 8072Cleavage; by host signal peptidaseBy similarity

    GO - Molecular functioni

    1. serine-type endopeptidase activity Source: InterPro
    2. structural molecule activity Source: InterPro

    GO - Biological processi

    1. clathrin-mediated endocytosis of virus by host cell Source: UniProtKB-KW
    2. fusion of virus membrane with host endosome membrane Source: UniProtKB-KW
    3. membrane fusion Source: CACAO
    4. virion attachment to host cell Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Clathrin-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):
    E3/E2
    Alternative name(s):
    Spike glycoprotein E3
    Alternative name(s):
    Spike glycoprotein E2
    Alternative name(s):
    Spike glycoprotein E1
    OrganismiSindbis virus (SINV)
    Taxonomic identifieri11034 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageTogaviridaeAlphavirusWEEV complex
    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]
    ProteomesiUP000006710: Genome

    Subcellular locationi

    Chain Capsid protein : Virion By similarity. Host cytoplasm By similarity

    GO - Cellular componenti

    1. host cell cytoplasm Source: UniProtKB-SubCell
    2. host cell plasma membrane Source: UniProtKB-SubCell
    3. icosahedral viral capsid, spike Source: CACAO
    4. integral component of membrane Source: UniProtKB-KW
    5. T=4 icosahedral viral capsid Source: UniProtKB-KW
    6. viral envelope Source: UniProtKB-KW
    7. 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)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi141 – 1411H → A or P: Complete loss of autocatalytic cleavage by capsid protein. 1 Publication
    Mutagenesisi141 – 1411H → R: No loss of autocatalytic cleavage by capsid protein. No infectious virus is produced. 1 Publication
    Mutagenesisi147 – 1471D → H or Y: No loss of autocatalytic cleavage by capsid protein. No infectious virus is produced. 1 Publication
    Mutagenesisi163 – 1631D → H: No loss of autocatalytic cleavage by capsid protein. No infectious virus is produced. 1 Publication
    Mutagenesisi163 – 1631D → N: No loss of autocatalytic cleavage by capsid protein. Infectious virus is produced. 1 Publication
    Mutagenesisi215 – 2151S → A or I: Complete loss of autocatalytic cleavage by capsid protein. 1 Publication
    Mutagenesisi215 – 2151S → C: 40% reduction in autocatalytic cleavage by capsid protein. No infectious virus is produced. 1 Publication
    Mutagenesisi215 – 2151S → T: 90% reduction in autocatalytic cleavage by capsid protein. No infectious virus is produced. 1 Publication
    Mutagenesisi264 – 2641W → F: 73% loss of cleavage by capsid protease. 1 Publication
    Mutagenesisi724 – 7241C → A: Loss of palmitoylation. 1 Publication
    Mutagenesisi744 – 7452CC → AA: Complete loss of infectivity. 1 Publication
    Mutagenesisi744 – 7441C → A: Loss of palmitoylation. 1 Publication
    Mutagenesisi745 – 7451C → A: Loss of palmitoylation. 1 Publication
    Mutagenesisi786 – 7872CC → SA: Loss of palmitoylation.
    Mutagenesisi790 – 7901C → A: Loss of palmitoylation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 264264Capsid proteinPRO_0000041321Add
    BLAST
    Chaini265 – 751487p62By similarityPRO_0000226238Add
    BLAST
    Chaini265 – 32864E3 proteinPRO_0000041322Add
    BLAST
    Signal peptidei265 – 28016Not cleavedSequence AnalysisAdd
    BLAST
    Chaini329 – 751423E2 envelope glycoproteinPRO_0000041323Add
    BLAST
    Chaini752 – 806556K proteinPRO_0000041324Add
    BLAST
    Chaini807 – 1245439E1 envelope glycoproteinPRO_0000041325Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi278 – 2781N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi524 – 5241N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi646 – 6461N-linked (GlcNAc...); by hostSequence Analysis
    Lipidationi724 – 7241S-palmitoyl cysteine; by host1 Publication
    Lipidationi744 – 7441S-palmitoyl cysteine; by host1 Publication
    Lipidationi745 – 7451S-palmitoyl cysteine; by host1 Publication
    Lipidationi786 – 7861S-palmitoyl cysteine; by host1 Publication
    Lipidationi787 – 7871S-palmitoyl cysteine; by host1 Publication
    Lipidationi790 – 7901S-palmitoyl cysteine; by host1 Publication
    Disulfide bondi855 ↔ 920By similarity
    Disulfide bondi868 ↔ 900By similarity
    Disulfide bondi869 ↔ 902By similarity
    Disulfide bondi874 ↔ 884By similarity
    Glycosylationi945 – 9451N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi1051 – 10511N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi1065 ↔ 1077By similarity
    Disulfide bondi1107 ↔ 1182By similarity
    Disulfide bondi1112 ↔ 1186By similarity
    Disulfide bondi1134 ↔ 1176By similarity

    Post-translational modificationi

    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.By similarity
    E2 and 6K are palmitoylated via thioester bonds.3 Publications

    Keywords - PTMi

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

    Miscellaneous databases

    PMAP-CutDBP03316.

    Interactioni

    Subunit structurei

    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.By similarity

    Protein-protein interaction databases

    DIPiDIP-29032N.

    Structurei

    Secondary structure

    1
    1245
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi114 – 1196
    Turni121 – 1233
    Beta strandi125 – 1328
    Beta strandi135 – 1395
    Beta strandi144 – 1485
    Helixi151 – 1533
    Beta strandi157 – 1593
    Helixi160 – 1623
    Beta strandi164 – 1685
    Helixi171 – 1733
    Beta strandi176 – 1783
    Beta strandi186 – 1916
    Beta strandi194 – 1996
    Beta strandi202 – 2065
    Beta strandi218 – 2203
    Beta strandi222 – 2243
    Beta strandi226 – 23510
    Beta strandi237 – 24711
    Beta strandi249 – 2513
    Beta strandi253 – 2564
    Beta strandi342 – 3454
    Beta strandi347 – 3515
    Beta strandi353 – 3575
    Beta strandi361 – 3633
    Beta strandi367 – 3748
    Beta strandi376 – 3805
    Beta strandi382 – 3854
    Beta strandi391 – 3933
    Beta strandi405 – 4073
    Beta strandi410 – 42516
    Beta strandi428 – 4325
    Beta strandi439 – 4479
    Beta strandi449 – 4546
    Beta strandi464 – 4663
    Beta strandi473 – 48311
    Beta strandi589 – 5968
    Beta strandi603 – 6075
    Beta strandi610 – 63021
    Beta strandi637 – 6437
    Beta strandi654 – 6618
    Beta strandi807 – 8148
    Beta strandi821 – 8255
    Beta strandi833 – 84210
    Beta strandi845 – 85410
    Beta strandi857 – 8604
    Beta strandi883 – 8897
    Turni894 – 8996
    Beta strandi903 – 9053
    Beta strandi907 – 91610
    Turni918 – 9225
    Beta strandi925 – 93410
    Beta strandi937 – 9437
    Beta strandi946 – 9516
    Beta strandi954 – 9574
    Beta strandi959 – 9613
    Beta strandi966 – 9694
    Beta strandi981 – 9855
    Beta strandi990 – 9923
    Beta strandi1003 – 10053
    Beta strandi1008 – 10136
    Turni1014 – 10163
    Helixi1045 – 10506
    Helixi1057 – 10593
    Beta strandi1066 – 10683
    Turni1069 – 10724
    Beta strandi1073 – 10753
    Beta strandi1080 – 108910
    Helixi1090 – 10923
    Beta strandi1102 – 111110
    Beta strandi1116 – 11183
    Beta strandi1120 – 113011
    Beta strandi1137 – 11404
    Beta strandi1144 – 11463
    Beta strandi1148 – 11503
    Beta strandi1157 – 11637

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1KXAX-ray3.10A106-264[»]
    1KXBX-ray2.90A106-264[»]
    1KXCX-ray3.10A106-264[»]
    1KXDX-ray3.00A106-264[»]
    1KXEX-ray3.20A106-264[»]
    1KXFX-ray2.38A1-264[»]
    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/F807-1186[»]
    3MUWelectron microscopy-A/D/E/F807-1190[»]
    U/X/Y/Z329-672[»]
    ProteinModelPortaliP03316.
    SMRiP03316. Positions 106-264, 691-726, 807-1096, 1101-1189, 1215-1245.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP03316.

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei696 – 71217HelicalSequence AnalysisAdd
    BLAST
    Transmembranei728 – 74619HelicalSequence AnalysisAdd
    BLAST
    Transmembranei768 – 78417HelicalSequence AnalysisAdd
    BLAST
    Transmembranei786 – 80217HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1216 – 123419HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini114 – 264151Peptidase S3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni93 – 1019Ribosome-bindingBy similarity

    Sequence similaritiesi

    Contains 1 peptidase S3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Family and domain databases

    Gene3Di2.60.40.350. 1 hit.
    2.60.98.10. 3 hits.
    InterProiIPR002548. Alpha_E1_glycop.
    IPR000936. Alpha_E2_glycop.
    IPR002533. Alpha_E3_glycop.
    IPR000336. Flavivir/Alphavir_Ig-like.
    IPR011998. Glycoprot_cen/dimer.
    IPR013754. GlyE_dim.
    IPR014756. Ig_E-set.
    IPR000930. Peptidase_S3.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view]
    PfamiPF01589. Alpha_E1_glycop. 1 hit.
    PF00943. Alpha_E2_glycop. 1 hit.
    PF01563. Alpha_E3_glycop. 1 hit.
    PF00944. Peptidase_S3. 1 hit.
    [Graphical view]
    PRINTSiPR00798. TOGAVIRIN.
    SUPFAMiSSF50494. SSF50494. 1 hit.
    SSF56983. SSF56983. 1 hit.
    SSF81296. SSF81296. 1 hit.
    PROSITEiPS51690. ALPHAVIRUS_CP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P03316-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNRGFFNMLG RRPFPAPTAM WRPRRRRQAA PMPARNGLAS QIQQLTTAVS     50
    ALVIGQATRP QPPRPRPPPR QKKQAPKQPP KPKKPKTQEK KKKQPAKPKP 100
    GKRQRMALKL EADRLFDVKN EDGDVIGHAL AMEGKVMKPL HVKGTIDHPV 150
    LSKLKFTKSS AYDMEFAQLP VNMRSEAFTY TSEHPEGFYN WHHGAVQYSG 200
    GRFTIPRGVG GRGDSGRPIM DNSGRVVAIV LGGADEGTRT ALSVVTWNSK 250
    GKTIKTTPEG TEEWSAAPLV TAMCLLGNVS FPCDRPPTCY TREPSRALDI 300
    LEENVNHEAY DTLLNAILRC GSSGRSKRSV IDDFTLTSPY LGTCSYCHHT 350
    VPCFSPVKIE QVWDEADDNT IRIQTSAQFG YDQSGAASAN KYRYMSLKQD 400
    HTVKEGTMDD IKISTSGPCR RLSYKGYFLL AKCPPGDSVT VSIVSSNSAT 450
    SCTLARKIKP KFVGREKYDL PPVHGKKIPC TVYDRLKETT AGYITMHRPR 500
    PHAYTSYLEE SSGKVYAKPP SGKNITYECK CGDYKTGTVS TRTEITGCTA 550
    IKQCVAYKSD QTKWVFNSPD LIRHDDHTAQ GKLHLPFKLI PSTCMVPVAH 600
    APNVIHGFKH ISLQLDTDHL TLLTTRRLGA NPEPTTEWIV GKTVRNFTVD 650
    RDGLEYIWGN HEPVRVYAQE SAPGDPHGWP HEIVQHYYHR HPVYTILAVA 700
    SATVAMMIGV TVAVLCACKA RRECLTPYAL APNAVIPTSL ALLCCVRSAN 750
    AETFTETMSY LWSNSQPFFW VQLCIPLAAF IVLMRCCSCC LPFLVVAGAY 800
    LAKVDAYEHA TTVPNVPQIP YKALVERAGY APLNLEITVM SSEVLPSTNQ 850
    EYITCKFTTV VPSPKIKCCG SLECQPAAHA DYTCKVFGGV YPFMWGGAQC 900
    FCDSENSQMS EAYVELSADC ASDHAQAIKV HTAAMKVGLR IVYGNTTSFL 950
    DVYVNGVTPG TSKDLKVIAG PISASFTPFD HKVVIHRGLV YNYDFPEYGA 1000
    MKPGAFGDIQ ATSLTSKDLI ASTDIRLLKP SAKNVHVPYT QASSGFEMWK 1050
    NNSGRPLQET APFGCKIAVN PLRAVDCSYG NIPISIDIPN AAFIRTSDAP 1100
    LVSTVKCEVS ECTYSADFGG MATLQYVSDR EGQCPVHSHS STATLQESTV 1150
    HVLEKGAVTV HFSTASPQAN FIVSLCGKKT TCNAECKPPA DHIVSTPHKN 1200
    DQEFQAAISK TSWSWLFALF GGASSLLIIG LMIFACSMML TSTRR 1245
    Length:1,245
    Mass (Da):136,766
    Last modified:July 21, 1986 - v1
    Checksum:iB77C18131703F1E6
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti329 – 3313SVI → RVT in strain: AR339.
    Natural varianti333 – 3331D → G in strain: HRLP.
    Natural varianti351 – 3511V → E in strain: AR339 and HRLP.
    Natural varianti398 – 3981K → E in strain: AR339.
    Natural varianti442 – 4421S → R Causes attenuation of the virus.
    Natural varianti447 – 4471N → KNGSF in strain: ov-100.
    Natural varianti500 – 5001R → G in strain: AR339.
    Natural varianti719 – 7191K → L in strain: TE12.
    Natural varianti919 – 9191D → V in strain: HRLP.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.

    Genome annotation databases

    GeneIDi1502155.

    Cross-referencesi

    Web resourcesi

    Virus Particle ExploreR db

    Icosahedral capsid structure

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi A03916. VHWVB.
    A25894. VHWVSB.
    B03916. VHWVB2.
    RefSeqi NP_062890.1. NC_001547.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1KXA X-ray 3.10 A 106-264 [» ]
    1KXB X-ray 2.90 A 106-264 [» ]
    1KXC X-ray 3.10 A 106-264 [» ]
    1KXD X-ray 3.00 A 106-264 [» ]
    1KXE X-ray 3.20 A 106-264 [» ]
    1KXF X-ray 2.38 A 1-264 [» ]
    1LD4 electron microscopy 11.40 A/B/C/D 1-264 [» ]
    M/N/O/P 807-1245 [» ]
    1SVP X-ray 2.00 A/B 106-266 [» ]
    1Z8Y electron microscopy 9.00 A/C/E/G 807-1096 [» ]
    B/D/F/H 1101-1189 [» ]
    I/K/M/O 1215-1245 [» ]
    J/L/N/P 691-726 [» ]
    Q/R/S/T 114-264 [» ]
    2SNV X-ray 2.80 A 114-264 [» ]
    2SNW X-ray 2.70 A/B 107-264 [» ]
    3J0F electron microscopy - A/B/C/D 1-264 [» ]
    E/F/G/H 807-1245 [» ]
    I/J/K/L 329-751 [» ]
    3MUU X-ray 3.29 A/B/C/D/E/F 329-672 [» ]
    A/B/C/D/E/F 807-1186 [» ]
    3MUW electron microscopy - A/D/E/F 807-1190 [» ]
    U/X/Y/Z 329-672 [» ]
    ProteinModelPortali P03316.
    SMRi P03316. Positions 106-264, 691-726, 807-1096, 1101-1189, 1215-1245.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-29032N.

    Protein family/group databases

    MEROPSi S03.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 1502155.

    Miscellaneous databases

    EvolutionaryTracei P03316.
    PMAP-CutDB P03316.

    Family and domain databases

    Gene3Di 2.60.40.350. 1 hit.
    2.60.98.10. 3 hits.
    InterProi IPR002548. Alpha_E1_glycop.
    IPR000936. Alpha_E2_glycop.
    IPR002533. Alpha_E3_glycop.
    IPR000336. Flavivir/Alphavir_Ig-like.
    IPR011998. Glycoprot_cen/dimer.
    IPR013754. GlyE_dim.
    IPR014756. Ig_E-set.
    IPR000930. Peptidase_S3.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF01589. Alpha_E1_glycop. 1 hit.
    PF00943. Alpha_E2_glycop. 1 hit.
    PF01563. Alpha_E3_glycop. 1 hit.
    PF00944. Peptidase_S3. 1 hit.
    [Graphical view ]
    PRINTSi PR00798. TOGAVIRIN.
    SUPFAMi SSF50494. SSF50494. 1 hit.
    SSF56983. SSF56983. 1 hit.
    SSF81296. SSF81296. 1 hit.
    PROSITEi PS51690. ALPHAVIRUS_CP. 1 hit.
    [Graphical view ]
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    Publicationsi

    1. "Nucleotide sequence of the 26S mRNA of Sindbis virus and deduced sequence of the encoded virus structural proteins."
      Rice C.M., Strauss J.H.
      Proc. Natl. Acad. Sci. U.S.A. 78:2062-2066(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: HRLP.
    2. "Complete nucleotide sequence of the genomic RNA of Sindbis virus."
      Strauss E.G., Rice C.M., Strauss J.H.
      Virology 133:92-110(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: HRSP.
    3. "A single nucleotide change in the E2 glycoprotein gene of Sindbis virus affects penetration rate in cell culture and virulence in neonatal mice."
      Davis N.L., Fuller F.J., Dougherty W.G., Olmsted R.A., Johnston R.E.
      Proc. Natl. Acad. Sci. U.S.A. 83:6771-6775(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: AR339.
    4. "Sequence analysis of cDNA's derived from the RNA of Sindbis virus, a potential oncolytic virus."
      Saito K., Shirasawa H., Yahata E., Yuan Q.
      Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: ov-100.
    5. "An evolutionary tree relating eight alphaviruses, based on amino-terminal sequences of their glycoproteins."
      Bell J.R., Kinney R.M., Trent D.W., Strauss E.G., Strauss J.H.
      Proc. Natl. Acad. Sci. U.S.A. 81:4702-4706(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 329-394.
      Strain: AR339.
    6. "Site-directed mutagenesis of the proposed catalytic amino acids of the Sindbis virus capsid protein autoprotease."
      Hahn C.S., Strauss J.H.
      J. Virol. 64:3069-3073(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: AUTOCATALYTIC CLEAVAGE BY CAPSID PROTEIN, MUTAGENESIS OF HIS-141; ASP-147; ASP-163 AND SER-215.
    7. "Site-directed mutations in the Sindbis virus 6K protein reveal sites for fatty acylation and the underacylated protein affects virus release and virion structure."
      Gaedigk-Nitschko K., Ding M.X., Levy M.A., Schlesinger M.J.
      Virology 175:282-291(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PALMITOYLATION AT CYS-786; CYS-787 AND CYS-790, MUTAGENESIS OF 786-CYS-CYS-787 AND CYS-790.
    8. "Site-directed mutations in Sindbis virus E2 glycoprotein's cytoplasmic domain and the 6K protein lead to similar defects in virus assembly and budding."
      Gaedigk-Nitschko K., Schlesinger M.J.
      Virology 183:206-214(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PALMITOYLATION AT CYS-724, MUTAGENESIS OF CYS-724.
    9. "Transient translocation of the cytoplasmic (endo) domain of a type I membrane glycoprotein into cellular membranes."
      Liu N., Brown D.T.
      J. Cell Biol. 120:877-883(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: LOCALIZATION OF E2 C-TERMINUS.
    10. "Site-directed mutations in the Sindbis virus E2 glycoprotein identify palmitoylation sites and affect virus budding."
      Ivanova L., Schlesinger M.J.
      J. Virol. 67:2546-2551(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PALMITOYLATION AT CYS-744 AND CYS-745, MUTAGENESIS OF CYS-744 AND CYS-745.
    11. "Structural localization of the E3 glycoprotein in attenuated Sindbis virus mutants."
      Paredes A.M., Heidner H., Thuman-Commike P., Prasad B.V.V., Johnston R.E., Chiu W.
      J. Virol. 72:1534-1541(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF TRP-264.
    12. "Low-pH-dependent fusion of Sindbis virus with receptor-free cholesterol-and sphingolipid-containing liposomes."
      Smit J.M., Bittman R., Wilschut J.
      J. Virol. 73:8476-8484(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF E1.
    13. "The clathrin endocytic pathway in viral infection."
      DeTulleo L., Kirchhausen T.
      EMBO J. 17:4585-4593(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "Interfacial domains in Sindbis virus 6K protein. Detection and functional characterization."
      Sanz M.A., Madan V., Carrasco L., Nieva J.L.
      J. Biol. Chem. 278:2051-2057(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF 6K PROTEIN.
    15. "The alphavirus 6K protein activates endogenous ionic conductances when expressed in Xenopus oocytes."
      Antoine A.F., Montpellier C., Cailliau K., Browaeys-Poly E., Vilain J.P., Dubuisson J.
      J. Membr. Biol. 215:37-48(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. "Structural analysis of Sindbis virus capsid mutants involving assembly and catalysis."
      Choi H.-K., Lee S., Zhang Y.-P., McKinney B.R., Wengler G., Rossmann M.G., Kuhn R.J.
      J. Mol. Biol. 262:151-167(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 107-264.
    17. Erratum
      Choi H.-K., Lee S., Zhang Y.-P., McKinney B.R., Wengler G., Rossmann M.G., Kuhn R.J.
      J. Mol. Biol. 266:633-634(1997)

    Entry informationi

    Entry nameiPOLS_SINDV
    AccessioniPrimary (citable) accession number: P03316
    Secondary accession number(s): C4T9C2
    , P11259, Q88870, Q88871, Q88872, Q88873, Q88874
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 135 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Structural polyprotein is translated from a subgenomic RNA synthesized during togavirus replication.
    The strain HRSP sequence is shown.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3