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P03316

- POLS_SINDV

UniProt

P03316 - POLS_SINDV

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Protein

Structural polyprotein

Gene
N/A
Organism
Sindbis virus (SINV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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

Topology

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

GO - Cellular componenti

  1. host cell cytoplasm Source: UniProtKB-KW
  2. host cell plasma membrane Source: UniProtKB-KW
  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: InterPro
Complete GO annotation...

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.
Mutagenesisi744 – 7441C → A: Loss of palmitoylation. 1 Publication
Mutagenesisi745 – 7451C → A: Loss of palmitoylation. 1 Publication
Mutagenesisi786 – 7872CC → SA: Loss of palmitoylation. 1 Publication
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 – 1196Combined sources
Turni121 – 1233Combined sources
Beta strandi125 – 1328Combined sources
Beta strandi135 – 1395Combined sources
Beta strandi144 – 1485Combined sources
Helixi151 – 1533Combined sources
Beta strandi157 – 1593Combined sources
Helixi160 – 1623Combined sources
Beta strandi164 – 1685Combined sources
Helixi171 – 1733Combined sources
Beta strandi176 – 1783Combined sources
Beta strandi186 – 1916Combined sources
Beta strandi194 – 1996Combined sources
Beta strandi202 – 2065Combined sources
Beta strandi218 – 2203Combined sources
Beta strandi222 – 2243Combined sources
Beta strandi226 – 23510Combined sources
Beta strandi237 – 24711Combined sources
Beta strandi249 – 2513Combined sources
Beta strandi253 – 2564Combined sources
Beta strandi342 – 3454Combined sources
Beta strandi347 – 3515Combined sources
Beta strandi353 – 3575Combined sources
Beta strandi361 – 3633Combined sources
Beta strandi367 – 3748Combined sources
Beta strandi376 – 3805Combined sources
Beta strandi382 – 3854Combined sources
Beta strandi391 – 3933Combined sources
Beta strandi405 – 4073Combined sources
Beta strandi410 – 42516Combined sources
Beta strandi428 – 4325Combined sources
Beta strandi439 – 4479Combined sources
Beta strandi449 – 4546Combined sources
Beta strandi464 – 4663Combined sources
Beta strandi473 – 48311Combined sources
Beta strandi589 – 5968Combined sources
Beta strandi603 – 6075Combined sources
Beta strandi610 – 63021Combined sources
Beta strandi637 – 6437Combined sources
Beta strandi654 – 6618Combined sources
Beta strandi807 – 8148Combined sources
Beta strandi821 – 8255Combined sources
Beta strandi833 – 84210Combined sources
Beta strandi845 – 85410Combined sources
Beta strandi857 – 8604Combined sources
Beta strandi883 – 8897Combined sources
Turni894 – 8996Combined sources
Beta strandi903 – 9053Combined sources
Beta strandi907 – 91610Combined sources
Turni918 – 9225Combined sources
Beta strandi925 – 93410Combined sources
Beta strandi937 – 9437Combined sources
Beta strandi946 – 9516Combined sources
Beta strandi954 – 9574Combined sources
Beta strandi959 – 9613Combined sources
Beta strandi966 – 9694Combined sources
Beta strandi981 – 9855Combined sources
Beta strandi990 – 9923Combined sources
Beta strandi1003 – 10053Combined sources
Beta strandi1008 – 10136Combined sources
Turni1014 – 10163Combined sources
Helixi1045 – 10506Combined sources
Helixi1057 – 10593Combined sources
Beta strandi1066 – 10683Combined sources
Turni1069 – 10724Combined sources
Beta strandi1073 – 10753Combined sources
Beta strandi1080 – 108910Combined sources
Helixi1090 – 10923Combined sources
Beta strandi1102 – 111110Combined sources
Beta strandi1116 – 11183Combined sources
Beta strandi1120 – 113011Combined sources
Beta strandi1137 – 11404Combined sources
Beta strandi1144 – 11463Combined sources
Beta strandi1148 – 11503Combined sources
Beta strandi1157 – 11637Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.

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

        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
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:
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.

Genome annotation databases

GeneIDi1502155.

Cross-referencesi

Web resourcesi

Virus Particle ExploreR db

Icosahedral capsid structure

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 .
PIRi A03916. VHWVB.
A25894. VHWVSB.
B03916. VHWVB2.
RefSeqi NP_062890.1. NC_001547.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 137 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