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P03316 (POLS_SINDV) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Structural polyprotein
Alternative name(s):
p130

Cleaved into the following 6 chains:

  1. Capsid protein
    EC=3.4.21.90
    Alternative name(s):
    Coat protein
    Short name=C
  2. p62
    Alternative name(s):
    E3/E2
  3. E3 protein
    Alternative name(s):
    Spike glycoprotein E3
  4. E2 envelope glycoprotein
    Alternative name(s):
    Spike glycoprotein E2
  5. 6K protein
  6. E1 envelope glycoprotein
    Alternative name(s):
    Spike glycoprotein E1
OrganismSindbis virus (SINV) [Reference proteome]
Taxonomic identifier11034 [NCBI]
Taxonomic lineageViruses › ssRNA positive-strand viruses, no DNA stage › Togaviridae › Alphavirus › WEEV complex
Virus hostAcrocephalus scirpaceus [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]

Protein attributes

Sequence length1245 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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 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. Ref.12 Ref.13 Ref.14 Ref.15

E3 protein's function is unknown By similarity. Ref.12 Ref.13 Ref.14 Ref.15

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. Ref.12 Ref.13 Ref.14 Ref.15

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. Ref.12 Ref.13 Ref.14 Ref.15

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. Ref.12 Ref.13 Ref.14 Ref.15

Catalytic activity

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

Subunit structure

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.

Subcellular location

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

p62: Virion membrane; Single-pass type I membrane protein By similarity. Host cell membrane; Single-pass type I membrane protein By similarity.

E2 envelope glycoprotein: Virion membrane; Single-pass type I membrane protein By similarity. Host cell membrane; Single-pass type I membrane protein By similarity.

E1 envelope glycoprotein: Virion membrane; Single-pass type I membrane protein By similarity. Host cell membrane; Single-pass type I membrane protein By similarity.

6K protein: Host cell membrane; Multi-pass membrane protein By similarity. Virion membrane; Multi-pass membrane protein By similarity.

Post-translational modification

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. Ref.6

E2 and 6K are palmitoylated via thioester bonds. Ref.7 Ref.8 Ref.10

Miscellaneous

Structural polyprotein is translated from a subgenomic RNA synthesized during togavirus replication.

The strain HRSP sequence is shown.

Sequence similarities

Contains 1 peptidase S3 domain.

Ontologies

Keywords
   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
   Cellular componentHost cell membrane
Host cytoplasm
Host membrane
Membrane
Viral envelope protein
Virion
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionCapsid protein
Hydrolase
Protease
Serine protease
T=4 icosahedral capsid protein
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Lipoprotein
Palmitate
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

viral attachment to host cell

Inferred from electronic annotation. Source: UniProtKB-KW

viral entry into host cell via clathrin-mediated endocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentT=4 icosahedral viral capsid

Inferred from electronic annotation. Source: UniProtKB-KW

host cell cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

host cell plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

viral envelope

Inferred from electronic annotation. Source: UniProtKB-KW

virion membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionserine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

structural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 264264Capsid protein
PRO_0000041321
Chain265 – 751487p62 By similarity
PRO_0000226238
Chain265 – 32864E3 protein
PRO_0000041322
Signal peptide265 – 28016Not cleaved Potential
Chain329 – 751423E2 envelope glycoprotein
PRO_0000041323
Chain752 – 806556K protein
PRO_0000041324
Chain807 – 1245439E1 envelope glycoprotein
PRO_0000041325

Regions

Transmembrane696 – 71217Helical; Potential
Transmembrane728 – 74619Helical; Potential
Transmembrane768 – 78417Helical; Potential
Transmembrane786 – 80217Helical; Potential
Transmembrane1216 – 123419Helical; Potential
Domain107 – 264158Peptidase S3
Region93 – 1019Ribosome-binding By similarity

Sites

Active site1411Charge relay system By similarity
Active site1471Charge relay system By similarity
Active site2151Charge relay system By similarity
Site264 – 2652Cleavage; by capsid protein By similarity
Site328 – 3292Cleavage; by host furin By similarity
Site751 – 7522Cleavage; by host signal peptidase By similarity
Site806 – 8072Cleavage; by host signal peptidase By similarity

Amino acid modifications

Lipidation7241S-palmitoyl cysteine; by host Ref.8
Lipidation7441S-palmitoyl cysteine; by host Ref.10
Lipidation7451S-palmitoyl cysteine; by host Ref.10
Lipidation7861S-palmitoyl cysteine; by host Ref.7
Lipidation7871S-palmitoyl cysteine; by host Ref.7
Lipidation7901S-palmitoyl cysteine; by host Ref.7
Glycosylation2781N-linked (GlcNAc...); by host Potential
Glycosylation5241N-linked (GlcNAc...); by host Potential
Glycosylation6461N-linked (GlcNAc...); by host Potential
Glycosylation9451N-linked (GlcNAc...); by host Potential
Glycosylation10511N-linked (GlcNAc...); by host Potential
Disulfide bond855 ↔ 920 By similarity
Disulfide bond868 ↔ 900 By similarity
Disulfide bond869 ↔ 902 By similarity
Disulfide bond874 ↔ 884 By similarity
Disulfide bond1065 ↔ 1077 By similarity
Disulfide bond1107 ↔ 1182 By similarity
Disulfide bond1112 ↔ 1186 By similarity
Disulfide bond1134 ↔ 1176 By similarity

Natural variations

Natural variant329 – 3313SVI → RVT in strain: AR339.
Natural variant3331D → G in strain: HRLP.
Natural variant3511V → E in strain: AR339 and HRLP.
Natural variant3981K → E in strain: AR339.
Natural variant4421S → R Causes attenuation of the virus.
Natural variant4471N → KNGSF in strain: ov-100.
Natural variant5001R → G in strain: AR339.
Natural variant7191K → L in strain: TE12.
Natural variant9191D → V in strain: HRLP.

Experimental info

Mutagenesis1411H → A or P: Complete loss of autocatalytic cleavage by capsid protein. Ref.6
Mutagenesis1411H → R: No loss of autocatalytic cleavage by capsid protein. No infectious virus is produced. Ref.6
Mutagenesis1471D → H or Y: No loss of autocatalytic cleavage by capsid protein. No infectious virus is produced. Ref.6
Mutagenesis1631D → H: No loss of autocatalytic cleavage by capsid protein. No infectious virus is produced. Ref.6
Mutagenesis1631D → N: No loss of autocatalytic cleavage by capsid protein. Infectious virus is produced. Ref.6
Mutagenesis2151S → A or I: Complete loss of autocatalytic cleavage by capsid protein. Ref.6
Mutagenesis2151S → C: 40% reduction in autocatalytic cleavage by capsid protein. No infectious virus is produced. Ref.6
Mutagenesis2151S → T: 90% reduction in autocatalytic cleavage by capsid protein. No infectious virus is produced. Ref.6
Mutagenesis2641W → F: 73% loss of cleavage by capsid protease. Ref.11
Mutagenesis7241C → A: Loss of palmitoylation. Ref.8
Mutagenesis744 – 7452CC → AA: Complete loss of infectivity. Ref.10
Mutagenesis7441C → A: Loss of palmitoylation. Ref.10
Mutagenesis7451C → A: Loss of palmitoylation. Ref.10
Mutagenesis786 – 7872CC → SA: Loss of palmitoylation.
Mutagenesis7901C → A: Loss of palmitoylation. Ref.7

Secondary structure

1 .................................................................................................................................................. 1245
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P03316 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: B77C18131703F1E6

FASTA1,245136,766
        10         20         30         40         50         60 
MNRGFFNMLG RRPFPAPTAM WRPRRRRQAA PMPARNGLAS QIQQLTTAVS ALVIGQATRP 

        70         80         90        100        110        120 
QPPRPRPPPR QKKQAPKQPP KPKKPKTQEK KKKQPAKPKP GKRQRMALKL EADRLFDVKN 

       130        140        150        160        170        180 
EDGDVIGHAL AMEGKVMKPL HVKGTIDHPV LSKLKFTKSS AYDMEFAQLP VNMRSEAFTY 

       190        200        210        220        230        240 
TSEHPEGFYN WHHGAVQYSG GRFTIPRGVG GRGDSGRPIM DNSGRVVAIV LGGADEGTRT 

       250        260        270        280        290        300 
ALSVVTWNSK GKTIKTTPEG TEEWSAAPLV TAMCLLGNVS FPCDRPPTCY TREPSRALDI 

       310        320        330        340        350        360 
LEENVNHEAY DTLLNAILRC GSSGRSKRSV IDDFTLTSPY LGTCSYCHHT VPCFSPVKIE 

       370        380        390        400        410        420 
QVWDEADDNT IRIQTSAQFG YDQSGAASAN KYRYMSLKQD HTVKEGTMDD IKISTSGPCR 

       430        440        450        460        470        480 
RLSYKGYFLL AKCPPGDSVT VSIVSSNSAT SCTLARKIKP KFVGREKYDL PPVHGKKIPC 

       490        500        510        520        530        540 
TVYDRLKETT AGYITMHRPR PHAYTSYLEE SSGKVYAKPP SGKNITYECK CGDYKTGTVS 

       550        560        570        580        590        600 
TRTEITGCTA IKQCVAYKSD QTKWVFNSPD LIRHDDHTAQ GKLHLPFKLI PSTCMVPVAH 

       610        620        630        640        650        660 
APNVIHGFKH ISLQLDTDHL TLLTTRRLGA NPEPTTEWIV GKTVRNFTVD RDGLEYIWGN 

       670        680        690        700        710        720 
HEPVRVYAQE SAPGDPHGWP HEIVQHYYHR HPVYTILAVA SATVAMMIGV TVAVLCACKA 

       730        740        750        760        770        780 
RRECLTPYAL APNAVIPTSL ALLCCVRSAN AETFTETMSY LWSNSQPFFW VQLCIPLAAF 

       790        800        810        820        830        840 
IVLMRCCSCC LPFLVVAGAY LAKVDAYEHA TTVPNVPQIP YKALVERAGY APLNLEITVM 

       850        860        870        880        890        900 
SSEVLPSTNQ EYITCKFTTV VPSPKIKCCG SLECQPAAHA DYTCKVFGGV YPFMWGGAQC 

       910        920        930        940        950        960 
FCDSENSQMS EAYVELSADC ASDHAQAIKV HTAAMKVGLR IVYGNTTSFL DVYVNGVTPG 

       970        980        990       1000       1010       1020 
TSKDLKVIAG PISASFTPFD HKVVIHRGLV YNYDFPEYGA MKPGAFGDIQ ATSLTSKDLI 

      1030       1040       1050       1060       1070       1080 
ASTDIRLLKP SAKNVHVPYT QASSGFEMWK NNSGRPLQET APFGCKIAVN PLRAVDCSYG 

      1090       1100       1110       1120       1130       1140 
NIPISIDIPN AAFIRTSDAP LVSTVKCEVS ECTYSADFGG MATLQYVSDR EGQCPVHSHS 

      1150       1160       1170       1180       1190       1200 
STATLQESTV HVLEKGAVTV HFSTASPQAN FIVSLCGKKT TCNAECKPPA DHIVSTPHKN 

      1210       1220       1230       1240 
DQEFQAAISK TSWSWLFALF GGASSLLIIG LMIFACSMML TSTRR

« Hide

References

[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)
+Additional computationally mapped references.

Web resources

Virus Particle ExploreR db

Icosahedral capsid structure

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		V01403 Genomic RNA. Translation: CAA24684.1.
J02363 Genomic RNA. Translation: AAA96976.1.
M13818 Genomic RNA. Translation: AAA47485.1.
AB372876 Genomic RNA. Translation: BAH70330.1.
PIRVHWVB. A03916.
VHWVSB. A25894.
VHWVB2. B03916.
RefSeqNP_062890.1. NC_001547.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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/F329-1186[»]
3MUWelectron microscopy-A/D/E/F807-1190[»]
U/X/Y/Z329-672[»]
ProteinModelPortalP03316.
SMRP03316. Positions 106-264, 691-726, 807-1096, 1101-1189, 1215-1245.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-29032N.

Protein family/group databases

MEROPSS03.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.40.350. 1 hit.
2.60.98.10. 3 hits.
InterProIPR002548. 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]
PfamPF01589. Alpha_E1_glycop. 1 hit.
PF00943. Alpha_E2_glycop. 1 hit.
PF01563. Alpha_E3_glycop. 1 hit.
PF00944. Peptidase_S3. 1 hit.
[Graphical view]
PRINTSPR00798. TOGAVIRIN.
SUPFAMSSF56983. Flavi_glycoprotE. 1 hit.
SSF81296. Ig_E-set. 1 hit.
SSF50494. Pept_Ser_Cys. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP03316.
PMAP-CutDBP03316.

Entry information

Entry namePOLS_SINDV
AccessionPrimary (citable) accession number: P03316
Secondary accession number(s): C4T9C2 expand/collapse secondary AC list , P11259, Q88870, Q88871, Q88872, Q88873, Q88874
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 3, 2013
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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