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Protein

Structural polyprotein

Gene
N/A
Organism
Venezuelan equine encephalitis virus (strain P676) (VEEV)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

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 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.By similarity
Assembly protein E3: Provides the signal sequence for the translocation of the precursor of protein E3/E2 to the host endoplasmic reticulum. Mediates pH protection of spike glycoprotein E1 during the transport via the secretory pathway.By similarity
Spike glycoprotein E2: Plays a role in 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
6K protein: Constitutive membrane protein involved in virus glycoprotein processing, cell permeabilization, and the budding of viral particles. Disrupts the calcium homeostasis of the cell, probably at the endoplasmic reticulum level. This leads to cytoplasmic calcium elevation. Because of its lipophilic properties, the 6K protein is postulated to influence the selection of lipids that interact with the transmembrane domains of the glycoproteins, which, in turn, affects the deformability of the bilayer required for the extreme curvature that occurs as budding proceeds. Present in low amount in virions, about 3% compared to viral glycoproteins.By similarity
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. Fusion is optimal at levels of about 1 molecule of cholesterol per 2 molecules of phospholipids, and is specific for sterols containing a 3-beta-hydroxyl group.By similarity

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.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei152Charge relay systemPROSITE-ProRule annotation1
Active sitei174Charge relay systemPROSITE-ProRule annotation1
Active sitei226Charge relay systemPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

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

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
OrganismiVenezuelan equine encephalitis virus (strain P676) (VEEV)
Taxonomic identifieri36385 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageTogaviridaeAlphavirus
Virus hostiBos taurus (Bovine) [TaxID: 9913]
Didelphis marsupialis (Southern opossum) [TaxID: 9268]
Equus asinus (Donkey) (Equus africanus asinus) [TaxID: 9793]
Equus caballus (Horse) [TaxID: 9796]
Homo sapiens (Human) [TaxID: 9606]
Melanoconion [TaxID: 53535]
Philander opossum (Gray four-eyed opossum) [TaxID: 9272]
Proechimys [TaxID: 10162]
Sigmodon hispidus (Hispid cotton rat) [TaxID: 42415]
Proteomesi
  • UP000008658 Componenti: Genome

Subcellular locationi

Capsid protein :
Spike glycoprotein E2 :
6K protein :
Spike glycoprotein E1 :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini276 – 701ExtracellularSequence analysisAdd BLAST426
Transmembranei702 – 722HelicalSequence analysisAdd BLAST21
Topological domaini723 – 757CytoplasmicSequence analysisAdd BLAST35
Topological domaini758 – 769ExtracellularSequence analysisAdd BLAST12
Transmembranei770 – 790HelicalSequence analysisAdd BLAST21
Topological domaini791CytoplasmicSequence analysis1
Transmembranei792 – 812HelicalSequence analysisAdd BLAST21
Topological domaini813 – 1225ExtracellularSequence analysisAdd BLAST413
Transmembranei1226 – 1246HelicalSequence analysisAdd BLAST21
Topological domaini1247 – 1255CytoplasmicSequence analysis9

GO - Cellular componenti

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000412711 – 275Capsid proteinAdd BLAST275
ChainiPRO_0000234322276 – 757Precursor of protein E3/E2Add BLAST482
ChainiPRO_0000041272276 – 334Assembly protein E3Add BLAST59
ChainiPRO_0000041273335 – 757Spike glycoprotein E2Add BLAST423
ChainiPRO_0000041274758 – 8136K proteinAdd BLAST56
ChainiPRO_0000041275814 – 1255Spike glycoprotein E1Add BLAST442

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi286N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi652N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Lipidationi730S-palmitoyl cysteine; by hostBy similarity1
Lipidationi750S-palmitoyl cysteine; by hostBy similarity1
Lipidationi751S-palmitoyl cysteine; by hostBy similarity1
Disulfide bondi862 ↔ 927By similarity
Disulfide bondi875 ↔ 907By similarity
Disulfide bondi876 ↔ 909By similarity
Disulfide bondi881 ↔ 891By similarity
Glycosylationi947N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi1072 ↔ 1084By similarity
Disulfide bondi1114 ↔ 1189By similarity
Disulfide bondi1119 ↔ 1193By similarity
Disulfide bondi1141 ↔ 1183By similarity

Post-translational modificationi

Structural polyprotein: Specific enzymatic cleavages in vivo yield mature proteins. Capsid protein is auto-cleaved during polyprotein translation, unmasking a signal peptide at the N-terminus of the precursor of E3/E2. The remaining polyprotein is then targeted to the host endoplasmic reticulum, where host signal peptidase cleaves it into pE2, 6K and E1 proteins. pE2 is further processed to mature E3 and E2 by host furin in trans-Golgi vesicle.By similarity
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.By similarity
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
Sitei275 – 276Cleavage; by autolysisBy similarity2
Sitei334 – 335Cleavage; by host furinBy similarity2
Sitei757 – 758Cleavage; by host signal peptidaseBy similarity2
Sitei813 – 814Cleavage; by host signal peptidaseBy similarity2

Keywords - PTMi

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

Proteomic databases

PRIDEiP36332

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliP36332
SMRiP36332
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini126 – 275Peptidase S3PROSITE-ProRule annotationAdd BLAST150

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni99 – 113Ribosome-bindingBy similarityAdd BLAST15
Regioni276 – 287Functions as an uncleaved signal peptide for the precursor of protein E3/E2By similarityAdd BLAST12
Regioni730 – 750Transient transmembrane before p62-6K protein processingSequence analysisAdd BLAST21
Regioni897 – 914E1 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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

KOiK19288
OrthoDBiVOG09000271

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

Sequencei

Sequence statusi: Complete.

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

P36332-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFPFQPMYPM QPMPYRNPFA APRRPWFPRT DPFLAMQVQE LTRSMANLTF
60 70 80 90 100
KQRRDAPPEG PPAKKPKREA PQKQKGGGQG KKKKNQGKKK AKTGPPNPKA
110 120 130 140 150
QSGNKKKPNK KPGKRQRMVM KLESDKTFPI MLEGKINGYA CVVGGKLFRP
160 170 180 190 200
MHVEGKIDND VLAALKTKKA SKYDLEYADV PQNMRADTFK YTHEKPQGYY
210 220 230 240 250
SWHHGAVQYE NGRFTVPKGV GAKGDSGRPI LDNQGRVVAI VLGGVNEGSR
260 270 280 290 300
TALSVVMWNE KGVTVKYTPE NCEQWSLVTT MCLLANVTFP CAEPPICYDR
310 320 330 340 350
KPAETLAMLS VNVDNPGYDE LLEAAVKCPG RKRRSTEELF KEYKLTRPYM
360 370 380 390 400
ARCIRCAVGS CHSPIAIEAV KSDGHDGYVR LQTSSQYGLD SSGNLKGRTM
410 420 430 440 450
RYDMHGTIEE IPLHQVSLHT SRPCHIVDGH GYFLLARCPA GDSITMEFKK
460 470 480 490 500
GSVTHSCSVP YEVKFNPVGR ELYTHPPEHG AEQACQVYAH DAQNRGAYVE
510 520 530 540 550
MHLPGSEVDS SLISLSGSSV TVTPPVGTSA LVKCKCGGTK ISETINKAKQ
560 570 580 590 600
FSQCTKKEQC RAYRLQNDKW VYNSDKLPKA AGATLKGKLH VPFLLADGKC
610 620 630 640 650
TVPLAPEPMI TFGFRSVSLK LHPKNPTYLT TRQLADEPHY THELISEPAV
660 670 680 690 700
RNFTVTEKGW EFVWGNHPPK RFWAQETAPG NPHGLPHEVI THYYHRYPMS
710 720 730 740 750
TILGLSICAA IVTVSVAAST WLFCKSRVSC LTPYRLTPNA RMPLCLAVLC
760 770 780 790 800
CARTARAETT WESLDHLWNN NQQMFWIQLL IPLAALIVVT RLLKCVCCVV
810 820 830 840 850
PFLVVAGAAG AGAYEHATTM PSQAGISYNT IVNRAGYAPL PISITPTKIK
860 870 880 890 900
LIPTVNLEYV TCHYKTGMDS PAIKCCGSQE CTPTNRPDEQ CKVFTGVYPF
910 920 930 940 950
MWGGAYCFCD TENTQVSKAY VMKSDDCLAD HAEAYKAHTA SVQAFLNITV
960 970 980 990 1000
GEHSIVTTVY VNGETPVNFN GVKLTAGPLS TAWTPFDRKI VQYAGEIYNY
1010 1020 1030 1040 1050
DFPEYGAGQP GAFGDIQSRT VSSSDLYANT NLVLQRPKAG AIHVPYTQAP
1060 1070 1080 1090 1100
SGFEQWKKDK APSLKFTAPF GCEIYTNPIR AENCAVGSIP LAFDIPDALF
1110 1120 1130 1140 1150
TRVSETPTLS AAECTLNECV YSSDFGGIAT VKYSASKSGK CAVHVPSGTA
1160 1170 1180 1190 1200
TLKEAAVELT EQGSATIHFS TANIHPEFRL QICTSYVTCK GDCHPPKDHI
1210 1220 1230 1240 1250
VTHPQYHAQT FTAAVSKTAW TWLTSLLGGS AVIIIIGLVL ATIVAMYVLT

NQKHN
Length:1,255
Mass (Da):138,214
Last modified:June 1, 1994 - v1
Checksum:i33CD302F5CAE8646
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04653 Genomic RNA Translation: AAC19319.1
PIRiB44213
RefSeqiNP_040824.1, NC_001449.1

Genome annotation databases

GeneIDi2652924
KEGGivg:2652924

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04653 Genomic RNA Translation: AAC19319.1
PIRiB44213
RefSeqiNP_040824.1, NC_001449.1

3D structure databases

ProteinModelPortaliP36332
SMRiP36332
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP36332

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2652924
KEGGivg:2652924

Phylogenomic databases

KOiK19288
OrthoDBiVOG09000271

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
ProtoNetiSearch...

Entry informationi

Entry nameiPOLS_EEVVP
AccessioniPrimary (citable) accession number: P36332
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: May 23, 2018
This is version 117 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

Complete proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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