UniProtKB - P09592 (POLS_EEVVT)
Structural polyprotein
Functioni
Miscellaneous
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 EC:3.4.21.90
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 152 | Charge relay systemPROSITE-ProRule annotation | 1 | |
Active sitei | 174 | Charge relay systemPROSITE-ProRule annotation | 1 | |
Sitei | 200 | Involved in dimerization of the capsid proteinBy similarity | 1 | |
Active sitei | 226 | Charge relay systemPROSITE-ProRule annotation | 1 | |
Sitei | 233 | Involved in dimerization of the capsid proteinBy similarity | 1 |
GO - Molecular functioni
- RNA binding Source: UniProtKB-KW
- serine-type endopeptidase activity Source: InterPro
- structural molecule activity Source: InterPro
GO - Biological processi
- clathrin-dependent endocytosis of virus by host cell Source: UniProtKB-KW
- fusion of virus membrane with host endosome membrane Source: UniProtKB-KW
- suppression by virus of host gene expression Source: UniProtKB-KW
- suppression by virus of host mRNA export from nucleus Source: UniProtKB-KW
- suppression by virus of host transcription Source: UniProtKB
- virion attachment to host cell Source: UniProtKB-KW
Keywordsi
Protein family/group databases
MEROPSi | S03.001 |
Names & Taxonomyi
Protein namesi | Recommended name: Structural polyproteinAlternative name(s): p130 Cleaved into the following 6 chains: Capsid protein (EC:3.4.21.90By similarity) 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 |
Organismi | Venezuelan equine encephalitis virus (strain Trinidad donkey) (VEEV) |
Taxonomic identifieri | 11038 [NCBI] |
Taxonomic lineagei | Viruses › Riboviria › Orthornavirae › Kitrinoviricota › Alsuviricetes › Martellivirales › Togaviridae › Alphavirus › |
Virus hosti | Bos 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 |
|
Subcellular locationi
- Virion By similarity
- Host cytoplasm 2 Publications
- Host cell membrane By similarity
- Host nucleus 2 Publications
- Virion membrane By similarity; Single-pass type I membrane protein Sequence analysis
- Host cell membrane By similarity; Single-pass type I membrane protein By similarity
- Host cell membrane By similarity; Multi-pass membrane protein Sequence analysis
- Virion membrane By similarity; Multi-pass membrane protein Sequence analysis
- Virion membrane By similarity; Single-pass type I membrane protein Sequence analysis
- Host cell membrane By similarity; Single-pass type I membrane protein Sequence analysis
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 276 – 701 | ExtracellularSequence analysisAdd BLAST | 426 | |
Transmembranei | 702 – 722 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 723 – 757 | CytoplasmicSequence analysisAdd BLAST | 35 | |
Topological domaini | 758 – 772 | ExtracellularSequence analysisAdd BLAST | 15 | |
Transmembranei | 773 – 793 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 794 – 795 | CytoplasmicSequence analysis | 2 | |
Transmembranei | 796 – 816 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 817 – 1224 | ExtracellularSequence analysisAdd BLAST | 408 | |
Transmembranei | 1225 – 1245 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 1246 – 1254 | CytoplasmicSequence analysis | 9 |
Keywords - Cellular componenti
Capsid protein, Host cell membrane, Host cytoplasm, Host membrane, Host nucleus, Membrane, T=4 icosahedral capsid protein, Viral envelope protein, VirionPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 48 | L → A: Complete loss of capsid protein nuclear export; when associated with A-50. 1 Publication | 1 | |
Mutagenesisi | 50 | F → A: Complete loss of capsid protein nuclear export; when associated with A-48. 1 Publication | 1 | |
Mutagenesisi | 51 | K → E: Non-cytopathic, incapable of inhibiting host transcription. 1 Publication | 1 | |
Mutagenesisi | 52 | Q → P: Non-cytopathic, incapable of inhibiting host transcription. 1 Publication | 1 | |
Mutagenesisi | 65 | K → A: Complete loss of capsid protein nuclear localization; when associated with A-67. 1 Publication | 1 | |
Mutagenesisi | 67 | K → A: Complete loss of capsid protein nuclear localization; when associated with A-65. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000041276 | 1 – 275 | Capsid proteinAdd BLAST | 275 | |
ChainiPRO_0000234323 | 276 – 757 | Precursor of protein E3/E2Add BLAST | 482 | |
ChainiPRO_0000041277 | 276 – 334 | Assembly protein E3Add BLAST | 59 | |
ChainiPRO_0000041278 | 335 – 757 | Spike glycoprotein E2Add BLAST | 423 | |
ChainiPRO_0000041279 | 758 – 812 | 6K proteinAdd BLAST | 55 | |
ChainiPRO_0000041280 | 813 – 1254 | Spike glycoprotein E1Add BLAST | 442 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 93 | Phosphothreonine1 Publication | 1 | |
Modified residuei | 108 | Phosphothreonine1 Publication | 1 | |
Modified residuei | 124 | Phosphoserine1 Publication | 1 | |
Modified residuei | 127 | Phosphothreonine1 Publication | 1 | |
Glycosylationi | 286 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Glycosylationi | 546 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Glycosylationi | 652 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Lipidationi | 730 | S-palmitoyl cysteine; by hostBy similarity | 1 | |
Lipidationi | 750 | S-palmitoyl cysteine; by hostBy similarity | 1 | |
Lipidationi | 751 | S-palmitoyl cysteine; by hostBy similarity | 1 | |
Disulfide bondi | 861 ↔ 926 | By similarity | ||
Disulfide bondi | 874 ↔ 906 | By similarity | ||
Disulfide bondi | 875 ↔ 908 | By similarity | ||
Disulfide bondi | 880 ↔ 890 | By similarity | ||
Glycosylationi | 946 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Disulfide bondi | 1071 ↔ 1083 | By similarity | ||
Disulfide bondi | 1113 ↔ 1188 | By similarity | ||
Disulfide bondi | 1118 ↔ 1192 | By similarity | ||
Disulfide bondi | 1140 ↔ 1182 | By similarity |
Post-translational modificationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 275 – 276 | Cleavage; by autolysisBy similarity | 2 | |
Sitei | 334 – 335 | Cleavage; by host furinBy similarity | 2 | |
Sitei | 757 – 758 | Cleavage; by host signal peptidaseBy similarity | 2 | |
Sitei | 812 – 813 | Cleavage; by host signal peptidaseBy similarity | 2 |
Keywords - PTMi
Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, PhosphoproteinPTM databases
iPTMneti | P09592 |
Interactioni
Subunit structurei
Part of a tetrameric complex composed of host CRM1, host importin alpha/beta dimer and the viral capsid; this complex blocks the receptor-mediated transport through the nuclear pore (PubMed:20147401).
Interacts with host phosphatase PPP1CA; this interaction dephosphorylates the capsid protein, which increases its ability to bind to the viral genome (PubMed:29769351).
2 PublicationsThe precursor of protein E3/E2 and E1 form a heterodimer shortly after synthesis (By similarity).
By similarityThe precursor of protein E3/E2 and E1 form a heterodimer shortly after synthesis (By similarity). Processing of the precursor of protein E3/E2 into E2 and E3 results in a heterodimer of the spike glycoproteins E2 and E1 (By similarity). 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).
Interacts with 6K protein (By similarity).
By similarityProcessing of the precursor of protein E3/E2 into E2 and E3 results in a heterodimer of the spike glycoproteins E2 and E1 (By similarity). Spike at virion surface are constituted of three E2-E1 heterodimers (By similarity).
Interacts with 6K protein (By similarity).
By similarityInteracts with spike glycoprotein E1 (By similarity).
Interacts with spike glycoprotein E2 (By similarity).
By similarityFamily & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 126 – 275 | Peptidase S3PROSITE-ProRule annotationAdd BLAST | 150 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 33 | Necessary for nucleocapsid assembly and virus assembly1 PublicationAdd BLAST | 33 | |
Regioni | 33 – 68 | Host transcription inhibition1 PublicationAdd BLAST | 36 | |
Regioni | 91 – 127 | Binding to the viral RNABy similarityAdd BLAST | 37 | |
Regioni | 112 – 126 | Ribosome-bindingBy similarityAdd BLAST | 15 | |
Regioni | 276 – 287 | Functions as an uncleaved signal peptide for the precursor of protein E3/E2By similarityAdd BLAST | 12 | |
Regioni | 730 – 750 | Transient transmembrane before p62-6K protein processingSequence analysisAdd BLAST | 21 | |
Regioni | 896 – 913 | E1 fusion peptide loopBy similarityAdd BLAST | 18 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 41 – 48 | Supraphysiological nuclear export signal1 Publication | 8 | |
Motifi | 64 – 68 | Nuclear localization signal1 Publication | 5 |
Domaini
Keywords - Domaini
Transmembrane, Transmembrane helixFamily and domain databases
Gene3Di | 2.40.10.10, 2 hits 2.60.40.2400, 1 hit 2.60.40.3200, 1 hit 2.60.40.350, 1 hit 2.60.98.10, 3 hits 3.30.1490.280, 1 hit |
InterProi | View protein in InterPro IPR002548, Alpha_E1_glycop IPR000936, Alpha_E2_glycop IPR002533, Alpha_E3_glycop IPR042304, Alphavir_E2_A IPR042305, Alphavir_E2_B IPR042306, Alphavir_E2_C IPR000336, Flavivir/Alphavir_Ig-like_sf IPR036253, Glycoprot_cen/dimer_sf IPR038055, Glycoprot_E_dimer_dom IPR014756, Ig_E-set IPR009003, Peptidase_S1_PA IPR043504, Peptidase_S1_PA_chymotrypsin IPR000930, Peptidase_S3 |
Pfami | View 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 |
PRINTSi | PR00798, TOGAVIRIN |
SUPFAMi | SSF50494, SSF50494, 1 hit SSF56983, SSF56983, 1 hit SSF81296, SSF81296, 1 hit |
PROSITEi | View protein in PROSITE PS51690, ALPHAVIRUS_CP, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
10 20 30 40 50
MFPFQPMYPM QPMPYRNPFA APRRPWFPRT DPFLAMQVQE LTRSMANLTF
60 70 80 90 100
KQRRDAPPEG PSAKKPKKEA SQKQKGGGQG KKKKNQGKKK AKTGPPNPKA
110 120 130 140 150
QNGNKKKTNK 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 CAQPPICYDR
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
RYDMHGTIKE IPLHQVSLHT SRPCHIVDGH GYFLLARCPA GDSITMEFKK
460 470 480 490 500
DSVTHSCSVP YEVKFNPVGR ELYTHPPEHG VEQACQVYAH DAQNRGAYVE
510 520 530 540 550
MHLPGSEVDS SLVSLSGSSV TVTPPVGTSA LVECECGGTK ISETINKTKQ
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 IATVSVAAST WLFCRSRVAC LTPYRLTPNA RIPFCLAVLC
760 770 780 790 800
CARTARAETT WESLDHLWNN NQQMFWIQLL IPLAALIVVT RLLRCVCCVV
810 820 830 840 850
PFLVMAGAAA GAYEHATTMP SQAGISYNTI VNRAGYAPLP ISITPTKIKL
860 870 880 890 900
IPTVNLEYVT CHYKTGMDSP AIKCCGSQEC TPTYRPDEQC KVFTGVYPFM
910 920 930 940 950
WGGAYCFCDT ENTQVSKAYV MKSDDCLADH AEAYKAHTAS VQAFLNITVG
960 970 980 990 1000
EHSIVTTVYV NGETPVNFNG VKLTAGPLST AWTPFDRKIV QYAGEIYNYD
1010 1020 1030 1040 1050
FPEYGAGQPG AFGDIQSRTV SSSDLYANTN LVLQRPKAGA IHVPYTQAPS
1060 1070 1080 1090 1100
GFEQWKKDKA PSLKFTAPFG CEIYTNPIRA ENCAVGSIPL AFDIPDALFT
1110 1120 1130 1140 1150
RVSETPTLSA AECTLNECVY SSDFGGIATV KYSASKSGKC AVHVPSGTAT
1160 1170 1180 1190 1200
LKEAAVELTE QGSATIHFST ANIHPEFRLQ ICTSYVTCKG DCHPPKDHIV
1210 1220 1230 1240 1250
THPQYHAQTF TAAVSKTAWT WLTSLLGGSA VIIIIGLVLA TIVAMYVLTN
QKHN
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural varianti | 341 | K → N in strain: Isolate TC-83. | 1 | |
Natural varianti | 419 | H → Y in strain: Isolate TC-83. | 1 | |
Natural varianti | 454 | T → R in strain: Isolate TC-83. | 1 | |
Natural varianti | 526 | V → D in strain: Isolate TC-83. | 1 | |
Natural varianti | 630 | T → I in strain: Isolate TC-83. | 1 | |
Natural varianti | 810 | A → GA in strain: Isolate CoAn5384 and Isolate TC-83. | 1 | |
Natural varianti | 811 | G → P. | 1 | |
Natural varianti | 973 | L → I in strain: Isolate TC-83. | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M14937 Genomic RNA Translation: AAA42997.1 J04332 Genomic RNA Translation: AAB02519.1 L01443 Genomic RNA Translation: AAB02517.1 L01442 Genomic RNA Translation: AAC19322.1 AF004466 Genomic RNA Translation: AAC36382.1 |
PIRi | B31467, VHWVVT |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M14937 Genomic RNA Translation: AAA42997.1 J04332 Genomic RNA Translation: AAB02519.1 L01443 Genomic RNA Translation: AAB02517.1 L01442 Genomic RNA Translation: AAC19322.1 AF004466 Genomic RNA Translation: AAC36382.1 |
PIRi | B31467, VHWVVT |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
3VE6 | X-ray | 2.83 | B | 59-70 | [»] | |
SMRi | P09592 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein family/group databases
MEROPSi | S03.001 |
PTM databases
iPTMneti | P09592 |
Family and domain databases
Gene3Di | 2.40.10.10, 2 hits 2.60.40.2400, 1 hit 2.60.40.3200, 1 hit 2.60.40.350, 1 hit 2.60.98.10, 3 hits 3.30.1490.280, 1 hit |
InterProi | View protein in InterPro IPR002548, Alpha_E1_glycop IPR000936, Alpha_E2_glycop IPR002533, Alpha_E3_glycop IPR042304, Alphavir_E2_A IPR042305, Alphavir_E2_B IPR042306, Alphavir_E2_C IPR000336, Flavivir/Alphavir_Ig-like_sf IPR036253, Glycoprot_cen/dimer_sf IPR038055, Glycoprot_E_dimer_dom IPR014756, Ig_E-set IPR009003, Peptidase_S1_PA IPR043504, Peptidase_S1_PA_chymotrypsin IPR000930, Peptidase_S3 |
Pfami | View 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 |
PRINTSi | PR00798, TOGAVIRIN |
SUPFAMi | SSF50494, SSF50494, 1 hit SSF56983, SSF56983, 1 hit SSF81296, SSF81296, 1 hit |
PROSITEi | View protein in PROSITE PS51690, ALPHAVIRUS_CP, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | POLS_EEVVT | |
Accessioni | P09592Primary (citable) accession number: P09592 Secondary accession number(s): Q66593 Q88695 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 1, 1989 |
Last sequence update: | May 30, 2006 | |
Last modified: | April 7, 2021 | |
This is version 133 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Viral Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structureDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references