Structural polyprotein
Details
- Name
- Structural polyprotein
- Synonyms
- p130
- Gene Name
- Not Available
- Organism
- VEEV
- Amino acid sequence
>lcl|BSEQ0020571|Structural polyprotein MFPFQPMYPMQPMPYRNPFAAPRRPWFPRTDPFLAMQVQELTRSMANLTFKQRRDAPPEG PSAKKPKKEASQKQKGGGQGKKKKNQGKKKAKTGPPNPKAQNGNKKKTNKKPGKRQRMVM KLESDKTFPIMLEGKINGYACVVGGKLFRPMHVEGKIDNDVLAALKTKKASKYDLEYADV PQNMRADTFKYTHEKPQGYYSWHHGAVQYENGRFTVPKGVGAKGDSGRPILDNQGRVVAI VLGGVNEGSRTALSVVMWNEKGVTVKYTPENCEQWSLVTTMCLLANVTFPCAQPPICYDR KPAETLAMLSVNVDNPGYDELLEAAVKCPGRKRRSTEELFKEYKLTRPYMARCIRCAVGS CHSPIAIEAVKSDGHDGYVRLQTSSQYGLDSSGNLKGRTMRYDMHGTIKEIPLHQVSLHT SRPCHIVDGHGYFLLARCPAGDSITMEFKKDSVTHSCSVPYEVKFNPVGRELYTHPPEHG VEQACQVYAHDAQNRGAYVEMHLPGSEVDSSLVSLSGSSVTVTPPVGTSALVECECGGTK ISETINKTKQFSQCTKKEQCRAYRLQNDKWVYNSDKLPKAAGATLKGKLHVPFLLADGKC TVPLAPEPMITFGFRSVSLKLHPKNPTYLTTRQLADEPHYTHELISEPAVRNFTVTEKGW EFVWGNHPPKRFWAQETAPGNPHGLPHEVITHYYHRYPMSTILGLSICAAIATVSVAAST WLFCRSRVACLTPYRLTPNARIPFCLAVLCCARTARAETTWESLDHLWNNNQQMFWIQLL IPLAALIVVTRLLRCVCCVVPFLVMAGAAAGAYEHATTMPSQAGISYNTIVNRAGYAPLP ISITPTKIKLIPTVNLEYVTCHYKTGMDSPAIKCCGSQECTPTYRPDEQCKVFTGVYPFM WGGAYCFCDTENTQVSKAYVMKSDDCLADHAEAYKAHTASVQAFLNITVGEHSIVTTVYV NGETPVNFNGVKLTAGPLSTAWTPFDRKIVQYAGEIYNYDFPEYGAGQPGAFGDIQSRTV SSSDLYANTNLVLQRPKAGAIHVPYTQAPSGFEQWKKDKAPSLKFTAPFGCEIYTNPIRA ENCAVGSIPLAFDIPDALFTRVSETPTLSAAECTLNECVYSSDFGGIATVKYSASKSGKC AVHVPSGTATLKEAAVELTEQGSATIHFSTANIHPEFRLQICTSYVTCKGDCHPPKDHIV THPQYHAQTFTAAVSKTAWTWLTSLLGGSAVIIIIGLVLATIVAMYVLTNQKHN
- Number of residues
- 1254
- Molecular Weight
- 138349.755
- Theoretical pI
- 8.82
- GO Classification
- Functionsserine-type endopeptidase activity / structural molecule activityProcessesclathrin-mediated endocytosis of virus by host cell / fusion of virus membrane with host endosome membrane / virion attachment to host cellComponentshost cell cytoplasm / host cell plasma membrane / integral component of membrane / T=4 icosahedral viral capsid / viral envelope / virion membrane
- General Function
- Structural molecule activity
- Specific 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).E3 protein's function is unknown.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).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 (By similarity).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).
- Pfam Domain Function
- Transmembrane Regions
- 702-722 773-793 796-816 1225-1245
- Cellular Location
- Virion
- Gene sequence
>lcl|BSEQ0003943|3765 bp ATGTTCCCGTTCCAGCCAATGTATCCGATGCAGCCAATGCCCTATCGCAACCCGTTCGCG GCCCCGCGCAGGCCCTGGTTCCCCAGAACCGACCCTTTTCTGGCGATGCAGGTGCAGGAA TTAACCCGCTCGATGGCTAACCTGACGTTCAAGCAACGCCGGGACGCGCCACCTGAGGGG CCATCCGCTAAGAAACCGAAGAAGGAGGCCTCGCAAAAACAGAAAGGGGGAGGCCAAGGG AAGAAGAAGAAGAACCAAGGGAAGAAGAAGGCTAAGACAGGGCCGCCTAATCCGAAGGCA CAGAATGGAAACAAGAAGAAGACCAACAAGAAACCAGGCAAGAGACAGCGCATGGTCATG AAATTGGAATCTGACAAGACGTTCCCAATCATGTTGGAAGGGAAGATAAACGGCTACGCT TGTGTGGTCGGAGGGAAGTTATTCAGGCCGATGCATGTGGAAGGCAAGATCGACAACGAC GTTCTGGCCGCGCTTAAGACGAAGAAAGCATCCAAATACGATCTTGAGTATGCAGATGTG CCACAGAACATGCGGGCCGATACATTCAAATACACCCATGAGAAACCCCAAGGCTATTAC AGCTGGCATCATGGAGCAGTCCAATATGAAAATGGGCGTTTCACGGTGCCGAAAGGAGTT GGGGCCAAGGGAGACAGCGGACGACCCATTCTGGATAACCAGGGACGGGTGGTCGCTATT GTGCTGGGAGGTGTGAATGAAGGATCTAGGACAGCCCTTTCAGTCGTCATGTGGAACGAG AAGGGAGTTACCGTGAAGTATACTCCGGAGAACTGCGAGCAATGGTCACTAGTGACCACC ATGTGTCTGCTCGCCAATGTGACGTTCCCATGTGCTCAACCACCAATTTGCTACGACAGA AAACCAGCAGAGACTTTGGCCATGCTCAGCGTTAACGTTGACAACCCGGGCTACGATGAG CTGCTGGAAGCAGCTGTTAAGTGCCCCGGAAGGAAAAGGAGATCCACCGAGGAGCTGTTT AAGGAGTATAAGCTAACGCGCCCTTACATGGCCAGATGCATCAGATGTGCAGTTGGGAGC TGCCATAGTCCAATAGCAATCGAGGCAGTAAAGAGCGACGGGCACGACGGTTATGTTAGA CTTCAGACTTCCTCGCAGTATGGCCTGGATTCCTCCGGCAACTTAAAGGGCAGGACCATG CGGTATGACATGCACGGGACCATTAAAGAGATACCACTACATCAAGTGTCACTCCATACA TCTCGCCCGTGTCACATTGTGGATGGGCACGGTTATTTCCTGCTTGCCAGGTGCCCGGCA GGGGACTCCATCACCATGGAATTTAAGAAAGATTCCGTCACACACTCCTGCTCGGTGCCG TATGAAGTGAAATTTAATCCTGTAGGCAGAGAACTCTATACTCATCCCCCAGAACACGGA GTAGAGCAAGCGTGCCAAGTCTACGCACATGATGCACAGAACAGAGGAGCTTATGTCGAG ATGCACCTCCCGGGCTCAGAAGTGGACAGCAGTTTGGTTTCCTTGAGCGGCAGTTCAGTC ACCGTGACACCTCCTGTTGGGACTAGCGCCCTGGTGGAATGCGAGTGTGGCGGCACAAAG ATCTCCGAGACCATCAACAAGACAAAACAGTTCAGCCAGTGCACAAAGAAGGAGCAGTGC AGAGCATATCGGCTGCAGAACGATAAGTGGGTGTATAATTCTGACAAACTGCCCAAAGCA GCGGGAGCCACCTTAAAAGGAAAACTGCATGTCCCATTCTTGCTGGCAGACGGCAAATGC ACCGTGCCTCTAGCACCAGAACCTATGATAACCTTTGGTTTCAGATCAGTGTCACTGAAA CTGCACCCTAAGAATCCCACATATCTAACCACCCGCCAACTTGCTGATGAGCCTCACTAC ACGCACGAGCTCATATCTGAACCAGCTGTTAGGAATTTTACCGTCACCGAAAAAGGGTGG GAGTTTGTATGGGGAAACCACCCGCCGAAAAGGTTTTGGGCACAGGAAACAGCACCCGGA AATCCACATGGGCTACCGCACGAGGTGATAACTCATTATTACCACAGATACCCTATGTCC ACCATCCTGGGTTTGTCAATTTGTGCCGCCATTGCAACCGTTTCCGTTGCAGCGTCTACC TGGCTGTTTTGCAGATCTAGAGTTGCGTGCCTAACTCCTTACCGGCTAACACCTAACGCT AGGATACCATTTTGTCTGGCTGTGCTTTGCTGCGCCCGCACTGCCCGGGCCGAGACCACC TGGGAGTCCTTGGATCACCTATGGAACAATAACCAACAGATGTTCTGGATTCAATTGCTG ATCCCTCTGGCCGCCTTGATCGTAGTGACTCGCCTGCTCAGGTGCGTGTGCTGTGTCGTG CCTTTTTTAGTCATGGCCGGCGCCGCAGCGCCGGCCTACGAGCACGCGACCACGATGCCG AGCCAAGCGGGAATCTCGTATAACACTATAGTCAACAGAGCAGGCTACGCACCACTCCCT ATCAGCATAACACCAACAAAGATCAAGCTGATACCTACAGTGAACTTGGAGTACGTCACC TGCCACTACAAAACAGGAATGGATTCACCAGCCATCAAATGCTGCGGATCTCAGGAATGC ACTCCAACTTACAGGCCTGATGAACAGTGCAAAGTCTTCACAGGGGTTTACCCGTTCATG TGGGGTGGTGCATATTGCTTTTGCGACACTGAGAACACCCAAGTCAGCAAGGCCTACGTA ATGAAATCTGACGACTGCCTTGCGGATCATGCTGAAGCATATAAAGCGCACACAGCCTCA GTGCAGGCGTTCCTCAACATCACAGTGGGAGAACACTCTATTGTGACTACCGTGTATGTG AATGGAGAAACTCCTGTGAATTTCAATGGGGTCAAATTAACTGCAGGTCCGCTTTCCACA GCTTGGACACCCTTTGATCGCAAAATCGTGCAGTATGCCGGGGAGATCTATAATTATGAT TTTCCTGAGTATGGGGCAGGACAACCAGGAGCATTTGGAGATATACAATCCAGAACAGTC TCAAGCTCAGATCTGTATGCCAATACCAACCTAGTGCTGCAGAGACCCAAAGCAGGAGCG ATCCACGTGCCATACACTCAGGCACCTTCGGGTTTTGAGCAATGGAAGAAAGATAAAGCT CCATCATTGAAATTTACCGCCCCTTTCGGATGCGAAATATATACAAACCCCATTCGCGCC GAAAACTGTGCTGTAGGGTCAATTCCATTAGCCTTTGACATTCCCGACGCCTTGTTCACC AGGGTGTCAGAAACACCGACACTTTCAGCGGCCGAATGCACTCTTAACGAGTGCGTGTAT TCTTCCGACTTTGGTGGGATCGCCACGGTCAAGTACTCGGCCAGCAAGTCAGGCAAGTGC GCAGTCCATGTGCCATCAGGGACTGCTACCCTAAAAGAAGCAGCAGTCGAGCTAACCGAG CAAGGGTCGGCGACTATCCATTTCTCGACCGCAAATATCCACCCGGAGTTCAGGCTCCAA ATATGCACATCATATGTTACGTGCAAAGGTGATTGTCACCCCCCGAAAGACCATATTGTG ACACACCCTCAGTATCACGCCCAAACATTTACAGCCGCGGTGTCAAAAACCGCGTGGACG TGGTTAACATCCCTGCTGGGAGGATCAGCCGTAATTATTATAATTGGCTTGGTGCTGGCT ACTATTGTGGCCATGTACGTGCTGACCAACCAGAAACATAATTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P09592 UniProtKB Entry Name POLS_EEVVT GenBank Protein ID 323726 GenBank Gene ID M14937 - General References
- Kinney RM, Johnson BJ, Brown VL, Trent DW: Nucleotide sequence of the 26 S mRNA of the virulent Trinidad donkey strain of Venezuelan equine encephalitis virus and deduced sequence of the encoded structural proteins. Virology. 1986 Jul 30;152(2):400-13. [Article]
- Kinney RM, Johnson BJ, Welch JB, Tsuchiya KR, Trent DW: The full-length nucleotide sequences of the virulent Trinidad donkey strain of Venezuelan equine encephalitis virus and its attenuated vaccine derivative, strain TC-83. Virology. 1989 May;170(1):19-30. [Article]
- Johnson BJ, Kinney RM, Kost CL, Trent DW: Molecular determinants of alphavirus neurovirulence: nucleotide and deduced protein sequence changes during attenuation of Venezuelan equine encephalitis virus. J Gen Virol. 1986 Sep;67 ( Pt 9):1951-60. [Article]
- Powers AM, Oberste MS, Brault AC, Rico-Hesse R, Schmura SM, Smith JF, Kang W, Sweeney WP, Weaver SC: Repeated emergence of epidemic/epizootic Venezuelan equine encephalitis from a single genotype of enzootic subtype ID virus. J Virol. 1997 Sep;71(9):6697-705. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details