Structural polyprotein
Details
- Name
- Structural polyprotein
- Kind
- protein
- Synonyms
- p130
- Gene Name
- Not Available
- UniProtKB Entry
- P03316Swiss-Prot
- Organism
- SINV
- NCBI Taxonomy ID
- 11034
- Amino acid sequence
>lcl|BSEQ0019189|Structural polyprotein MNRGFFNMLGRRPFPAPTAMWRPRRRRQAAPMPARNGLASQIQQLTTAVSALVIGQATRP QPPRPRPPPRQKKQAPKQPPKPKKPKTQEKKKKQPAKPKPGKRQRMALKLEADRLFDVKN EDGDVIGHALAMEGKVMKPLHVKGTIDHPVLSKLKFTKSSAYDMEFAQLPVNMRSEAFTY TSEHPEGFYNWHHGAVQYSGGRFTIPRGVGGRGDSGRPIMDNSGRVVAIVLGGADEGTRT ALSVVTWNSKGKTIKTTPEGTEEWSAAPLVTAMCLLGNVSFPCDRPPTCYTREPSRALDI LEENVNHEAYDTLLNAILRCGSSGRSKRSVIDDFTLTSPYLGTCSYCHHTVPCFSPVKIE QVWDEADDNTIRIQTSAQFGYDQSGAASANKYRYMSLKQDHTVKEGTMDDIKISTSGPCR RLSYKGYFLLAKCPPGDSVTVSIVSSNSATSCTLARKIKPKFVGREKYDLPPVHGKKIPC TVYDRLKETTAGYITMHRPRPHAYTSYLEESSGKVYAKPPSGKNITYECKCGDYKTGTVS TRTEITGCTAIKQCVAYKSDQTKWVFNSPDLIRHDDHTAQGKLHLPFKLIPSTCMVPVAH APNVIHGFKHISLQLDTDHLTLLTTRRLGANPEPTTEWIVGKTVRNFTVDRDGLEYIWGN HEPVRVYAQESAPGDPHGWPHEIVQHYYHRHPVYTILAVASATVAMMIGVTVAVLCACKA RRECLTPYALAPNAVIPTSLALLCCVRSANAETFTETMSYLWSNSQPFFWVQLCIPLAAF IVLMRCCSCCLPFLVVAGAYLAKVDAYEHATTVPNVPQIPYKALVERAGYAPLNLEITVM SSEVLPSTNQEYITCKFTTVVPSPKIKCCGSLECQPAAHADYTCKVFGGVYPFMWGGAQC FCDSENSQMSEAYVELSADCASDHAQAIKVHTAAMKVGLRIVYGNTTSFLDVYVNGVTPG TSKDLKVIAGPISASFTPFDHKVVIHRGLVYNYDFPEYGAMKPGAFGDIQATSLTSKDLI ASTDIRLLKPSAKNVHVPYTQASSGFEMWKNNSGRPLQETAPFGCKIAVNPLRAVDCSYG NIPISIDIPNAAFIRTSDAPLVSTVKCEVSECTYSADFGGMATLQYVSDREGQCPVHSHS STATLQESTVHVLEKGAVTVHFSTASPQANFIVSLCGKKTTCNAECKPPADHIVSTPHKN DQEFQAAISKTSWSWLFALFGGASSLLIIGLMIFACSMMLTSTRR
- Number of residues
- 1245
- Molecular Weight
- 136764.73
- Theoretical pI
- 8.77
- GO Classification
- Functionsserine-type endopeptidase activity / structural molecule activity / ubiquitin-like protein ligase bindingProcessesclathrin-mediated endocytosis of virus by host cell / fusion of virus membrane with host endosome membrane / membrane fusion / virion attachment to host cellComponentshost cell cytoplasm / host cell plasma membrane / icosahedral viral capsid, spike / integral component of membrane / T=4 icosahedral viral capsid / viral envelope / virion membrane
- General Function
- Capsid protein Forms an icosahedral capsid with a T=4 symmetry composed of 240 copies of the capsid protein surrounded by a lipid membrane through which penetrate 80 spikes composed of trimers of E1-E2 heterodimers (PubMed:8415660). The capsid protein binds to the viral RNA genome at a site adjacent to a ribosome binding site for viral genome translation following genome release (By similarity). Possesses a protease activity that results in its autocatalytic cleavage from the nascent structural protein (PubMed:1944569). 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 (By similarity). 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 (PubMed:9143274). In case of infection, new virions attach to target cells and after clathrin-mediated endocytosis their membrane fuses with the host endosomal membrane (By similarity). This leads to the release of the nucleocapsid into the cytoplasm, followed by an uncoating event necessary for the genomic RNA to become accessible (By similarity). The uncoating might be triggered by the interaction of capsid proteins with ribosomes (PubMed:3656418). Binding of ribosomes would release the genomic RNA since the same region is genomic RNA-binding and ribosome-binding (By similarity). Specifically inhibits interleukin-1 receptor-associated kinase 1/IRAK1-dependent signaling during viral entry, representing a means by which the alphaviruses may evade innate immune detection and activation prior to viral gene expression (PubMed:33673546).
- Specific Function
- RNA binding
- Pfam Domain Function
- Signal Regions
- 265-280
- Transmembrane Regions
- 696-712 728-746 768-784 786-802 1216-1234
- Cellular Location
- Virion
- Gene sequence
>lcl|BSEQ0019190|Structural polyprotein ATGAATAGAGGATTCTTTAACATGCTCGGCCGCCGCCCCTTCCCGGCCCCCACTGCCATG TGGAGGCCGCGGAGAAGGAGGCAGGCGGCCCCGATGCCTGCCCGCAACGGGCTGGCTTCT CAAATCCAGCAACTGACCACAGCCGTCAGTGCCCTAGTCATTGGACAGGCAACTAGACCT CAACCCCCACGTCCACGCCCGCCACCGCGCCAGAAGAAGCAGGCGCCCAAGCAACCACCG AAGCCGAAGAAACCAAAAACGCAGGAGAAGAAGAAGAAGCAACCTGCAAAACCCAAACCC GGAAAGAGACAGCGCATGGCACTTAAGTTGGAGGCCGACAGATTGTTCGACGTCAAGAAC GAGGACGGAGATGTCATCGGGCACGCACTGGCCATGGAAGGAAAGGTAATGAAACCTCTG CACGTGAAAGGAACCATCGACCACCCTGTGCTATCAAAGCTCAAATTTACCAAGTCGTCA GCATACGACATGGAGTTCGCACAGTTGCCAGTCAACATGAGAAGTGAGGCATTCACCTAC ACCAGTGAACACCCCGAAGGATTCTATAACTGGCACCACGGAGCGGTGCAGTATAGTGGA GGTAGATTTACCATCCCTCGCGGAGTAGGAGGCAGAGGAGACAGCGGTCGTCCGATCATG GATAACTCCGGTCGGGTTGTCGCGATAGTCCTCGGTGGCGCTGATGAAGGAACACGAACT GCCCTTTCGGTCGTCACCTGGAATAGTAAAGGGAAGACAATTAAGACGACCCCGGAAGGG ACAGAAGAGTGGTCCGCAGCACCACTGGTCACGGCAATGTGTTTGCTCGGAAATGTGAGC TTCCCATGCGACCGCCCGCCCACATGCTATACCCGCGAACCTTCCAGAGCCCTCGACATC CTTGAAGAGAACGTGAACCATGAGGCCTACGATACCCTGCTCAATGCCATATTGCGGTGC GGATCGTCTGGCAGAAGCAAAAGAAGCGTCATTGACGACTTTACCCTGACCAGCCCCTAC TTGGGCACATGCTCGTACTGCCACCATACTGTACCGTGCTTCAGCCCTGTTAAGATCGAG CAGGTCTGGGACGAAGCGGACGATAACACCATACGCATACAGACTTCCGCCCAGTTTGGA TACGACCAAAGCGGAGCAGCAAGCGCAAACAAGTACCGCTACATGTCGCTTAAGCAGGAT CACACCGTTAAAGAAGGCACCATGGATGACATCAAGATTAGCACCTCAGGACCGTGTAGA AGGCTTAGCTACAAAGGATACTTTCTCCTCGCAAAATGCCCTCCAGGGGACAGCGTAACG GTTAGCATAGTGAGTAGCAACTCAGCAACGTCATGTACACTGGCCCGCAAGATAAAACCA AAATTCGTGGGACGGGAAAAATATGATCTACCTCCCGTTCACGGTAAAAAAATTCCTTGC ACAGTGTACGACCGTCTGAAAGAAACAACTGCAGGCTACATCACTATGCACAGGCCGAGA CCGCACGCTTATACATCCTACCTGGAAGAATCATCAGGGAAAGTTTACGCAAAGCCGCCA TCTGGGAAGAACATTACGTATGAGTGCAAGTGCGGCGACTACAAGACCGGAACCGTTTCG ACCCGCACCGAAATCACTGGTTGCACCGCCATCAAGCAGTGCGTCGCCTATAAGAGCGAC CAAACGAAGTGGGTCTTCAACTCACCGGACTTGATCAGACATGACGACCACACGGCCCAA GGGAAATTGCATTTGCCTTTCAAGTTGATCCCGAGTACCTGCATGGTCCCTGTTGCCCAC GCGCCGAATGTAATACATGGCTTTAAACACATCAGCCTCCAATTAGATACAGACCACTTG ACATTGCTCACCACCAGGAGACTAGGGGCAAACCCGGAACCAACCACTGAATGGATCGTC GGAAAGACGGTCAGAAACTTCACCGTCGACCGAGATGGCCTGGAATACATATGGGGAAAT CATGAGCCAGTGAGGGTCTATGCCCAAGAGTCAGCACCAGGAGACCCTCACGGATGGCCA CACGAAATAGTACAGCATTACTACCATCGCCATCCTGTGTACACCATCTTAGCCGTCGCA TCAGCTACCGTGGCGATGATGATTGGCGTAACTGTTGCAGTGTTATGTGCCTGTAAAGCG CGCCGTGAGTGCCTGACGCCATACGCCCTGGCCCCAAACGCCGTAATCCCAACTTCGCTG GCACTCTTGTGCTGCGTTAGGTCGGCCAATGCTGAAACGTTCACCGAGACCATGAGTTAC TTGTGGTCGAACAGTCAGCCGTTCTTCTGGGTCCAGTTGTGCATACCTTTGGCCGCTTTC ATCGTTCTAATGCGCTGCTGCTCCTGCTGCCTGCCTTTTTTAGTGGTTGCCGGCGCCTAC CTGGCGAAGGTAGACGCCTACGAACATGCGACCACTGTTCCAAATGTGCCACAGATACCG TATAAGGCACTTGTTGAAAGGGCAGGGTATGCCCCGCTCAATTTGGAGATCACTGTCATG TCCTCGGAGGTTTTGCCTTCCACCAACCAAGAGTACATTACCTGCAAATTCACCACTGTG GTCCCCTCCCCAAAAATCAAATGCTGCGGCTCCTTGGAATGTCAGCCGGCCGCTCATGCA GACTATACCTGCAAGGTCTTCGGAGGGGTCTACCCCTTTATGTGGGGAGGAGCGCAATGT TTTTGCGACAGTGAGAACAGCCAGATGAGTGAGGCGTACGTCGAATTGTCAGCAGATTGC GCGTCTGACCACGCGCAGGCGATTAAGGTGCACACTGCCGCGATGAAAGTAGGACTGCGT ATTGTGTACGGGAACACTACCAGTTTCCTAGATGTGTACGTGAACGGAGTCACACCAGGA ACGTCTAAAGACTTGAAAGTCATAGCTGGACCAATTTCAGCATCGTTTACGCCATTCGAT CATAAGGTCGTTATCCATCGCGGCCTGGTGTACAACTATGACTTCCCGGAATATGGAGCG ATGAAACCAGGAGCGTTTGGAGACATTCAAGCTACCTCCTTGACTAGCAAGGATCTCATC GCCAGCACAGACATTAGGCTACTCAAGCCTTCCGCCAAGAACGTGCATGTCCCGTACACG CAGGCCTCATCAGGATTTGAGATGTGGAAAAACAACTCAGGCCGCCCACTGCAGGAAACC GCACCTTTCGGGTGTAAGATTGCAGTAAATCCGCTCCGAGCGGTGGACTGTTCATACGGG AACATTCCCATTTCTATTGACATCCCGAACGCTGCCTTTATCAGGACATCAGATGCACCA CTGGTCTCAACAGTCAAATGTGAAGTCAGTGAGTGCACTTATTCAGCAGACTTCGGCGGG ATGGCCACCCTGCAGTATGTATCCGACCGCGAAGGTCAATGCCCCGTACATTCGCATTCG AGCACAGCAACTCTCCAAGAGTCGACAGTACATGTCCTGGAGAAAGGAGCGGTGACAGTA CACTTTAGCACCGCGAGTCCACAGGCGAACTTTATCGTATCGCTGTGTGGGAAGAAGACA ACATGCAATGCAGAATGTAAACCACCAGCTGACCATATCGTGAGCACCCCGCACAAAAAT GACCAAGAATTTCAAGCCGCCATCTCAAAAACATCATGGAGTTGGCTGTTTGCCCTTTTC GGCGGCGCCTCGTCGCTATTAATTATAGGACTTATGATTTTTGCTTGCAGCATGATGCTG ACTAGCACACGAAGATGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P03316 UniProtKB Entry Name POLS_SINDV GenBank Protein ID 62099 GenBank Gene ID V01403 PDB ID(s) 1KXA, 1KXB, 1KXC, 1KXD, 1KXE, 1KXF, 1LD4, 1SVP, 1Z8Y, 2SNV, 2SNW, 3J0F, 3MUU, 3MUW KEGG ID vg:1502155 NCBI Gene ID 1502155 - General References
- Rice CM, Strauss JH: Nucleotide sequence of the 26S mRNA of Sindbis virus and deduced sequence of the encoded virus structural proteins. Proc Natl Acad Sci U S A. 1981 Apr;78(4):2062-6. [Article]
- Strauss EG, Rice CM, Strauss JH: Complete nucleotide sequence of the genomic RNA of Sindbis virus. Virology. 1984 Feb;133(1):92-110. [Article]
- Davis NL, Fuller FJ, Dougherty WG, Olmsted RA, Johnston RE: A single nucleotide change in the E2 glycoprotein gene of Sindbis virus affects penetration rate in cell culture and virulence in neonatal mice. Proc Natl Acad Sci U S A. 1986 Sep;83(18):6771-5. [Article]
- Bell JR, Kinney RM, Trent DW, Strauss EG, Strauss JH: An evolutionary tree relating eight alphaviruses, based on amino-terminal sequences of their glycoproteins. Proc Natl Acad Sci U S A. 1984 Aug;81(15):4702-6. [Article]
- Hahn CS, Strauss JH: Site-directed mutagenesis of the proposed catalytic amino acids of the Sindbis virus capsid protein autoprotease. J Virol. 1990 Jun;64(6):3069-73. [Article]
- Gaedigk-Nitschko K, Ding MX, Levy MA, Schlesinger MJ: Site-directed mutations in the Sindbis virus 6K protein reveal sites for fatty acylation and the underacylated protein affects virus release and virion structure. Virology. 1990 Mar;175(1):282-91. [Article]
- Gaedigk-Nitschko K, Schlesinger MJ: Site-directed mutations in Sindbis virus E2 glycoprotein's cytoplasmic domain and the 6K protein lead to similar defects in virus assembly and budding. Virology. 1991 Jul;183(1):206-14. [Article]
- Liu N, Brown DT: Transient translocation of the cytoplasmic (endo) domain of a type I membrane glycoprotein into cellular membranes. J Cell Biol. 1993 Feb;120(4):877-83. [Article]
- Ivanova L, Schlesinger MJ: Site-directed mutations in the Sindbis virus E2 glycoprotein identify palmitoylation sites and affect virus budding. J Virol. 1993 May;67(5):2546-51. [Article]
- Paredes AM, Heidner H, Thuman-Commike P, Prasad BV, Johnston RE, Chiu W: Structural localization of the E3 glycoprotein in attenuated Sindbis virus mutants. J Virol. 1998 Feb;72(2):1534-41. [Article]
- Smit JM, Bittman R, Wilschut J: Low-pH-dependent fusion of Sindbis virus with receptor-free cholesterol- and sphingolipid-containing liposomes. J Virol. 1999 Oct;73(10):8476-84. [Article]
- DeTulleo L, Kirchhausen T: The clathrin endocytic pathway in viral infection. EMBO J. 1998 Aug 17;17(16):4585-93. [Article]
- Sanz MA, Madan V, Carrasco L, Nieva JL: Interfacial domains in Sindbis virus 6K protein. Detection and functional characterization. J Biol Chem. 2003 Jan 17;278(3):2051-7. Epub 2002 Nov 6. [Article]
- Antoine AF, Montpellier C, Cailliau K, Browaeys-Poly E, Vilain JP, Dubuisson J: The alphavirus 6K protein activates endogenous ionic conductances when expressed in Xenopus oocytes. J Membr Biol. 2007 Jan;215(1):37-48. Epub 2007 May 5. [Article]
- Choi HK, Lee S, Zhang YP, McKinney BR, Wengler G, Rossmann MG, Kuhn RJ: Structural analysis of Sindbis virus capsid mutants involving assembly and catalysis. J Mol Biol. 1996 Sep 20;262(2):151-67. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details 1,4-Dioxane experimental unknown target Details