Structural polyprotein
Details
- Name
- Structural polyprotein
- Synonyms
- p130
- Gene Name
- Not Available
- Organism
- SINV
- 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
- Ubiquitin-like protein ligase binding
- 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.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
- 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 - General References
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