Genome polyprotein
Details
- Name
- Genome polyprotein
- Synonyms
- 3.4.22.29
- P2A
- Gene Name
- Not Available
- Organism
- E-1
- Amino acid sequence
>lcl|BSEQ0017374|Genome polyprotein MGAQVSTQKTGAHETSLSATGNSIIHYTNINYYKDAASNSANRQDFTQDPGKFTEPMKDV MIKTLPALNSPTVEECGYSDRVRSITLGNSTITTQECANVVVGYGEWPEYLSDNEATAED QPTQPDVATCRFYTLDSVQWENGSPGWWWKFPDALRDMGLFGQNMYYHYLGRAGYTIHVQ CNASKFHQGCILVVCVPEAEMGSAQTSGVVNYEHISKGEIASRFTTTTTAEDHGVQAAVW NAGMGVGVGNLTIFPHQWINLRTNNSATIVMPYVNSVPMDNMYRHHNFTLMIIPFVPLDF SAGASTYVPITVTVAPMCAEYNGLRLAGHQGLPTMNTPGSNQFLTSDDFQSPSAMPQFDV TPEMHIPGEVRNLMEIAEVDSVMPINNDSAAKVSSMEAYRVELSTNTNAGTQVFGFQLNP GAESVMNRTLMGEILNYYAHWSGSIKITFVFCGSAMTTGKFLLSYAPPGAGAPKTRKDAM LGTHVVWDVGLQSSCVLCIPWISQTHYRFVEKDPYTNAGFVTCWYQTSVVSPASNQPKCY MMCMVSACNDFSVRMLRDTKFIEQTSFYQGDVQNAVEGAMVRVADTVQTSATNSERVPNL TAVETGHTSQAVPGDTMQTRHVINNHVRSESTIENFLARSACVFYLEYKTGTKEDSNSFN NWVITTRRVAQLRRKLEMFTYLRFDMEITVVITSSQDQSTSQNQNAPVLTHQIMYVPPGG PIPVSVDDYSWQTSTNPSIFWTEGNAPARMSIPFISIGNAYSNFYDGWSHFSQAGVYGFT TLNNMGQLFFRHVNKPNPAAITSVARIYFKPKHVRAWVPRPPRLCPYINSTNVNFEPKPV TEVRTNIITTGAFGQQSGAVYVGNYRVVNRHLATHIDWQNCVWEDYNRDLLVSTTTAHGC DTIARCQCTTGVYFCLSRNKHYPVSFEGPGLVEVQESEYYPKRYQSHVLLAAGFSEPGDC GGILRCEHGVIGIVTMGGEGVVGFADVRDLLWLEDDAMEQGVKDYVEQLGNAFGSGFTNQ ICEQVNLLKESLVGQDSILEKSLKALVKIISALVIVVRNHDDLITVTATLALIGCTSSPW RWLKQKVSQYYGIPMAERQNNGWLKKFTEMTNACKGMEWIAIKIQKFIEWLKVKILPEVK EKHEFLNRLKQLPLLESQIATIEQSAPSQGDQEQLFSNVQYFAHYCRKYAPLYAAEAKRV FSLEKKMSNYIQFKSKCRIEPVCLLLHGSPGAGKSVATNLIGRSLAEKLNSSVYSLPPDP DHFDGYKQQAVVIMDDLCQNPDGKDVSLFCQMVSSVDFVPPMAALEEKGILFTSPFVLAS TNAGSINAPTVSDSRALARRFHFDMNIEVISMYSQNGKINMPMSVKTCDEDCCPVNFKKC CPLVCGKAIQFIDRKTQVRYSLDMLVTEMFREYNHRHSVGATLEALFQGPPVYREIKISV APETPPPPAIADLLKSVDSEAVREYCKEKGWLVPEISSTLQIEKHVSRAFICLQALTTFV SVAGIIYIIYKLFAGFQGAYTGMPNQKPKVPTLRQAKVQGPAFEFAVAMMKRNASTVKTE YGEFTMLGIYDRWAVLPRHAKPGPTILMNDQEVGVLDAKELVDKDGTNLELTLLKLNRNE KFRDIRGFLAREEAEVNEAVLAINTSKFPNMYIPVGQVTDYGFLNLGGTPTKRMLMYNFP TRAGQCGGVLMSTGKVLGIHVGGNGHQGFSAALLRHYFNEEQGEIEFIESSKDAGFPVIN TPSKTKLEPSVFHQVFEGNKEPAVLRNGDPRLKVNFEEAIFSKYIGNVNTHVDEYMQEAV DHYAGQLATLDISTEPMKLEDAVYGTEGLEALDLTTSAGYPYVALGIKKRDILSKKTKDL TKLKECMDKYGLNLPMVTYVKDELRSAEKVAKGKSRLIEASSLNDSVAMRQTFGNLYKTF HLNPGIVTGSAVGCDPDVFWSKIPVMLDGHLIAFDYSGYDASLSPVWFACLKLLLEKLGY TNKETNYIDYLCNSHHLYRDKHYFVRGGMPSGCSGTSIFNSMINNIIIRTLMLKVYKGID LDQFRMIAYGDDVIASYPWPIDASLLAEAGKDYGLIMTPADKGECFNEVTWTNVTFLKRY FRADEQYPFLVHPVMPMKDIHESIRWTKDPKNTQDHVRSLCLLAWHNGEHEYEEFIRKIR SVPVGRCLTLPAFSTLRRKWLDSF
- Number of residues
- 2184
- Molecular Weight
- 244002.735
- Theoretical pI
- 6.72
- GO Classification
- FunctionsATP binding / cysteine-type endopeptidase activity / ion channel activity / RNA binding / RNA helicase activity / RNA-directed RNA polymerase activity / structural molecule activityProcessescaveolin-mediated endocytosis of virus by host cell / DNA replication / induction by virus of host autophagy / pore formation by virus in membrane of host cell / pore-mediated entry of viral genome into host cell / positive stranded viral RNA replication / protein oligomerization / RNA-protein covalent cross-linking / suppression by virus of host gene expression / suppression by virus of host mRNA export from nucleus / suppression by virus of host RIG-I activity by RIG-I proteolysis / suppression by virus of host translation initiation factor activity / transcription, DNA-templated / viral RNA genome replication / virion attachment to host cellComponentshost cell cytoplasmic vesicle membrane / integral to membrane of host cell / membrane / T=pseudo3 icosahedral viral capsid
- General Function
- Structural molecule activity
- Specific Function
- Capsid protein VP1: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Capsid protein VP1 mainly forms the vertices of the capsid. Capsid protein VP1 interacts with host integrin ITGA2/ITGB1 to provide virion attachment to target host cells. This attachment induces virion internalization. Tyrosine kinases are probably involved in the entry process. After binding to its receptor, the capsid undergoes conformational changes. Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized. Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm. After genome has been released, the channel shrinks (By similarity).Capsid protein VP2: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity).Capsid protein VP3: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity).Capsid protein VP4: Lies on the inner surface of the capsid shell. After binding to the host receptor, the capsid undergoes conformational changes. Capsid protein VP4 is released, Capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytoplasm. After genome has been released, the channel shrinks (By similarity).Capsid protein VP0: Component of immature procapsids, which is cleaved into capsid proteins VP4 and VP2 after maturation. Allows the capsid to remain inactive before the maturation step (By similarity).Protein 2A: Cysteine protease that cleaves viral polyprotein and specific host proteins. It is responsible for the cleavage between the P1 and P2 regions, first cleavage occurring in the polyprotein. Cleaves also the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA translation. Inhibits the host nucleus-cytoplasm protein and RNA trafficking by cleaving host members of the nuclear pores (By similarity).Protein 2B: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca2+ in the cytoplasm of infected cell. In turn, high levels of cyctoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (By similarity).Protein 2C: Induces and associates with structural rearrangements of intracellular membranes. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3 (By similarity).Protein 3AB: Localizes the viral replication complex to the surface of membranous vesicles. Together with protein 3CD binds the Cis-Active RNA Element (CRE) which is involved in RNA synthesis initiation. Acts as a cofactor to stimulate the activity of 3D polymerase, maybe through a nucleid acid chaperone activity (By similarity).Protein 3A: Localizes the viral replication complex to the surface of membranous vesicles. It inhibits host cell endoplasmic reticulum-to-Golgi apparatus transport and causes the dissassembly of the Golgi complex, possibly through GBF1 interaction. This would result in depletion of MHC, trail receptors and IFN receptors at the host cell surface (By similarity).Viral protein genome-linked: acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU. The oriI viral genomic sequence may act as a template for this. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome. VPg may be removed in the cytoplasm by an unknown enzyme termed "unlinkase". VPg is not cleaved off virion genomes because replicated genomic RNA are encapsidated at the site of replication (By similarity).Protein 3CD: Is involved in the viral replication complex and viral polypeptide maturation. It exhibits protease activity with a specificity and catalytic efficiency that is different from protease 3C. Protein 3CD lacks polymerase activity. The 3C domain in the context of protein 3CD may have an RNA binding activity (By similarity).Protease 3C: cleaves host DDX58/RIG-I and thus contributes to the inhibition of type I interferon production. Cleaves also host PABPC1 (By similarity).RNA-directed RNA polymerase: Replicates the viral genomic RNA on the surface of intracellular membranes. May form linear arrays of subunits that propagate along a strong head-to-tail interaction called interface-I. Covalently attaches UMP to a tyrosine of VPg, which is used to prime RNA synthesis. The positive stranded RNA genome is first replicated at virus induced membranous vesicles, creating a dsRNA genomic replication form. This dsRNA is then used as template to synthesize positive stranded RNA genomes. ss(+)RNA genomes are either translated, replicated or encapsidated (By similarity).
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Virion
- Gene sequence
>lcl|BSEQ0008045|6555 bp ATGGGAGCACAGGTATCAACACAGAAGACCGGGGCGCACGAGACTAGCTTGAGCGCTACT GGCAACTCCATAATACACTACACGAATATTAATTATTACAAAGATGCAGCCTCTAACTCT GCCAATAGACAAGATTTCACCCAAGACCCTGGTAAGTTTACTGAACCAATGAAAGATGTC ATGATAAAAACCCTGCCAGCGCTGAATTCTCCAACGGTTGAAGAGTGCGGGTACAGTGAC AGGGTCAGGTCAATCACACTTGGGAACTCCACTATTACAACTCAAGAGTGTGCCAATGTG GTGGTGGGGTACGGTGAATGGCCTGAGTATCTGAGTGATAACGAGGCAACTGCTGAGGAC CAACCAACGCAGCCGGACGTGGCCACTTGCCGTTTTTACACCCTAGACTCAGTCCAATGG GAGAATGGGTCACCAGGTTGGTGGTGGAAGTTTCCCGACGCTCTAAGGGATATGGGATTA TTTGGCCAAAATATGTACTACCATTACTTAGGCAGAGCCGGGTATACCATCCACGTACAA TGCAATGCTTCCAAGTTTCATCAAGGCTGTATCCTGGTAGTGTGTGTCCCTGAGGCGGAG ATGGGAAGTGCCCAAACCTCAGGGGTGGTCAACTACGAACACATTAGTAAGGGTGAGATC GCATCAAGGTTCACTACCACGACAACAGCAGAAGACCATGGCGTGCAGGCCGCGGTATGG AATGCTGGTATGGGCGTTGGAGTTGGGAACTTGACGATCTTCCCGCACCAATGGATCAAC CTTCGCACCAACAACAGCGCCACAATTGTTATGCCATACGTAAATAGTGTACCAATGGAC AATATGTATAGACATCACAACTTTACACTAATGATAATACCCTTTGTGCCTCTGGATTTC AGCGCGGGTGCATCCACATACGTGCCCATAACGGTGACAGTGGCCCCCATGTGTGCCGAG TACAATGGACTACGACTAGCTGGACACCAAGGACTACCGACCATGAACACCCCTGGCAGC AACCAATTTCTTACATCGGACGATTTCCAATCCCCGTCAGCGATGCCTCAATTTGATGTA ACTCCAGAAATGCACATCCCTGGTGAGGTGCGCAACCTCATGGAAATTGCCGAAGTTGAT TCTGTAATGCCAATTAACAATGATAGCGCCGCAAAAGTTTCATCCATGGAGGCTTATAGA GTCGAATTGAGCACCAACACTAATGCCGGGACTCAAGTGTTTGGCTTTCAACTGAACCCC GGAGCGGAATCAGTAATGAACCGCACATTAATGGGTGAAATCCTAAATTACTACGCACAC TGGTCAGGAAGCATAAAGATAACATTCGTGTTCTGTGGTTCTGCCATGACCACTGGCAAG TTTCTGCTGTCTTACGCCCCACCAGGTGCAGGTGCGCCAAAAACTCGCAAGGATGCCATG TTAGGCACTCATGTGGTGTGGGATGTTGGGCTCCAATCCAGCTGCGTGTTATGCATCCCC TGGATTAGTCAAACCCATTACAGATTTGTGGAAAAGGATCCATACACCAATGCCGGGTTT GTGACATGTTGGTATCAGACCAGTGTAGTGTCCCCAGCGAGCAACCAGCCAAAGTGTTAT ATGATGTGCATGGTTTCTGCGTGTAATGACTTCTCAGTTCGCATGTTGAGAGATACCAAG TTCATTGAGCAAACATCTTTTTACCAAGGTGATGTGCAGAATGCTGTCGAAGGGGCTATG GTCAGGGTGGCAGATACAGTGCAAACTTCAGCCACAAACTCAGAGAGGGTGCCTAACTTG ACAGCAGTAGAAACTGGTCACACTTCGCAGGCAGTACCTGGTGATACCATGCAGACTAGA CATGTGATCAACAATCACGTGAGGTCAGAATCTACAATTGAGAACTTCCTTGCCAGATCA GCGTGTGTTTTCTACCTAGAGTACAAGACAGGGACCAAAGAGGATTCCAATAGCTTCAAC AATTGGGTGATTACAACCAGGCGAGTGGCTCAACTACGTAGAAAACTGGAAATGTTTACT TACCTACGGTTTGACATGGAAATCACCGTGGTCATTACAAGCTCGCAAGATCAGTCTACA TCACAAAACCAGAATGCACCAGTGCTAACACACCAGATAATGTATGTACCACCAGGGGGA CCCATACCCGTAAGCGTGGATGATTACAGCTGGCAAACATCCACCAACCCCAGTATCTTT TGGACCGAAGGGAACGCTCCGGCACGCATGTCAATTCCATTTATTAGCATAGGCAATGCG TATAGTAATTTCTACGATGGGTGGTCTCACTTCTCCCAGGCTGGCGTGTATGGCTTCACT ACTCTGAACAACATGGGTCAATTGTTCTTCCGGCACGTAAACAAGCCCAACCCAGCCGCT ATTACAAGTGTGGCGCGCATTTACTTCAAACCGAAACATGTACGCGCTTGGGTGCCTAGA CCACCGCGCTTGTGTCCATACATCAATAGCACGAATGTCAACTTTGAACCCAAGCCAGTG ACTGAAGTACGTACCAACATAATAACAACGGGTGCCTTTGGGCAGCAATCTGGCGCAGTG TACGTGGGCAACTACAGAGTGGTCAATAGGCACTTGGCGACTCACATTGATTGGCAAAAC TGTGTATGGGAGGACTATAACAGGGATCTACTGGTCAGCACAACTACAGCTCATGGGTGC GACACCATAGCTAGGTGCCAGTGCACGACAGGGGTGTACTTCTGCCTGAGCAGAAACAAA CACTACCCAGTGTCATTTGAAGGTCCAGGATTGGTTGAGGTTCAAGAGAGTGAGTATTAC CCAAAAAGGTACCAATCCCACGTGCTTCTTGCAGCCGGATTTTCTGAACCTGGAGATTGT GGTGGTATCTTGAGGTGTGAGCATGGTGTTATTGGTATAGTGACCATGGGAGGTGAAGGT GTCGTTGGTTTCGCCGATGTGCGAGACCTTCTATGGCTAGAGGATGACGCCATGGAGCAG GGAGTCAAGGACTACGTGGAACAGCTCGGCAACGCCTTTGGTTCAGGTTTCACCAATCAG ATTTGTGAGCAGGTCAATCTCCTGAAAGAGTCCTTGGTAGGTCAAGACTCCATCTTGGAA AAGTCTTTAAAAGCACTAGTAAAAATCATATCAGCATTAGTGATCGTGGTAAGGAACCAC GACGACTTGATCACAGTGACTGCTACACTAGCCCTCATTGGCTGCACCTCTTCACCATGG CGATGGCTCAAGCAGAAGGTATCACAATATTATGGAATACCCATGGCCGAGCGTCAGAAC AATGGATGGCTCAAGAAATTCACTGAGATGACTAACGCCTGCAAAGGCATGGAGTGGATT GCCATTAAAATTCAGAAATTTATTGAATGGCTGAAAGTTAAGATTCTACCTGAAGTAAAA GAAAAACATGAATTTCTCAATAGATTAAAACAGCTGCCACTTCTTGAAAGTCAGATTGCT ACCATAGAACAGAGCGCACCATCACAAGGTGACCAAGAACAGCTCTTCTCCAATGTGCAG TATTTTGCCCACTATTGCAGAAAGTACGCACCTCTGTATGCCGCCGAAGCAAAAAGAGTG TTCTCGTTGGAGAAAAAGATGAGCAACTACATACAGTTCAAGTCCAAATGCCGTATTGAG CCTGTATGTTTACTTCTCCATGGCAGCCCAGGAGCGGGGAAATCCGTGGCTACAAACCTA ATTGGTAGATCCCTCGCGGAGAAACTTAACAGCTCTGTGTACTCGTTACCACCAGACCCA GATCATTTTGATGGATACAAACAACAAGCCGTAGTGATCATGGATGACCTGTGCCAGAAT CCAGATGGGAAGGATGTGTCACTATTCTGTCAAATGGTATCCAGCGTGGACTTCGTACCA CCCATGGCAGCTCTGGAGGAGAAAGGGATTCTTTTCACGTCCCCGTTTGTGCTAGCATCA ACCAATGCGGGGTCTATCAATGCACCCACTGTGTCTGACAGCAGGGCACTTGCCAGAAGG TTCCACTTTGATATGAACATCGAGGTGATCTCCATGTATAGCCAGAATGGGAAGATTAAC ATGCCCATGTCTGTCAAAACATGTGATGAGGATTGCTGCCCGGTCAATTTCAAGAAATGC TGCCCGCTGGTGTGTGGTAAGGCCATTCAATTTATTGACAGAAAGACCCAAGTTAGGTAT TCACTGGACATGTTGGTCACCGAGATGTTCAGGGAGTACAACCACAGACACAGCGTGGGT GCCACCCTCGAGGCTTTGTTCCAAGGGCCACCGGTCTACAGGGAGATTAAGATCAGTGTC GCTCCAGAAACACCCCCTCCACCAGCAATCGCTGACCTGCTAAAATCAGTAGACAGTGAG GCAGTAAGGGAGTACTGCAAGGAAAAAGGCTGGCTTGTGCCGGAAATTAGCTCCACCCTA CAGATTGAGAAGCACGTCAGTAGAGCATTTATCTGCCTACAGGCTCTGACTACATTTGTC TCAGTAGCTGGCATAATCTACATTATCTACAAATTGTTTGCCGGTTTTCAGGGCGCGTAT ACGGGGATGCCAAATCAGAAACCCAAGGTGCCCACTCTGAGACAGGCTAAGGTGCAGGGC CCGGCATTCGAGTTCGCCGTGGCGATGATGAAGAGAAACGCCAGCACAGTGAAAACAGAA TATGGTGAGTTCACCATGCTCGGCATCTATGACAGATGGGCAGTGTTACCACGCCACGCC AAGCCCGGACCGACCATCTTAATGAATGATCAGGAGGTCGGTGTGCTAGATGCCAAAGAA TTGGTTGACAAAGATGGGACAAATCTGGAGTTGACTCTCCTAAAGCTCAATCGCAATGAG AAGTTTAGGGATATCAGAGGGTTTCTGGCAAGAGAAGAAGCTGAGGTGAATGAGGCTGTT TTGGCAATAAACACAAGCAAGTTCCCCAACATGTACATACCCGTAGGTCAAGTCACCGAC TACGGTTTTCTGAACTTGGGAGGAACGCCCACAAAGAGGATGCTCATGTACAATTTCCCA ACTAGAGCAGGCCAATGTGGCGGTGTCCTCATGTCAACAGGGAAGGTTCTAGGAATACAT GTAGGCGGAAATGGACACCAAGGATTCTCTGCTGCCCTCCTTAGACATTACTTCAATGAG GAACAAGGTGAGATAGAATTCATTGAGAGCTCAAAGGACGCAGGCTTCCCTGTGATCAAC ACCCCCAGCAAAACCAAGCTGGAACCAAGCGTGTTTCACCAGGTGTTTGAGGGCAACAAA GAGCCGGCAGTGCTTAGAAATGGGGATCCACGACTCAAGGTCAACTTTGAGGAGGCAATC TTCTCCAAGTACATTGGCAATGTTAACACCCACGTGGACGAATACATGCAAGAGGCCGTG GACCATTATGCAGGGCAGCTAGCTACACTGGACATCAGCACAGAGCCCATGAAACTGGAG GATGCCGTGTATGGTACAGAGGGGCTGGAAGCACTAGACCTAACCACCAGTGCAGGCTAT CCGTACGTGGCCCTAGGTATCAAGAAAAGAGACATTCTCTCTAAGAAGACCAAAGACCTT ACCAAGTTGAAGGAATGCATGGACAAGTATGGCCTAAACTTACCAATGGTAACTTACGTC AAAGATGAATTAAGATCTGCCGAGAAGGTAGCCAAGGGAAAGTCCAGACTTATTGAGGCC TCCAGTCTCAATGACTCAGTAGCAATGAGGCAAACATTTGGAAACCTGTACAAAACCTTT CATCTCAATCCGGGCATTGTCACGGGCAGTGCTGTTGGGTGTGACCCAGATGTATTTTGG AGTAAGATCCCTGTCATGCTTGATGGACATCTCATAGCTTTTGACTATTCAGGTTATGAC GCCAGTCTCAGCCCGGTGTGGTTTGCATGTCTGAAACTCCTCCTAGAGAAACTAGGGTAT ACGAATAAGGAAACAAACTACATAGATTACCTCTGCAACTCTCACCACTTATATAGGGAC AAGCACTACTTTGTGAGAGGCGGTATGCCATCAGGATGTTCGGGCACTAGCATATTTAAT TCCATGATTAACAACATTATAATCAGGACTCTCATGCTGAAAGTTTATAAAGGCATTGAT TTGGACCAATTCAGAATGATCGCTTATGGGGATGATGTGATTGCCTCCTACCCGTGGCCC ATCGATGCGTCACTGTTAGCTGAAGCAGGAAAAGATTATGGATTGATCATGACCCCAGCA GACAAAGGTGAGTGCTTTAATGAGGTAACCTGGACAAATGTGACCTTTTTGAAAAGGTAC TTCAGAGCAGATGAACAGTACCCATTCCTGGTCCATCCTGTTATGCCAATGAAGGACATA CATGAGTCCATTAGATGGACTAAAGACCCCAAAAACACACAGGATCACGTGCGCTCGCTG TGCCTATTGGCTTGGCACAACGGGGAGCACGAATATGAGGAGTTTATTCGCAAGATCAGA AGCGTGCCCGTCGGGCGCTGCTTGACCCTTCCTGCATTTTCGACACTGCGTAGGAAGTGG TTGGACTCCTTCTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID O91734 UniProtKB Entry Name POLG_EC01F GenBank Protein ID 7408184 GenBank Gene ID AF029859 - General References
- Huttunen P, Santti J, Pulli T, Hyypia T: The major echovirus group is genetically coherent and related to coxsackie B viruses. J Gen Virol. 1996 Apr;77 ( Pt 4):715-25. [Article]
- Oberste MS, Maher K, Kilpatrick DR, Pallansch MA: Molecular evolution of the human enteroviruses: correlation of serotype with VP1 sequence and application to picornavirus classification. J Virol. 1999 Mar;73(3):1941-8. [Article]
- Bergelson JM, St John N, Kawaguchi S, Chan M, Stubdal H, Modlin J, Finberg RW: Infection by echoviruses 1 and 8 depends on the alpha 2 subunit of human VLA-2. J Virol. 1993 Nov;67(11):6847-52. [Article]
- Marjomaki V, Pietiainen V, Matilainen H, Upla P, Ivaska J, Nissinen L, Reunanen H, Huttunen P, Hyypia T, Heino J: Internalization of echovirus 1 in caveolae. J Virol. 2002 Feb;76(4):1856-65. [Article]
- Pietiainen V, Marjomaki V, Upla P, Pelkmans L, Helenius A, Hyypia T: Echovirus 1 endocytosis into caveosomes requires lipid rafts, dynamin II, and signaling events. Mol Biol Cell. 2004 Nov;15(11):4911-25. Epub 2004 Sep 8. [Article]
- Filman DJ, Wien MW, Cunningham JA, Bergelson JM, Hogle JM: Structure determination of echovirus 1. Acta Crystallogr D Biol Crystallogr. 1998 Nov 1;54(Pt 6 Pt 2):1261-72. [Article]